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Conserved domains on  [gi|2119559688|gb|KAH3719227|]
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hypothetical protein DPMN_062059, partial [Dreissena polymorpha]

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 ...
59-296 3.34e-152

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: 444.68  E-value: 3.34e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIG 138
Cdd:cd03249     1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKI 218
Cdd:cd03249    81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 219 LLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVTLQ 296
Cdd:cd03249   161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
361-677 2.76e-147

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: 435.34  E-value: 2.76e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 361 LKLNKSEAPFIVMGCFASLVNGGAMPAFAVIFSEILGVFAILDEGEQERKIIQYVLMFVGVGVISLIAYFVQGYMFGRSG 440
Cdd:cd18578     1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 441 EYLTLRLRSMSFKAMLRQEIAFFDDHNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLV 520
Cdd:cd18578    81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 521 IAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIG 600
Cdd:cd18578   161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 601 FSLSQAVMFFAYAASFWLGAYLIKQSEVDYVDVFKAFSAILFGGMAIGNASAFAPDAAKAEQSAKEIFKLIDKKPDI 677
Cdd:cd18578   241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
696-822 5.44e-68

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd03249:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 238  Bit Score: 225.11  E-value: 5.44e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 696 FANIIFRYPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIV 775
Cdd:cd03249     3 FKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLV 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2119559688 776 SQEPVLFDRTIAENIAYGDNSRevTMDEIIDAARKANIHNFIASLPD 822
Cdd:cd03249    83 SQEPVLFDGTIAENIRYGKPDA--TDEEVEEAAKKANIHDFIMSLPD 127
ABC_6TM_exporters super family cl38913
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
1-32 4.42e-07

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 cd18577:

Pssm-ID: 365789 [Multi-domain]  Cd Length: 300  Bit Score: 52.48  E-value: 4.42e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2119559688   1 VFFSVMIGAFSLGNAMPHLQTLATARGAAYYL 32
Cdd:cd18577   269 VFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
 
Name Accession Description Interval E-value
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
59-296 3.34e-152

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: 444.68  E-value: 3.34e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIG 138
Cdd:cd03249     1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKI 218
Cdd:cd03249    81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 219 LLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVTLQ 296
Cdd:cd03249   161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
361-677 2.76e-147

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: 435.34  E-value: 2.76e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 361 LKLNKSEAPFIVMGCFASLVNGGAMPAFAVIFSEILGVFAILDEGEQERKIIQYVLMFVGVGVISLIAYFVQGYMFGRSG 440
Cdd:cd18578     1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 441 EYLTLRLRSMSFKAMLRQEIAFFDDHNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLV 520
Cdd:cd18578    81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 521 IAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIG 600
Cdd:cd18578   161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 601 FSLSQAVMFFAYAASFWLGAYLIKQSEVDYVDVFKAFSAILFGGMAIGNASAFAPDAAKAEQSAKEIFKLIDKKPDI 677
Cdd:cd18578   241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
19-300 1.68e-133

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 409.55  E-value: 1.68e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  19 LQTLATARGAAYYLYQLITMDPPIDSySTEGKKLDNFQGNVQIRGVHFRYPsrPEAKILYGVNLQIKRGQTVALVGSSGC 98
Cdd:COG1132   301 LNQLQRALASAERIFELLDEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGS 377
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  99 GKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHD 178
Cdd:COG1132   378 GKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHE 457
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 179 FIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLST 258
Cdd:COG1132   458 FIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLST 537
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2119559688 259 IKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVTLQSMKS 300
Cdd:COG1132   538 IRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFGEE 579
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
1-822 1.76e-114

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 380.14  E-value: 1.76e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688    1 VFFSVMIGAFSLGNAMPHLQTLATARGAAYYLYQLITMDPPIDSySTEGKKLDNFQgNVQIRGVHFRYPSRPEAKILYGV 80
Cdd:PTZ00265   327 ILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVEN-NDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDL 404
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   81 NLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILI-DGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRY-- 157
Cdd:PTZ00265   405 NFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYsl 484
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  158 ------------------------------------------------GHLDVTKE-------DIEQAAKMANAHDFIMD 182
Cdd:PTZ00265   485 yslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsnELIEMRKNyqtikdsEVVDVSKKVLIHDFVSA 564
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  183 LPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALE--KASHGRTTIVIAHRLSTIK 260
Cdd:PTZ00265   565 LPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIR 644
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  261 TADMI------------------------------------AGFKD-----------GVVAEQGTHNELM-SKQGIYQQL 292
Cdd:PTZ00265   645 YANTIfvlsnrergstvdvdiigedptkdnkennnknnkddNNNNNnnnnnkinnagSYIIEQGTHDALMkNKNGIYYTM 724
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  293 VTLQSMKSADDNEIEDFNRDDTKRPSLRHQKSTIDmtPKKLAQDKKEEIKEEEKGEKEEEVDAS------------LGRI 360
Cdd:PTZ00265   725 INNQKVSSKKSSNNDNDKDSDMKSSAYKDSERGYD--PDEMNGNSKHENESASNKKSCKMSDENasennaggklpfLRNL 802
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  361 LKlNKSEAPF---------------IVMGCFASLVNGGAMPAFAVIFSEILGvfAILDEGEQERKIIQYVLMFVGVGVIS 425
Cdd:PTZ00265   803 FK-RKPKAPNnlrivyreifsykkdVTIIALSILVAGGLYPVFALLYAKYVS--TLFDFANLEANSNKYSLYILVIAIAM 879
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  426 LIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDHNNSVGALTTRLATDASQVQGA-----------AGIKLGS 494
Cdd:PTZ00265   880 FISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGlvnnivifthfIVLFLVS 959
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  495 SLMA--FCSVVTGIVIGFVFswkITLLVIAFLPFVMIGGALEMQMMQGAAG-----KNKEALESAGKIAIESIENIRTVA 567
Cdd:PTZ00265   960 MVMSfyFCPIVAAVLTGTYF---IFMRVFAIRARLTANKDVEKKEINQPGTvfaynSDDEIFKDPSFLIQEAFYNMNTVI 1036
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  568 SLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLIKQSEVDYVDVFKAFSAILFGGMAI 647
Cdd:PTZ00265  1037 IYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYA 1116
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  648 GNASAFAPDAAKAEQSAKEIFKLIDKKPDIDNESEKGEQLHT---FTANLSFANIIFRYPTRPDTTILKGLDLEVPQGQT 724
Cdd:PTZ00265  1117 GKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNkndIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKT 1196
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  725 VALVGSSGCGKSTTVQLTERFYDPAD------------------------------------------------------ 750
Cdd:PTZ00265  1197 TAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfkns 1276
                          970       980       990      1000      1010      1020      1030
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688  751 GIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENIAYGdnSREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:PTZ00265  1277 GKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG--KEDATREDVKRACKFAAIDEFIESLPN 1346
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
1-296 8.34e-106

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: 337.06  E-value: 8.34e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   1 VFFSVMIGAfSLGNAMPHLQTLATARGAAYYLYQLITMDPPIDSYSTEGKKLDNFQGNVQIRGVHFRYPSRPEAKILYGV 80
Cdd:TIGR02204 281 VFYAVMVAG-SIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGL 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  81 NLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYGHL 160
Cdd:TIGR02204 360 NLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRP 439
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 161 DVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDAL 240
Cdd:TIGR02204 440 DATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQAL 519
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 241 EKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVTLQ 296
Cdd:TIGR02204 520 ETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
355-822 1.89e-104

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 333.67  E-value: 1.89e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 355 ASLGRILKLNKSEAPFIVMGCFASLVNGGAMPAFAVIFSEIlgVFAILDEGEQERkIIQYVLMFVGVGVISLIAYFVQGY 434
Cdd:COG1132     7 KLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRI--IDALLAGGDLSA-LLLLLLLLLGLALLRALLSYLQRY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 435 MFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDHnnSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSW 514
Cdd:COG1132    84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRR--RTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 515 KITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKA 594
Cdd:COG1132   162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 595 HLIGIGFSLSQAVMFFAYAASFWLGAYLIKQSEVDYVDVFKAFSAILFGGMAIGNASAFAPDAAKAEQSAKEIFKLIDKK 674
Cdd:COG1132   242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEP 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 675 PDIDnESEKGEQLHTFTANLSFANIIFRYPtrPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVS 754
Cdd:COG1132   322 PEIP-DPPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 755 LDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENIAYGDNsrEVTMDEIIDAARKANIHNFIASLPD 822
Cdd:COG1132   399 IDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRP--DATDEEVEEAAKAAQAHEFIEALPD 464
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
696-822 5.44e-68

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: 225.11  E-value: 5.44e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 696 FANIIFRYPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIV 775
Cdd:cd03249     3 FKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLV 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2119559688 776 SQEPVLFDRTIAENIAYGDNSRevTMDEIIDAARKANIHNFIASLPD 822
Cdd:cd03249    83 SQEPVLFDGTIAENIRYGKPDA--TDEEVEEAAKKANIHDFIMSLPD 127
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
371-645 2.42e-62

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: 210.96  E-value: 2.42e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 371 IVMGCFASLVNGGAMPAFAVIFSEILGVFAILDEGEqERKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSM 450
Cdd:pfam00664   1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPE-TQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 451 SFKAMLRQEIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIG 530
Cdd:pfam00664  80 LFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 531 GALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFF 610
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2119559688 611 AYAASFWLGAYLIKQSEVDY--VDVFKAFSAILFGGM 645
Cdd:pfam00664 238 SYALALWFGAYLVISGELSVgdLVAFLSLFAQLFGPL 274
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
353-822 3.39e-62

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 223.06  E-value: 3.39e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 353 VDASLGRILKLNKSEAPFIVMG---CFASLVNGGAMPAFAVIFSEILGVfailDEGEQERKIIQYVLMFVGVGviSLIAY 429
Cdd:TIGR00958 145 TADLLFRLLGLSGRDWPWLISAfvfLTLSSLGEMFIPFYTGRVIDTLGG----DKGPPALASAIFFMCLLSIA--SSVSA 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 430 FVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIG 509
Cdd:TIGR00958 219 GLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFD--ENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFM 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 510 FVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNI 589
Cdd:TIGR00958 297 LWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQL 376
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 590 ALKKAhLIGIGFSLSQAVM-FFAYAASFWLGAYLIKQSEVDYVDVFkafsAILFGGMAIGNA----SAFAPDAAKAEQSA 664
Cdd:TIGR00958 377 NKRKA-LAYAGYLWTTSVLgMLIQVLVLYYGGQLVLTGKVSSGNLV----SFLLYQEQLGEAvrvlSYVYSGMMQAVGAS 451
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 665 KEIFKLIDKKPDIDNEsekGEQLHTF-TANLSFANIIFRYPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTE 743
Cdd:TIGR00958 452 EKVFEYLDRKPNIPLT---GTLAPLNlEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQ 528
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 744 RFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENIAYGDNSREvtMDEIIDAARKANIHNFIASLPD 822
Cdd:TIGR00958 529 NLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTP--DEEIMAAAKAANAHDFIMEFPN 605
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
79-226 1.98e-48

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: 168.21  E-value: 1.98e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  79 GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLF-GTTIEENIRY 157
Cdd:pfam00005   3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENLRL 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 158 GHLDVTKEDIEQAAKMANAHDFiMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATS 226
Cdd:pfam00005  83 GLLLKGLSKREKDARAEEALEK-LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
378-822 6.06e-47

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 181.77  E-value: 6.06e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  378 SLVNGGAMPAFAVIFSEILgvfAILDEGEQERKIIqyvLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLR 457
Cdd:PTZ00265    69 ATISGGTLPFFVSVFGVIM---KNMNLGENVNDII---FSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFY 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  458 QEIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLgSSLMAFCSVVTGIVIGFVF-SWKITLLVIAFLPFVMIGGALEMQ 536
Cdd:PTZ00265   143 QDGQFHD--NNPGSKLTSDLDFYLEQVNAGIGTKF-ITIFTYASAFLGLYIWSLFkNARLTLCITCVFPLIYICGVICNK 219
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  537 MMQgaAGKNKEALESAGKIAI--ESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAA 614
Cdd:PTZ00265   220 KVK--INKKTSLLYNNNTMSIieEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAF 297
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  615 SFWLGAYLI------KQSEVDY--VDVFKAFSAILFGGMAIGNASAFAPDAAKAEQSAKEIFKLIDKKPDIDNESEkGEQ 686
Cdd:PTZ00265   298 GFWYGTRIIisdlsnQQPNNDFhgGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDD-GKK 376
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  687 LHTFTaNLSFANIIFRYPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADG-IVSLDGHNLKDLNL 765
Cdd:PTZ00265   377 LKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGdIIINDSHNLKDINL 455
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  766 QWLRSQIGIVSQEPVLFDRTIAENIAY------------------------GDNSREV--------------TMD----- 802
Cdd:PTZ00265   456 KWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealsnyynedgndsqeNKNKRNScrakcagdlndmsnTTDsneli 535
                          490       500       510
                   ....*....|....*....|....*....|..
gi 2119559688  803 ------------EIIDAARKANIHNFIASLPD 822
Cdd:PTZ00265   536 emrknyqtikdsEVVDVSKKVLIHDFVSALPD 567
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
668-822 2.35e-44

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: 169.62  E-value: 2.35e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 668 FKLIDKKPDIdNESEKGEQLHTFTANLSFANIIFRYptRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYD 747
Cdd:COG5265   333 FDLLDQPPEV-ADAPDAPPLVVGGGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYD 409
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 748 PADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENIAYGDNsrEVTMDEIIDAARKANIHNFIASLPD 822
Cdd:COG5265   410 VTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRP--DASEEEVEAAARAAQIHDFIESLPD 482
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
663-791 1.81e-25

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 111.84  E-value: 1.81e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 663 SAKEIFKLIDKKPDIDNESEKGEQLHTftANLSFANIIFRYPTRPDTtILKGLDLEVPQGQTVALVGSSGCGKSTTVQLT 742
Cdd:PRK11160  310 SARRINEITEQKPEVTFPTTSTAAADQ--VSLTLNNVSFTYPDQPQP-VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2119559688 743 ERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENIA 791
Cdd:PRK11160  387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLL 435
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
712-822 5.08e-23

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: 95.79  E-value: 5.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDR-TIAENI 790
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2119559688 791 AYG----DNSREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:pfam00005  81 RLGlllkGLSKREKDARAEEALEKLGLGDLADRPVG 116
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
67-263 7.03e-20

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 88.06  E-value: 7.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  67 RYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlkdinlkwwRENIGIVSQ---E 143
Cdd:NF040873    1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrseV 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 144 PVLFGTTIEENI---RYGHLD----VTKEDIEQAAKMANAhdfiMDLpqkyETLVGERGAQLSGGQKQRIAIARALVRNP 216
Cdd:NF040873   67 PDSLPLTVRDLVamgRWARRGlwrrLTRDDRAAVDDALER----VGL----ADLAGRQLGELSGGQRQRALLAQGLAQEA 138
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2119559688 217 KILLLDEATSALDTESEGIVQDAL-EKASHGRTTIVIAHRLSTIKTAD 263
Cdd:NF040873  139 DLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRAD 186
GguA NF040905
sugar ABC transporter ATP-binding protein;
72-271 1.81e-17

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 86.38  E-value: 1.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  72 PEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYdPE---EGQILIDG--VNLKDINLKwwrENIGIV--SQE- 143
Cdd:NF040905   12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGevCRFKDIRDS---EALGIViiHQEl 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 144 ---PVLfgtTIEENIRYGHldvtkediEQAAKManahdfIMDLPQKY----------------ETLVGERGAqlsgGQKQ 204
Cdd:NF040905   88 aliPYL---SIAENIFLGN--------ERAKRG------VIDWNETNrrarellakvgldespDTLVTDIGV----GKQQ 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 205 RIAIARALVRNPKILLLDEATSAL-DTESEGIVQDALEKASHGRTTIVIAHRLSTI-KTADMIAGFKDG 271
Cdd:NF040905  147 LVEIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDG 215
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
86-268 3.69e-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: 67.78  E-value: 3.69e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   86 RGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIdgvnlkdINLKWWRENIGIvsqepvlfgttieeniryghldvtke 165
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------IDGEDILEEVLD-------------------------- 47
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  166 dieqaakmanahdfimdlpQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALE---- 241
Cdd:smart00382  48 -------------------QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrll 108
                          170       180       190
                   ....*....|....*....|....*....|
gi 2119559688  242 ---KASHGRTTIVIAHRLSTIKTADMIAGF 268
Cdd:smart00382 109 lllKSEKNLTVILTTNDEKDLGPALLRRRF 138
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
80-229 5.87e-10

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 63.22  E-value: 5.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG--VNLKDINLkwwRENIGIVSQEPVLFGT-TIEENIR 156
Cdd:NF033858  285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDAGDIAT---RRRVGYMSQAFSLYGElTVRQNLE 361
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 157 -YGHL-DVTKEDIEQA-AKMAnaHDFimDLpqkyETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 229
Cdd:NF033858  362 lHARLfHLPAAEIAARvAEML--ERF--DL----ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
712-757 6.31e-08

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: 54.39  E-value: 6.31e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDG 757
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG 46
ABC_6TM_Pgp_ABCB1_D1_like cd18577
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...
1-32 4.42e-07

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: 52.48  E-value: 4.42e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2119559688   1 VFFSVMIGAFSLGNAMPHLQTLATARGAAYYL 32
Cdd:cd18577   269 VFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
59-278 1.38e-04

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 45.11  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGV--HFrypsrPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVqLLQRFYDPEEGQilidgvnlKDINLKWW--- 133
Cdd:NF000106   14 VEVRGLvkHF-----GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGR--------RPWRF*TWcan 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 134 ----RENIGIvsQEPVLFGT----TIEENIRY--GHLDVTKEDIEQAAKmanahdfimDLPQKYE--TLVGERGAQLSGG 201
Cdd:NF000106   80 rralRRTIG*--HRPVR*GRresfSGRENLYMigR*LDLSRKDARARAD---------ELLERFSltEAAGRAAAKYSGG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 202 QKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIV-----------IAHRLSTIKTADMIAgfkD 270
Cdd:NF000106  149 MRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLlttqymeeaeqLAHELTVIDRGRVIA---D 225

                  ....*...
gi 2119559688 271 GVVAEQGT 278
Cdd:NF000106  226 GKVDELKT 233
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
721-769 6.21e-03

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: 38.12  E-value: 6.21e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2119559688  721 QGQTVALVGSSGCGKSTTVQLTERFYDPAD-GIVSLDGHNLKDLNLQWLR 769
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGgGVIYIDGEDILEEVLDQLL 50
 
Name Accession Description Interval E-value
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
59-296 3.34e-152

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: 444.68  E-value: 3.34e-152
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIG 138
Cdd:cd03249     1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKI 218
Cdd:cd03249    81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 219 LLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVTLQ 296
Cdd:cd03249   161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
ABC_6TM_Pgp_ABCB1_D2_like cd18578
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...
361-677 2.76e-147

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: 435.34  E-value: 2.76e-147
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 361 LKLNKSEAPFIVMGCFASLVNGGAMPAFAVIFSEILGVFAILDEGEQERKIIQYVLMFVGVGVISLIAYFVQGYMFGRSG 440
Cdd:cd18578     1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIAYFLQGYLFGIAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 441 EYLTLRLRSMSFKAMLRQEIAFFDDHNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLV 520
Cdd:cd18578    81 ERLTRRLRKLAFRAILRQDIAWFDDPENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 521 IAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIG 600
Cdd:cd18578   161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 601 FSLSQAVMFFAYAASFWLGAYLIKQSEVDYVDVFKAFSAILFGGMAIGNASAFAPDAAKAEQSAKEIFKLIDKKPDI 677
Cdd:cd18578   241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPEI 317
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
19-300 1.68e-133

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 409.55  E-value: 1.68e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  19 LQTLATARGAAYYLYQLITMDPPIDSySTEGKKLDNFQGNVQIRGVHFRYPsrPEAKILYGVNLQIKRGQTVALVGSSGC 98
Cdd:COG1132   301 LNQLQRALASAERIFELLDEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGS 377
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  99 GKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHD 178
Cdd:COG1132   378 GKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHE 457
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 179 FIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLST 258
Cdd:COG1132   458 FIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLST 537
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2119559688 259 IKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVTLQSMKS 300
Cdd:COG1132   538 IRNADRILVLDDGRIVEQGTHEELLARGGLYARLYRLQFGEE 579
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
3-296 5.15e-117

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: 370.70  E-value: 5.15e-117
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   3 FSVMIGAF--SLGNAMPHLQTLATARGAAYYLYQLitMDPPIDSYSTEGKK-LDNFQGNVQIRGVHFRYPSRpEAKILYG 79
Cdd:COG2274   417 FNILSGRFlaPVAQLIGLLQRFQDAKIALERLDDI--LDLPPEREEGRSKLsLPRLKGDIELENVSFRYPGD-SPPVLDN 493
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYGH 159
Cdd:COG2274   494 ISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGD 573
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 160 LDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDA 239
Cdd:COG2274   574 PDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILEN 653
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 240 LEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVTLQ 296
Cdd:COG2274   654 LRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLARKGLYAELVQQQ 710
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
59-292 1.06e-116

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: 353.07  E-value: 1.06e-116
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPEAkILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIG 138
Cdd:cd03251     1 VEFKNVTFRYPGDGPP-VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKI 218
Cdd:cd03251    80 LVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 219 LLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQL 292
Cdd:cd03251   160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
1-822 1.76e-114

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 380.14  E-value: 1.76e-114
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688    1 VFFSVMIGAFSLGNAMPHLQTLATARGAAYYLYQLITMDPPIDSySTEGKKLDNFQgNVQIRGVHFRYPSRPEAKILYGV 80
Cdd:PTZ00265   327 ILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVEN-NDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDL 404
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   81 NLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILI-DGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRY-- 157
Cdd:PTZ00265   405 NFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYsl 484
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  158 ------------------------------------------------GHLDVTKE-------DIEQAAKMANAHDFIMD 182
Cdd:PTZ00265   485 yslkdlealsnyynedgndsqenknkrnscrakcagdlndmsnttdsnELIEMRKNyqtikdsEVVDVSKKVLIHDFVSA 564
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  183 LPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALE--KASHGRTTIVIAHRLSTIK 260
Cdd:PTZ00265   565 LPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIR 644
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  261 TADMI------------------------------------AGFKD-----------GVVAEQGTHNELM-SKQGIYQQL 292
Cdd:PTZ00265   645 YANTIfvlsnrergstvdvdiigedptkdnkennnknnkddNNNNNnnnnnkinnagSYIIEQGTHDALMkNKNGIYYTM 724
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  293 VTLQSMKSADDNEIEDFNRDDTKRPSLRHQKSTIDmtPKKLAQDKKEEIKEEEKGEKEEEVDAS------------LGRI 360
Cdd:PTZ00265   725 INNQKVSSKKSSNNDNDKDSDMKSSAYKDSERGYD--PDEMNGNSKHENESASNKKSCKMSDENasennaggklpfLRNL 802
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  361 LKlNKSEAPF---------------IVMGCFASLVNGGAMPAFAVIFSEILGvfAILDEGEQERKIIQYVLMFVGVGVIS 425
Cdd:PTZ00265   803 FK-RKPKAPNnlrivyreifsykkdVTIIALSILVAGGLYPVFALLYAKYVS--TLFDFANLEANSNKYSLYILVIAIAM 879
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  426 LIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDHNNSVGALTTRLATDASQVQGA-----------AGIKLGS 494
Cdd:PTZ00265   880 FISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDQDKHAPGLLSAHINRDVHLLKTGlvnnivifthfIVLFLVS 959
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  495 SLMA--FCSVVTGIVIGFVFswkITLLVIAFLPFVMIGGALEMQMMQGAAG-----KNKEALESAGKIAIESIENIRTVA 567
Cdd:PTZ00265   960 MVMSfyFCPIVAAVLTGTYF---IFMRVFAIRARLTANKDVEKKEINQPGTvfaynSDDEIFKDPSFLIQEAFYNMNTVI 1036
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  568 SLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLIKQSEVDYVDVFKAFSAILFGGMAI 647
Cdd:PTZ00265  1037 IYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWGFSQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYA 1116
                          810       820       830       840       850       860       870       880
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  648 GNASAFAPDAAKAEQSAKEIFKLIDKKPDIDNESEKGEQLHT---FTANLSFANIIFRYPTRPDTTILKGLDLEVPQGQT 724
Cdd:PTZ00265  1117 GKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVRDNGGIRIKNkndIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKT 1196
                          890       900       910       920       930       940       950       960
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  725 VALVGSSGCGKSTTVQLTERFYDPAD------------------------------------------------------ 750
Cdd:PTZ00265  1197 TAIVGETGSGKSTVMSLLMRFYDLKNdhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfkns 1276
                          970       980       990      1000      1010      1020      1030
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688  751 GIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENIAYGdnSREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:PTZ00265  1277 GKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFG--KEDATREDVKRACKFAAIDEFIESLPN 1346
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
56-297 7.79e-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: 359.13  E-value: 7.79e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  56 QGNVQIRGVHFRYpsRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRE 135
Cdd:COG5265   355 GGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRA 432
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRN 215
Cdd:COG5265   433 AIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKN 512
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 216 PKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVTL 295
Cdd:COG5265   513 PPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMWAR 592

                  ..
gi 2119559688 296 QS 297
Cdd:COG5265   593 QQ 594
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
59-296 8.32e-111

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: 338.05  E-value: 8.32e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPsrPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIG 138
Cdd:cd03253     1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKI 218
Cdd:cd03253    79 VVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 219 LLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVTLQ 296
Cdd:cd03253   159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
1-296 8.34e-106

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: 337.06  E-value: 8.34e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   1 VFFSVMIGAfSLGNAMPHLQTLATARGAAYYLYQLITMDPPIDSYSTEGKKLDNFQGNVQIRGVHFRYPSRPEAKILYGV 80
Cdd:TIGR02204 281 VFYAVMVAG-SIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGL 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  81 NLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYGHL 160
Cdd:TIGR02204 360 NLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGRP 439
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 161 DVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDAL 240
Cdd:TIGR02204 440 DATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQAL 519
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 241 EKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVTLQ 296
Cdd:TIGR02204 520 ETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
57-287 1.39e-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: 324.18  E-value: 1.39e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  57 GNVQIRGVHFRYpsRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWREN 136
Cdd:cd03254     1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNP 216
Cdd:cd03254    79 IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDP 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 217 KILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQG 287
Cdd:cd03254   159 KILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
355-822 1.89e-104

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 333.67  E-value: 1.89e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 355 ASLGRILKLNKSEAPFIVMGCFASLVNGGAMPAFAVIFSEIlgVFAILDEGEQERkIIQYVLMFVGVGVISLIAYFVQGY 434
Cdd:COG1132     7 KLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRI--IDALLAGGDLSA-LLLLLLLLLGLALLRALLSYLQRY 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 435 MFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDHnnSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSW 514
Cdd:COG1132    84 LLARLAQRVVADLRRDLFEHLLRLPLSFFDRR--RTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 515 KITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKA 594
Cdd:COG1132   162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 595 HLIGIGFSLSQAVMFFAYAASFWLGAYLIKQSEVDYVDVFKAFSAILFGGMAIGNASAFAPDAAKAEQSAKEIFKLIDKK 674
Cdd:COG1132   242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEP 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 675 PDIDnESEKGEQLHTFTANLSFANIIFRYPtrPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVS 754
Cdd:COG1132   322 PEIP-DPPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRIL 398
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 755 LDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENIAYGDNsrEVTMDEIIDAARKANIHNFIASLPD 822
Cdd:COG1132   399 IDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRP--DATDEEVEEAAKAAQAHEFIEALPD 464
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
23-287 6.53e-100

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: 321.32  E-value: 6.53e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  23 ATARGAAYYLYQLITMDPPIDSYSTEGKKLDNfQGNVQIRGVHFRYPSRPEAkiLYGVNLQIKRGQTVALVGSSGCGKST 102
Cdd:COG4988   302 ANGIAAAEKIFALLDAPEPAAPAGTAPLPAAG-PPSIELEDVSFSYPGGRPA--LDGLSLTIPPGERVALVGPSGAGKST 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 103 IVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMD 182
Cdd:COG4988   379 LLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAA 458
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 183 LPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTA 262
Cdd:COG4988   459 LPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQA 538
                         250       260
                  ....*....|....*....|....*
gi 2119559688 263 DMIAGFKDGVVAEQGTHNELMSKQG 287
Cdd:COG4988   539 DRILVLDDGRIVEQGTHEELLAKNG 563
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
1-296 5.07e-95

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 308.87  E-value: 5.07e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   1 VFFSVMIGAF----SLGNAMPHLQtlataRG--AAYYLYQLITMDPPIDsystEGK-KLDNFQGNVQIRGVHFRYPSRpE 73
Cdd:PRK11176  286 VVFSSMIALMrplkSLTNVNAQFQ-----RGmaACQTLFAILDLEQEKD----EGKrVIERAKGDIEFRNVTFTYPGK-E 355
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  74 AKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEE 153
Cdd:PRK11176  356 VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIAN 435
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 154 NIRYGHLDV-TKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 232
Cdd:PRK11176  436 NIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTES 515
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 233 EGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVTLQ 296
Cdd:PRK11176  516 ERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQ 579
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
4-293 5.64e-95

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 312.43  E-value: 5.64e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   4 SVMIGAFSLGNAMPHLQT----LATARGAAYYLYQLITMDPPIDSysTEGKKLDNFQGNVQIRGVHFRYPSRPEAKILYG 79
Cdd:TIGR00958 422 SFLLYQEQLGEAVRVLSYvysgMMQAVGASEKVFEYLDRKPNIPL--TGTLAPLNLEGLIEFQDVSFSYPNRPDVPVLKG 499
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYGH 159
Cdd:TIGR00958 500 LTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGL 579
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 160 LDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDA 239
Cdd:TIGR00958 580 TDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQES 659
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 240 LEKAShgRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLV 293
Cdd:TIGR00958 660 RSRAS--RTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
1-296 1.94e-94

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: 307.03  E-value: 1.94e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   1 VFFSVMIGAF----SLGNAMPHLQTLATArgaAYYLYQLITMDPPIDsysTEGKKLDNFQGNVQIRGVHFRYPSRpEAKI 76
Cdd:TIGR02203 275 AFITAMIALIrplkSLTNVNAPMQRGLAA---AESLFTLLDSPPEKD---TGTRAIERARGDVEFRNVTFRYPGR-DRPA 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  77 LYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIR 156
Cdd:TIGR02203 348 LDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIA 427
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 157 YGHL-DVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGI 235
Cdd:TIGR02203 428 YGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERL 507
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 236 VQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVTLQ 296
Cdd:TIGR02203 508 VQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
50-303 5.22e-94

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 306.50  E-value: 5.22e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  50 KKLDNFQGNVQIRGVHFRYPSRPEAkiLYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN 129
Cdd:PRK13657  326 IDLGRVKGAVEFDDVSFSYDNSRQG--VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT 403
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 130 LKWWRENIGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIA 209
Cdd:PRK13657  404 RASLRRNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIA 483
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 210 RALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIY 289
Cdd:PRK13657  484 RALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRF 563
                         250
                  ....*....|....
gi 2119559688 290 QQLVTLQSMKSADD 303
Cdd:PRK13657  564 AALLRAQGMLQEDE 577
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
59-296 6.11e-93

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: 291.31  E-value: 6.11e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYpsRP-EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENI 137
Cdd:cd03252     1 ITFEHVRFRY--KPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 GIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPK 217
Cdd:cd03252    79 GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 218 ILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVTLQ 296
Cdd:cd03252   159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
38-297 1.30e-85

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: 287.02  E-value: 1.30e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  38 MDPPIDSYSTEGKKLDNFQGNVQIRGVHFRY-PSRPEakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEG 116
Cdd:TIGR01846 435 LNSPTEPRSAGLAALPELRGAITFENIRFRYaPDSPE--VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHG 512
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 117 QILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGA 196
Cdd:TIGR01846 513 QVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGA 592
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 197 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQ 276
Cdd:TIGR01846 593 NLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAES 672
                         250       260
                  ....*....|....*....|.
gi 2119559688 277 GTHNELMSKQGIYQQLVTLQS 297
Cdd:TIGR01846 673 GRHEELLALQGLYARLWQQQS 693
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
1-295 2.64e-85

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: 282.43  E-value: 2.64e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   1 VFFSVMiGAF----SLGNAMPHLqtlATARGAAYYLYQLITMDPPIdSYSTEGKKLDNfQGNVQIRGVHFRYPSRPEAkI 76
Cdd:COG4987   278 LVLAAL-ALFealaPLPAAAQHL---GRVRAAARRLNELLDAPPAV-TEPAEPAPAPG-GPSLELEDVSFRYPGAGRP-V 350
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  77 LYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIR 156
Cdd:COG4987   351 LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLR 430
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 157 YGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIV 236
Cdd:COG4987   431 LARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQAL 510
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 237 QDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVTL 295
Cdd:COG4987   511 LADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQLYQR 569
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
59-271 1.03e-83

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: 1.03e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPEaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIG 138
Cdd:cd03228     1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFGTTIEENIryghldvtkedieqaakmanahdfimdlpqkyetlvgergaqLSGGQKQRIAIARALVRNPKI 218
Cdd:cd03228    80 YVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPI 117
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 219 LLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDG 271
Cdd:cd03228   118 LILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDG 170
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
53-265 2.51e-82

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: 262.79  E-value: 2.51e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  53 DNFQGNVQIRGVHFRYPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKW 132
Cdd:cd03248     6 DHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 133 WRENIGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARAL 212
Cdd:cd03248    86 LHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARAL 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 213 VRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMI 265
Cdd:cd03248   166 IRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQI 218
ABC_6TM_Pgp_ABCB1_D1_like cd18577
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...
371-667 2.47e-81

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: 263.18  E-value: 2.47e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 371 IVMGCFASLVNGGAMPAFAVIFSEILGVFA-----ILDEGEQERKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTL 445
Cdd:cd18577     1 LIIGLLAAIAAGAALPLMTIVFGDLFDAFTdfgsgESSPDEFLDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQAR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 446 RLRSMSFKAMLRQEIAFFDDHnnSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLP 525
Cdd:cd18577    81 RIRKRYLKALLRQDIAWFDKN--GAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLP 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 526 FVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQ 605
Cdd:cd18577   159 LIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLF 238
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 606 AVMFFAYAASFWLGAYLIKQSEVDYVDVFKAFSAILFGGMAIGNASAFAPDAAKAEQSAKEI 667
Cdd:cd18577   239 FIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
ABC_6TM_Pgp_ABCB1 cd18558
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ...
371-667 8.14e-78

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: 254.12  E-value: 8.14e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 371 IVMGCFASLVNGGAMPAFAVIFSEILGVFAILDE-----------------GEQERKIIQYVLMFVGVGVISLIAYFVQG 433
Cdd:cd18558     1 MVVGILCAIIHGGLLPAFMVIFGDMTDSFTNGGMtnitgnssglnssagpfEKLEEEMTLYAYYYLIIGAIVLITAYIQG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 434 YMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFS 513
Cdd:cd18558    81 SFWGLAAGRQTKKIRYKFFHAIMRQEIGWFD--VNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 514 WKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKK 593
Cdd:cd18558   159 WKLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKK 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 594 AHLIGIGFSLSQAVMFFAYAASFWLGAYLIKQSEVDYVDVFKA-FSAILFGGMAIGNASAFAPdAAKAEQSAKEI 667
Cdd:cd18558   239 AITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSIGEVLTVfFSVLIGAFSAGQQVPSIEA-FANARGAAYHI 312
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
41-293 8.08e-71

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: 246.78  E-value: 8.08e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  41 PIDSYSTEGKKLdnfQGNVQIRGVHFRYpSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILI 120
Cdd:TIGR03796 463 GSAATSEPPRRL---SGYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILF 538
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 121 DGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSG 200
Cdd:TIGR03796 539 DGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSG 618
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 201 GQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKasHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHN 280
Cdd:TIGR03796 619 GQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHE 696
                         250
                  ....*....|...
gi 2119559688 281 ELMSKQGIYQQLV 293
Cdd:TIGR03796 697 ELWAVGGAYARLI 709
chvA TIGR01192
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ...
51-303 4.02e-69

glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 130260 [Multi-domain]  Cd Length: 585  Bit Score: 239.41  E-value: 4.02e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  51 KLDNFQGNVQIRGVHFRYPSRPEAkiLYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINL 130
Cdd:TIGR01192 327 ELPNVKGAVEFRHITFEFANSSQG--VFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTR 404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 131 KWWRENIGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIAR 210
Cdd:TIGR01192 405 ESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIAR 484
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 211 ALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQ 290
Cdd:TIGR01192 485 AILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFY 564
                         250
                  ....*....|...
gi 2119559688 291 QLVTLQSMKSADD 303
Cdd:TIGR01192 565 KLLRRSGLLTNQP 577
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
26-305 1.63e-68

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 237.30  E-value: 1.63e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  26 RGAAYY--LYQLITMDPPIDSYStegKKLDNFQGNVQIRGVHFRYPSRpEAKILYGVNLQIKRGQTVALVGSSGCGKSTI 103
Cdd:PRK10789  282 RGSAAYsrIRAMLAEAPVVKDGS---EPVPEGRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTL 357
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 104 VQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDL 183
Cdd:PRK10789  358 LSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRL 437
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 184 PQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTAD 263
Cdd:PRK10789  438 PQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEAS 517
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 2119559688 264 MIAGFKDGVVAEQGTHNELMSKQGIYQQLVTLQSMKSADDNE 305
Cdd:PRK10789  518 EILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQLEAALDDA 559
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
356-822 5.30e-68

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: 238.97  E-value: 5.30e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 356 SLGRILKLNKSEAPFIVMGCFASLVNGgampAFAVIFSeiLGVFAILDE---GEQERKIIQYVLMFVGVGVISLIAYFVQ 432
Cdd:COG2274   143 GLRWFLRLLRRYRRLLLQVLLASLLIN----LLALATP--LFTQVVIDRvlpNQDLSTLWVLAIGLLLALLFEGLLRLLR 216
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 433 GYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDHnnSVGALTTRLaTDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVF 512
Cdd:COG2274   217 SYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESR--SVGDLASRF-RDVESIREFLTGSLLTALLDLLFVLIFLIVLFFY 293
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 513 SWKITLLVIAFLPFVMIGGALemqMMQGAAGKNKEALESAGKIA---IESIENIRTVASLTREDMFQKKFNHELQMPYNI 589
Cdd:COG2274   294 SPPLALVVLLLIPLYVLLGLL---FQPRLRRLSREESEASAKRQsllVETLRGIETIKALGAESRFRRRWENLLAKYLNA 370
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 590 ALKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLIKQSEVDyVDVFKAFSaILFGGM--AIGNASAFAPDAAKAEQSAKEI 667
Cdd:COG2274   371 RFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLT-LGQLIAFN-ILSGRFlaPVAQLIGLLQRFQDAKIALERL 448
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 668 FKLIDKKPDIDnESEKGEQLHTFTANLSFANIIFRYPTRpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYD 747
Cdd:COG2274   449 DDILDLPPERE-EGRSKLSLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYE 526
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 748 PADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENIAYGDnsREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:COG2274   527 PTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGD--PDATDEEIIEAARLAGLHDFIEALPM 599
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
696-822 5.44e-68

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: 225.11  E-value: 5.44e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 696 FANIIFRYPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIV 775
Cdd:cd03249     3 FKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLV 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2119559688 776 SQEPVLFDRTIAENIAYGDNSRevTMDEIIDAARKANIHNFIASLPD 822
Cdd:cd03249    83 SQEPVLFDGTIAENIRYGKPDA--TDEEVEEAAKKANIHDFIMSLPD 127
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
23-265 1.21e-67

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: 233.72  E-value: 1.21e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  23 ATARGAAYYLYQLITMDPPIDSYSTEGKKLDNFQgnVQIRGVHFRYPSRPEAkiLYGVNLQIKRGQTVALVGSSGCGKST 102
Cdd:TIGR02857 288 ADGVAAAEALFAVLDAAPRPLAGKAPVTAAPASS--LEFSGVSVAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGKST 363
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 103 IVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMD 182
Cdd:TIGR02857 364 LLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAA 443
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 183 LPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTA 262
Cdd:TIGR02857 444 LPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALA 523

                  ...
gi 2119559688 263 DMI 265
Cdd:TIGR02857 524 DRI 526
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
57-278 2.02e-67

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: 222.75  E-value: 2.02e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  57 GNVQIRGVHFRYpsRPEAK-ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRE 135
Cdd:cd03244     1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEPVLFGTTIEENiryghLD----VTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARA 211
Cdd:cd03244    79 RISIIPQDPVLFSGTIRSN-----LDpfgeYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARA 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 212 LVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGT 278
Cdd:cd03244   154 LLRKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
57-274 4.87e-67

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: 221.69  E-value: 4.87e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  57 GNVQIRGVHFRYPSRpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWREN 136
Cdd:cd03245     1 GRIEFRNVSFSYPNQ-EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNP 216
Cdd:cd03245    80 IGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDP 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 217 KILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDG-VVA 274
Cdd:cd03245   160 PILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGrIVA 218
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
56-296 1.85e-63

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: 225.99  E-value: 1.85e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  56 QGNVQIRGVHFRYpsRPEAK-ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWR 134
Cdd:TIGR03797 449 SGAIEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVR 526
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 135 ENIGIVSQEPVLFGTTIEENIrYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVR 214
Cdd:TIGR03797 527 RQLGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVR 605
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 215 NPKILLLDEATSALDTESEGIVQDALEKASHGRttIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVT 294
Cdd:TIGR03797 606 KPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREGLFAQLAR 683

                  ..
gi 2119559688 295 LQ 296
Cdd:TIGR03797 684 RQ 685
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
33-295 1.09e-62

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 230.30  E-value: 1.09e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   33 YQLITMDPPIDSYSTEGKKLDN---FQGNVQIRGVHFRYPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQR 109
Cdd:PTZ00265  1137 YPLIIRKSNIDVRDNGGIRIKNkndIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMR 1216
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  110 FYD------------------------------------------------------PEEGQILIDGVNLKDINLKWWRE 135
Cdd:PTZ00265  1217 FYDlkndhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLRN 1296
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  136 NIGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRN 215
Cdd:PTZ00265  1297 LFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLRE 1376
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  216 PKILLLDEATSALDTESEGIVQ----DALEKAShgRTTIVIAHRLSTIKTADMIAGFKD-----GVVAEQGTHNELMSKQ 286
Cdd:PTZ00265  1377 PKILLLDEATSSLDSNSEKLIEktivDIKDKAD--KTIITIAHRIASIKRSDKIVVFNNpdrtgSFVQAHGTHEELLSVQ 1454
                          330
                   ....*....|
gi 2119559688  287 -GIYQQLVTL 295
Cdd:PTZ00265  1455 dGVYKKYVKL 1464
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
23-292 1.49e-62

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 221.26  E-value: 1.49e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  23 ATARGAAYYLYQLitMDPPIDSYSTEGKKLDNFQGnVQIRGVHFRYPSrPEAKILYG-VNLQIKRGQTVALVGSSGCGKS 101
Cdd:PRK11174  315 AQAVGAAESLVTF--LETPLAHPQQGEKELASNDP-VTIEAEDLEILS-PDGKTLAGpLNFTLPAGQRIALVGPSGAGKT 390
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 102 TIVQLLQRFYdPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIM 181
Cdd:PRK11174  391 SLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQQALENAWVSEFLP 469
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 182 DLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKT 261
Cdd:PRK11174  470 LLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQ 549
                         250       260       270
                  ....*....|....*....|....*....|.
gi 2119559688 262 ADMIAGFKDGVVAEQGTHNELMSKQGIYQQL 292
Cdd:PRK11174  550 WDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
ABC_membrane pfam00664
ABC transporter transmembrane region; This family represents a unit of six transmembrane ...
371-645 2.42e-62

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: 210.96  E-value: 2.42e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 371 IVMGCFASLVNGGAMPAFAVIFSEILGVFAILDEGEqERKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSM 450
Cdd:pfam00664   1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPE-TQALNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 451 SFKAMLRQEIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIG 530
Cdd:pfam00664  80 LFKKILRQPMSFFD--TNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 531 GALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFF 610
Cdd:pfam00664 158 SAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYL 237
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2119559688 611 AYAASFWLGAYLIKQSEVDY--VDVFKAFSAILFGGM 645
Cdd:pfam00664 238 SYALALWFGAYLVISGELSVgdLVAFLSLFAQLFGPL 274
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
353-822 3.39e-62

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 223.06  E-value: 3.39e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 353 VDASLGRILKLNKSEAPFIVMG---CFASLVNGGAMPAFAVIFSEILGVfailDEGEQERKIIQYVLMFVGVGviSLIAY 429
Cdd:TIGR00958 145 TADLLFRLLGLSGRDWPWLISAfvfLTLSSLGEMFIPFYTGRVIDTLGG----DKGPPALASAIFFMCLLSIA--SSVSA 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 430 FVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIG 509
Cdd:TIGR00958 219 GLRGGSFNYTMARINLRIREDLFRSLLRQDLGFFD--ENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFM 296
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 510 FVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNI 589
Cdd:TIGR00958 297 LWLSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQL 376
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 590 ALKKAhLIGIGFSLSQAVM-FFAYAASFWLGAYLIKQSEVDYVDVFkafsAILFGGMAIGNA----SAFAPDAAKAEQSA 664
Cdd:TIGR00958 377 NKRKA-LAYAGYLWTTSVLgMLIQVLVLYYGGQLVLTGKVSSGNLV----SFLLYQEQLGEAvrvlSYVYSGMMQAVGAS 451
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 665 KEIFKLIDKKPDIDNEsekGEQLHTF-TANLSFANIIFRYPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTE 743
Cdd:TIGR00958 452 EKVFEYLDRKPNIPLT---GTLAPLNlEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQ 528
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 744 RFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENIAYGDNSREvtMDEIIDAARKANIHNFIASLPD 822
Cdd:TIGR00958 529 NLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTP--DEEIMAAAKAANAHDFIMEFPN 605
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
56-285 6.38e-61

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: 216.15  E-value: 6.38e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  56 QGNVQIRGVHFRYPSRPEAkILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDinlkWWRE 135
Cdd:COG4618   328 KGRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQ----WDRE 402
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 ----NIGIVSQEPVLFGTTIEENI-RYGhlDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIAR 210
Cdd:COG4618   403 elgrHIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLAR 480
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 211 ALVRNPKILLLDEATSALDTESEGIVQDALEKA-SHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSK 285
Cdd:COG4618   481 ALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
1-292 1.86e-57

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 206.60  E-value: 1.86e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   1 VFFSVMiGAFS----LGNAMPHL-QTLATARgaayYLYQLITMDPPIDSYSTEGKKLDnfQGNVQIRGVHFRYPSRPEaK 75
Cdd:PRK11160  283 FVFAAL-AAFEalmpVAGAFQHLgQVIASAR----RINEITEQKPEVTFPTTSTAAAD--QVSLTLNNVSFTYPDQPQ-P 354
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  76 ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENI 155
Cdd:PRK11160  355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNL 434
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 156 RYGHLDVTKEDIEQAAKMANAHDFIMDlPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGI 235
Cdd:PRK11160  435 LLAAPNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQ 513
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 236 VQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQL 292
Cdd:PRK11160  514 ILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
38-296 4.64e-55

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 200.33  E-value: 4.64e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  38 MDPPIDSYSTEGKKLDnfQGNVQIRGVHFRYpsRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQ 117
Cdd:PRK10790  322 MDGPRQQYGNDDRPLQ--SGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGE 397
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 118 ILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYGHlDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQ 197
Cdd:PRK10790  398 IRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGR-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNN 476
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 198 LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQG 277
Cdd:PRK10790  477 LSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQG 556
                         250
                  ....*....|....*....
gi 2119559688 278 THNELMSKQGIYQQLVTLQ 296
Cdd:PRK10790  557 THQQLLAAQGRYWQMYQLQ 575
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
1-256 1.85e-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: 194.50  E-value: 1.85e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   1 VFFSVMIGAFSLGNAMPH-LQTLATARGAAYYLYQLITMDPPIDSYSTEGKKLDNFQG-NVQIRGVHFRYPSRPEAkiLY 78
Cdd:TIGR02868 275 VLVLLPLAAFEAFAALPAaAQQLTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAPPV--LD 352
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  79 GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYG 158
Cdd:TIGR02868 353 GVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLA 432
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 159 HLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQD 238
Cdd:TIGR02868 433 RPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLE 512
                         250
                  ....*....|....*...
gi 2119559688 239 ALEKASHGRTTIVIAHRL 256
Cdd:TIGR02868 513 DLLAALSGRTVVLITHHL 530
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
379-822 1.69e-52

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: 192.62  E-value: 1.69e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 379 LVNGGAMPAFAVIFSEILGVFA-ILDEG--EQERKIIQYV-LMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKA 454
Cdd:TIGR02203  17 VLAGVAMILVAATESTLAALLKpLLDDGfgGRDRSVLWWVpLVVIGLAVLRGICSFVSTYLLSWVSNKVVRDIRVRMFEK 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 455 MLRQEIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIggale 534
Cdd:TIGR02203  97 LLGLPVSFFD--RQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLTLIVVVMLPVLSI----- 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 535 mqMMQGAAGK----NKEALESAGK---IAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAV 607
Cdd:TIGR02203 170 --LMRRVSKRlrriSKEIQNSMGQvttVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSPITQLI 247
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 608 MFFAYAASFWLGAYlikQSEVDYVDV--FKAF-SAILFGGMAIGNASAFAPDAAKAEQSAKEIFKLIDKKPDIDnesEKG 684
Cdd:TIGR02203 248 ASLALAVVLFIALF---QAQAGSLTAgdFTAFiTAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKD---TGT 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 685 EQLHTFTANLSFANIIFRYPTRpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN 764
Cdd:TIGR02203 322 RAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT 400
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 765 LQWLRSQIGIVSQEPVLFDRTIAENIAYGDnSREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:TIGR02203 401 LASLRRQVALVSQDVVLFNDTIANNIAYGR-TEQADRAEIERALAAAYAQDFVDKLPL 457
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
14-294 8.06e-51

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: 190.34  E-value: 8.06e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  14 NAMPHLQT--LATARGAAYYLyqlitmdppIDSYSTEGKKLD---NFQGNVQIRGVHFRYPSrpEAKILYGVNLQIKRGQ 88
Cdd:TIGR01193 433 NLQPKLQAarVANNRLNEVYL---------VDSEFINKKKRTelnNLNGDIVINDVSYSYGY--GSNILSDISLTIKMNS 501
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  89 TVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRYG-HLDVTKEDI 167
Cdd:TIGR01193 502 KTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEI 581
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 168 EQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHgR 247
Cdd:TIGR01193 582 WAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-K 660
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 2119559688 248 TTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVT 294
Cdd:TIGR01193 661 TIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLIH 707
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
60-254 4.42e-50

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 175.00  E-value: 4.42e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGI 139
Cdd:COG4619     2 ELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 VSQEPVLFGTTIEENI----RYGHLDVTKEDIEQAAKMANAHDFIMDLPqkyetlvgerGAQLSGGQKQRIAIARALVRN 215
Cdd:COG4619    79 VPQEPALWGGTVRDNLpfpfQLRERKFDRERALELLERLGLPPDILDKP----------VERLSGGERQRLALIRALLLQ 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2119559688 216 PKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAH 254
Cdd:COG4619   149 PDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSH 189
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
24-285 4.98e-50

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: 184.86  E-value: 4.98e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  24 TARGAAYYLYQLITMDPPIDsystEGKKLDNFQGNVQIRGVHFRYPSrPEAKILYGVNLQIKRGQTVALVGSSGCGKSTI 103
Cdd:TIGR01842 286 GARQAYKRLNELLANYPSRD----PAMPLPEPEGHLSVENVTIVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKSTL 360
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 104 VQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENI-RYGHlDVTKEDIEQAAKMANAHDFIMD 182
Cdd:TIGR01842 361 ARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIaRFGE-NADPEKIIEAAKLAGVHELILR 439
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 183 LPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKA-SHGRTTIVIAHRLSTIKT 261
Cdd:TIGR01842 440 LPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGC 519
                         250       260
                  ....*....|....*....|....
gi 2119559688 262 ADMIAGFKDGVVAEQGTHNELMSK 285
Cdd:TIGR01842 520 VDKILVLQDGRIARFGERDEVLAK 543
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
59-286 4.36e-49

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: 172.90  E-value: 4.36e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPsrPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIG 138
Cdd:COG1122     1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPV--LFGTTIEENIRYG--HLDVTKEDIEQAAKMANAhdfIMDLpqkyETLVGERGAQLSGGQKQRIAIARALVR 214
Cdd:COG1122    79 LVFQNPDdqLFAPTVEEDVAFGpeNLGLPREEIRERVEEALE---LVGL----EHLADRPPHELSGGQKQRVAIAGVLAM 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 215 NPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIA-HRLSTI-KTADMIAGFKDGVVAEQGTHNELMSKQ 286
Cdd:COG1122   152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVtHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
60-273 1.14e-48

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: 1.14e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHFRYPSRpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGI 139
Cdd:cd03246     2 EVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 VSQEPVLFGTTIEENIryghldvtkedieqaakmanahdfimdlpqkyetlvgergaqLSGGQKQRIAIARALVRNPKIL 219
Cdd:cd03246    81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 220 LLDEATSALDTESEGIVQDALEKAS-HGRTTIVIAHRLSTIKTADMIAGFKDGVV 273
Cdd:cd03246   119 VLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASADRILVLEDGRV 173
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
79-226 1.98e-48

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: 168.21  E-value: 1.98e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  79 GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLF-GTTIEENIRY 157
Cdd:pfam00005   3 NVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENLRL 82
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 158 GHLDVTKEDIEQAAKMANAHDFiMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATS 226
Cdd:pfam00005  83 GLLLKGLSKREKDARAEEALEK-LGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
60-273 5.64e-47

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: 166.49  E-value: 5.64e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHFRYPSRPEaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGI 139
Cdd:cd03225     1 ELKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 VSQEP--VLFGTTIEENIRYG--HLDVTKEDIEQAAKMANAhDFIMDLPQKYETlvgergAQLSGGQKQRIAIARALVRN 215
Cdd:cd03225    80 VFQNPddQFFGPTVEEEVAFGleNLGLPEEEIEERVEEALE-LVGLEGLRDRSP------FTLSGGQKQRVAIAGVLAMD 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 216 PKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIA-HRLstiktaDMIAGFKDGVV 273
Cdd:cd03225   153 PDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVtHDL------DLLLELADRVI 205
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
378-822 6.06e-47

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 181.77  E-value: 6.06e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  378 SLVNGGAMPAFAVIFSEILgvfAILDEGEQERKIIqyvLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLR 457
Cdd:PTZ00265    69 ATISGGTLPFFVSVFGVIM---KNMNLGENVNDII---FSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFY 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  458 QEIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLgSSLMAFCSVVTGIVIGFVF-SWKITLLVIAFLPFVMIGGALEMQ 536
Cdd:PTZ00265   143 QDGQFHD--NNPGSKLTSDLDFYLEQVNAGIGTKF-ITIFTYASAFLGLYIWSLFkNARLTLCITCVFPLIYICGVICNK 219
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  537 MMQgaAGKNKEALESAGKIAI--ESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAA 614
Cdd:PTZ00265   220 KVK--INKKTSLLYNNNTMSIieEALVGIRTVVSYCGEKTILKKFNLSEKLYSKYILKANFMESLHIGMINGFILASYAF 297
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  615 SFWLGAYLI------KQSEVDY--VDVFKAFSAILFGGMAIGNASAFAPDAAKAEQSAKEIFKLIDKKPDIDNESEkGEQ 686
Cdd:PTZ00265   298 GFWYGTRIIisdlsnQQPNNDFhgGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDD-GKK 376
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  687 LHTFTaNLSFANIIFRYPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADG-IVSLDGHNLKDLNL 765
Cdd:PTZ00265   377 LKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGdIIINDSHNLKDINL 455
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  766 QWLRSQIGIVSQEPVLFDRTIAENIAY------------------------GDNSREV--------------TMD----- 802
Cdd:PTZ00265   456 KWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealsnyynedgndsqeNKNKRNScrakcagdlndmsnTTDsneli 535
                          490       500       510
                   ....*....|....*....|....*....|..
gi 2119559688  803 ------------EIIDAARKANIHNFIASLPD 822
Cdd:PTZ00265   536 emrknyqtikdsEVVDVSKKVLIHDFVSALPD 567
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
59-284 6.48e-47

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: 6.48e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRP--EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN---LKWW 133
Cdd:COG1123   261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 134 RENIGIVSQEPV--LF-GTTIEENIRYG---HLDVTKEDIEQAAKMAnahdfiMD---LPqkyETLVGERGAQLSGGQKQ 204
Cdd:COG1123   341 RRRVQMVFQDPYssLNpRMTVGDIIAEPlrlHGLLSRAERRERVAEL------LErvgLP---PDLADRYPHELSGGQRQ 411
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 205 RIAIARALVRNPKILLLDEATSALDTESEGIVQDALE--KASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGTHNE 281
Cdd:COG1123   412 RVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEE 491

                  ...
gi 2119559688 282 LMS 284
Cdd:COG1123   492 VFA 494
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
59-282 1.51e-46

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: 165.82  E-value: 1.51e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYD-----PEEGQILIDGVNL--KDINLK 131
Cdd:cd03260     1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIydLDVDVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 132 WWRENIGIVSQEPVLFGTTIEENIRYG---HL----DVTKEDIEQAAKMANAHDFIMDLPQkyetlvgerGAQLSGGQKQ 204
Cdd:cd03260    78 ELRRRVGMVFQKPNPFPGSIYDNVAYGlrlHGiklkEELDERVEEALRKAALWDEVKDRLH---------ALGLSGGQQQ 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 205 RIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIK-TADMIAGFKDGVVAEQGTHNEL 282
Cdd:cd03260   149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAArVADRTAFLLNGRLVEFGPTEQI 227
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
59-276 4.08e-46

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 164.45  E-value: 4.08e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPEA-KILYGVNLQIKRGQTVALVGSSGCGKST---IVQLLQRfydPEEGQILIDGVN---LKDINL- 130
Cdd:COG1136     5 LELRNLTKSYGTGEGEvTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDissLSERELa 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 131 KWWRENIGIVSQEPVLFGT-TIEENI----RYGHLDVtKEDIEQAAKMANAhdfiMDLpqkyETLVGERGAQLSGGQKQR 205
Cdd:COG1136    82 RLRRRHIGFVFQFFNLLPElTALENValplLLAGVSR-KERRERARELLER----VGL----GDRLDHRPSQLSGGQQQR 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 206 IAIARALVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQ 276
Cdd:COG1136   153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
694-822 4.05e-45

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: 162.01  E-value: 4.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRPDTtILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIG 773
Cdd:cd03251     1 VEFKNVTFRYPGDGPP-VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2119559688 774 IVSQEPVLFDRTIAENIAYGDnsREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:cd03251    80 LVSQDVFLFNDTVAENIAYGR--PGATREEVEEAARAANAHEFIMELPE 126
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
57-278 6.77e-45

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: 160.27  E-value: 6.77e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  57 GNVQIRGVHFRY-PSRPEakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRE 135
Cdd:cd03369     5 GEIEVENLSVRYaPDLPP--VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEPVLFGTTIEENI-RYGHLDvtKEDIEQAAKmanahdfimdlpqkyetlVGERGAQLSGGQKQRIAIARALVR 214
Cdd:cd03369    83 SLTIIPQDPTLFSGTIRSNLdPFDEYS--DEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLK 142
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 215 NPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGT 278
Cdd:cd03369   143 RPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
444-822 9.89e-45

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: 169.95  E-value: 9.89e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 444 TLR----LRSMSFKAMLRQEIAFFDDHNNsvGALTTRLATDASQVQG----------AAGIklgsslmafCSVVTGIVIG 509
Cdd:COG4987    83 TLRlladLRVRLYRRLEPLAPAGLARLRS--GDLLNRLVADVDALDNlylrvllpllVALL---------VILAAVAFLA 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 510 FvFSWKITLLVIAFLpfVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLT---REDMFQKKFN---HEL 583
Cdd:COG4987   152 F-FSPALALVLALGL--LLAGLLLPLLAARLGRRAGRRLAAARAALRARLTDLLQGAAELAaygALDRALARLDaaeARL 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 584 QmpyNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLIKQSEVDYVdvfkAFSAILFGGMAIGNASAFAPDAA----K 659
Cdd:COG4987   229 A---AAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGP----LLALLVLAALALFEALAPLPAAAqhlgR 301
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 660 AEQSAKEIFKLIDKKPDIDnESEKGEQLHTFTAnLSFANIIFRYPTRPdTTILKGLDLEVPQGQTVALVGSSGCGKSTTV 739
Cdd:COG4987   302 VRAAARRLNELLDAPPAVT-EPAEPAPAPGGPS-LELEDVSFRYPGAG-RPVLDGLSLTLPPGERVAIVGPSGSGKSTLL 378
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 740 QLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENIAYGDNsrEVTMDEIIDAARKANIHNFIAS 819
Cdd:COG4987   379 ALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARP--DATDEELWAALERVGLGDWLAA 456

                  ...
gi 2119559688 820 LPD 822
Cdd:COG4987   457 LPD 459
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
668-822 2.35e-44

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: 169.62  E-value: 2.35e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 668 FKLIDKKPDIdNESEKGEQLHTFTANLSFANIIFRYptRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYD 747
Cdd:COG5265   333 FDLLDQPPEV-ADAPDAPPLVVGGGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYD 409
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 748 PADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENIAYGDNsrEVTMDEIIDAARKANIHNFIASLPD 822
Cdd:COG5265   410 VTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRP--DASEEEVEAAARAAQIHDFIESLPD 482
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
59-277 6.28e-44

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: 158.44  E-value: 6.28e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPEA-KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN---LKWWR 134
Cdd:cd03257     2 LEVKNLSVSFPTGGGSvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 135 ENIGIVSQEPVL-------FGTTIEENIRYgHLDVTKEDIEQAAKMANAHDFIMDlpqkyETLVGERGAQLSGGQKQRIA 207
Cdd:cd03257    82 KEIQMVFQDPMSslnprmtIGEQIAEPLRI-HGKLSKKEARKEAVLLLLVGVGLP-----EEVLNRYPHELSGGQRQRVA 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 208 IARALVRNPKILLLDEATSALDTESEGIVQDALE--KASHGRTTIVIAHRLSTIK-TADMIAGFKDGVVAEQG 277
Cdd:cd03257   156 IARALALNPKLLIADEPTSALDVSVQAQILDLLKklQEELGLTLLFITHDLGVVAkIADRVAVMYAGKIVEEG 228
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
59-283 1.01e-43

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: 158.22  E-value: 1.01e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN---LKWWRE 135
Cdd:COG1127     6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEPVLFGT-TIEENIRYG---HLDVTKEDIEQAAKMANAhdfimdlpqkyetLVGERGA------QLSGGQKQR 205
Cdd:COG1127    83 RIGMLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELVLEKLE-------------LVGLPGAadkmpsELSGGMRKR 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 206 IAIARALVRNPKILLLDEATSALDTESEGIVqDAL---EKASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGTHNE 281
Cdd:COG1127   150 VALARALALDPEILLYDEPTAGLDPITSAVI-DELireLRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEE 228

                  ..
gi 2119559688 282 LM 283
Cdd:COG1127   229 LL 230
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
59-284 2.31e-43

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: 157.66  E-value: 2.31e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPEAK-ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENI 137
Cdd:COG1124     2 LEVRNLSVSYGQGGRRVpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 GIVSQEP---------VlfGTTIEENIRYGHLDVTKEDIEQAAKmanahdfIMDLPqkyETLVGERGAQLSGGQKQRIAI 208
Cdd:COG1124    82 QMVFQDPyaslhprhtV--DRILAEPLRIHGLPDREERIAELLE-------QVGLP---PSFLDRYPHQLSGGQRQRVAI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 209 ARALVRNPKILLLDEATSALDTesegIVQ----DALE--KASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGTHNE 281
Cdd:COG1124   150 ARALILEPELLLLDEPTSALDV----SVQaeilNLLKdlREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVAD 225

                  ...
gi 2119559688 282 LMS 284
Cdd:COG1124   226 LLA 228
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
59-277 3.50e-43

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: 155.76  E-value: 3.50e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDinLKWWRENIG 138
Cdd:cd03259     1 LELKGLSKTYGSVR---ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG--VPPERRNIG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFGT-TIEENIRYG--HLDVTKEDIEQAAKMANAHdfiMDLpqkyETLVGERGAQLSGGQKQRIAIARALVRN 215
Cdd:cd03259    76 MVFQDYALFPHlTVAENIAFGlkLRGVPKAEIRARVRELLEL---VGL----EGLLNRYPHELSGGQQQRVALARALARE 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 216 PKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLS-TIKTADMIAGFKDGVVAEQG 277
Cdd:cd03259   149 PSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
59-254 3.83e-43

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: 156.09  E-value: 3.83e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPEA-KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKwwrenI 137
Cdd:cd03293     1 LEVRNVSKTYGGGGGAvTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD-----R 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 GIVSQEPVLFG-TTIEENIRYGhLDVTKEDIEQAAkmANAHDFImdlpqkyeTLVGERGA------QLSGGQKQRIAIAR 210
Cdd:cd03293    76 GYVFQQDALLPwLTVLDNVALG-LELQGVPKAEAR--ERAEELL--------ELVGLSGFenayphQLSGGMRQRVALAR 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2119559688 211 ALVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAH 254
Cdd:cd03293   145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTH 190
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
60-271 4.47e-43

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: 153.55  E-value: 4.47e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGI 139
Cdd:cd00267     1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 VSQepvlfgttieeniryghldvtkedieqaakmanahdfimdlpqkyetlvgergaqLSGGQKQRIAIARALVRNPKIL 219
Cdd:cd00267    78 VPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 220 LLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTIKTA-DMIAGFKDG 271
Cdd:cd00267   103 LLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDG 156
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
59-278 4.76e-43

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 156.31  E-value: 4.76e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNL--KDINLKWWREN 136
Cdd:COG1126     2 IEIENLHKSFGDLE---VLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLFG-TTIEENIRYGHLDVTKEDIEQAAKMAnahdfiMDLPQKyetlVG--ERG----AQLSGGQKQRIAIA 209
Cdd:COG1126    79 VGMVFQQFNLFPhLTVLENVTLAPIKVKKMSKAEAEERA------MELLER----VGlaDKAdaypAQLSGGQQQRVAIA 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 210 RALVRNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGT 278
Cdd:COG1126   149 RALAMEPKVMLFDEPTSALDPELVGEVLDVMRDlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGP 219
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
59-286 7.52e-43

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: 156.36  E-value: 7.52e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIG 138
Cdd:COG1120     2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVL-FGTTIEENI---RYGHLD----VTKED---IEQAAKMANAHDFImdlpqkyETLVGErgaqLSGGQKQRIA 207
Cdd:COG1120    79 YVPQEPPApFGLTVRELValgRYPHLGlfgrPSAEDreaVEEALERTGLEHLA-------DRPVDE----LSGGERQRVL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 208 IARALVRNPKILLLDEATSALDtesegI-----VQDALEK--ASHGRTTIVIAHRLS-TIKTADMIAGFKDGVVAEQGTH 279
Cdd:COG1120   148 IARALAQEPPLLLLDEPTSHLD-----LahqleVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPP 222

                  ....*..
gi 2119559688 280 NELMSKQ 286
Cdd:COG1120   223 EEVLTPE 229
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
59-271 7.67e-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: 153.50  E-value: 7.67e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPsrpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKD--INLKWWREN 136
Cdd:cd03229     1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDleDELPPLRRR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLF-GTTIEENIRYGhldvtkedieqaakmanahdfimdlpqkyetlvgergaqLSGGQKQRIAIARALVRN 215
Cdd:cd03229    78 IGMVFQDFALFpHLTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 216 PKILLLDEATSALDTESEGIVQDALE--KASHGRTTIVIAHRLSTIKT-ADMIAGFKDG 271
Cdd:cd03229   119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
59-286 9.35e-43

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: 155.35  E-value: 9.35e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVN---LKDINLKWWRE 135
Cdd:cd03261     1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDisgLSEAELYRLRR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEPVLFGT-TIEENIRYG---HLDVTKEDIEQAAKManahdfimdlpqKYEtLVGERG------AQLSGGQKQR 205
Cdd:cd03261    78 RMGMLFQSGALFDSlTVFENVAFPlreHTRLSEEEIREIVLE------------KLE-AVGLRGaedlypAELSGGMKKR 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 206 IAIARALVRNPKILLLDEATSALDTESEGIVQDALE--KASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNEL 282
Cdd:cd03261   145 VALARALALDPELLLYDEPTAGLDPIASGVIDDLIRslKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEEL 224

                  ....
gi 2119559688 283 MSKQ 286
Cdd:cd03261   225 RASD 228
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
59-278 1.40e-42

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 158.72  E-value: 1.40e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDI-NLKWWRENI 137
Cdd:COG3842     6 LELENVSKRYGDVT---ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG---RDVtGLPPEKRNV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 GIVSQEPVLFG-TTIEENIRYG--HLDVTKEDIEQ-AAKMANahdfIMDLPQKYETLVgergAQLSGGQKQRIAIARALV 213
Cdd:COG3842    80 GMVFQDYALFPhLTVAENVAFGlrMRGVPKAEIRArVAELLE----LVGLEGLADRYP----HQLSGGQQQRVALARALA 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 214 RNPKILLLDEATSALDTESEGIVQDALeKASH---GRTTIVIAHRLS---TIktADMIAGFKDGVVAEQGT 278
Cdd:COG3842   152 PEPRVLLLDEPLSALDAKLREEMREEL-RRLQrelGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
59-273 2.29e-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: 153.80  E-value: 2.29e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPEA-KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWW---- 133
Cdd:cd03255     1 IELKNLSKTYGGGGEKvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 134 RENIGIVSQEPVLFGT-TIEENIRYGHL---DVTKEDIEQAAKMANahdfIMDLPQKYETLVgergAQLSGGQKQRIAIA 209
Cdd:cd03255    81 RRHIGFVFQSFNLLPDlTALENVELPLLlagVPKKERRERAEELLE----RVGLGDRLNHYP----SELSGGQQQRVAIA 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 210 RALVRNPKILLLDEATSALDTESEGIVQDALEKASH--GRTTIVIAHRLSTIKTADMIAGFKDGVV 273
Cdd:cd03255   153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
59-254 2.69e-42

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 154.86  E-value: 2.69e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPEAK-ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKwwrenI 137
Cdd:COG1116     8 LELRGVSKRFPTGGGGVtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD-----R 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 GIVSQEPVLFG-TTIEENIRYGhLDVTKEDIEQAAKMAnahdfimdlpQKYETLVGERGA------QLSGGQKQRIAIAR 210
Cdd:COG1116    83 GVVFQEPALLPwLTVLDNVALG-LELRGVPKAERRERA----------RELLELVGLAGFedayphQLSGGMRQRVAIAR 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2119559688 211 ALVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAH 254
Cdd:COG1116   152 ALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTH 197
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
60-287 3.36e-42

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: 154.25  E-value: 3.36e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWwRENIGI 139
Cdd:COG4555     3 EVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA-RRQIGV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 VSQEPVLF-GTTIEENIRY------GHLDVTKEDIEQAAKManahdfiMDLPQKYETLVGErgaqLSGGQKQRIAIARAL 212
Cdd:COG4555    79 LPDERGLYdRLTVRENIRYfaelygLFDEELKKRIEELIEL-------LGLEEFLDRRVGE----LSTGMKKKVALARAL 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 213 VRNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNELMSKQG 287
Cdd:COG4555   148 VHDPKVLLLDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVeALCDRVVILHKGKVVAQGSLDELREEIG 224
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
59-277 4.18e-42

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: 151.31  E-value: 4.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINlKWWRENIG 138
Cdd:cd03247     1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLIS 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFGTTIEENIryghldvtkedieqaakmanahdfimdlpqkyetlvgerGAQLSGGQKQRIAIARALVRNPKI 218
Cdd:cd03247    79 VLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPI 119
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 219 LLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQG 277
Cdd:cd03247   120 VLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
359-822 1.21e-41

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: 160.69  E-value: 1.21e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 359 RILKLNKSEAPFIVMGCFASLVNGGAMPAFAVIFSEILGvfAILDEGEQERKIIQYVLMFVGVGVISLIAYFVQGYMFGR 438
Cdd:COG4988     7 RLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLA--GLIIGGAPLSALLPLLGLLLAVLLLRALLAWLRERAAFR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 439 SGEYLTLRLRSMSFKAMLRQEIAFFDDHnnSVGALTTRLATDASQVQGAAGIKLGSslMAFCSVVTGIVIGFVF--SWKI 516
Cdd:COG4988    85 AAARVKRRLRRRLLEKLLALGPAWLRGK--STGELATLLTEGVEALDGYFARYLPQ--LFLAALVPLLILVAVFplDWLS 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 517 TLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHE-----------LQM 585
Cdd:COG4988   161 GLILLVTAPLIPLFMILVGKGAAKASRRQWRALARLSGHFLDRLRGLTTLKLFGRAKAEAERIAEAsedfrkrtmkvLRV 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 586 pyniALkkahligigfsLSQAVM-FFAYAASFWLGAYLIKQSEVDYVDVFKAFSAILfggMAignASAFAP--------- 655
Cdd:COG4988   241 ----AF-----------LSSAVLeFFASLSIALVAVYIGFRLLGGSLTLFAALFVLL---LA---PEFFLPlrdlgsfyh 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 656 DAAKAEQSAKEIFKLIDKKPDidnESEKGEQLHTFTAN--LSFANIIFRYPtrPDTTILKGLDLEVPQGQTVALVGSSGC 733
Cdd:COG4988   300 ARANGIAAAEKIFALLDAPEP---AAPAGTAPLPAAGPpsIELEDVSFSYP--GGRPALDGLSLTIPPGERVALVGPSGA 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 734 GKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENIAYGDnsREVTMDEIIDAARKANI 813
Cdd:COG4988   375 GKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGR--PDASDEELEAALEAAGL 452

                  ....*....
gi 2119559688 814 HNFIASLPD 822
Cdd:COG4988   453 DEFVAALPD 461
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
694-822 2.16e-40

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: 148.53  E-value: 2.16e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPtrPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIG 773
Cdd:cd03253     1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2119559688 774 IVSQEPVLFDRTIAENIAYGDNSreVTMDEIIDAARKANIHNFIASLPD 822
Cdd:cd03253    79 VVPQDTVLFNDTIGYNIRYGRPD--ATDEEVIEAAKAAQIHDKIMRFPD 125
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
59-285 3.36e-40

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 148.29  E-value: 3.36e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDiNLKWWRENIG 138
Cdd:COG1131     1 IEVRGLTKRYGDK---TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFGT-TIEENIRY-GHL-----DVTKEDIEQAAKManahdfiMDLPQKYETLVGergaQLSGGQKQRIAIARA 211
Cdd:COG1131    77 YVPQEPALYPDlTVRENLRFfARLyglprKEARERIDELLEL-------FGLTDAADRKVG----TLSGGMKQRLGLALA 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 212 LVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIA-HRLSTI-KTADMIAGFKDGVVAEQGTHNELMSK 285
Cdd:COG1131   146 LLHDPELLILDEPTSGLDPEARRELWELLRELAAEGKTVLLStHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
57-289 5.39e-40

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: 160.11  E-value: 5.39e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   57 GNVQIRGVHFRYpsRPEAK-ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRE 135
Cdd:TIGR00957 1283 GRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRF 1360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  136 NIGIVSQEPVLFGTTIEENIR-YGHLdvTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVR 214
Cdd:TIGR00957 1361 KITIIPQDPVLFSGSLRMNLDpFSQY--SDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLR 1438
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688  215 NPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIY 289
Cdd:TIGR00957 1439 KTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
59-284 6.69e-40

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: 154.68  E-value: 6.69e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPEAkILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPE---EGQILIDGVNLKDINLKWWRE 135
Cdd:COG1123     5 LEVRDLSVRYPGGDVP-AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEP--VLFGTTIEENIRYG--HLDVTKEDIEQAAKMANAHDFIMDLPQKYEtlvgergAQLSGGQKQRIAIARA 211
Cdd:COG1123    84 RIGMVFQDPmtQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEAVGLERRLDRYP-------HQLSGGQRQRVAIAMA 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 212 LVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNELMS 284
Cdd:COG1123   157 LALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
42-822 7.79e-40

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: 159.73  E-value: 7.79e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   42 IDSYSTEGKKLDNFQGN-VQIRGVHFRYpSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILI 120
Cdd:TIGR00957  619 LEPDSIERRTIKPGEGNsITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM 697
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  121 DGvNLKDINLKWWRENIGIvsQEPVLFGTTIEENiRYghldvtKEDIEQAAKMAnahDFIMdLPQKYETLVGERGAQLSG 200
Cdd:TIGR00957  698 KG-SVAYVPQQAWIQNDSL--RENILFGKALNEK-YY------QQVLEACALLP---DLEI-LPSGDRTEIGEKGVNLSG 763
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  201 GQKQRIAIARALVRNPKILLLDEATSALDTE-SEGIVQDAL--EKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQG 277
Cdd:TIGR00957  764 GQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMG 843
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  278 THNELMSKQGIYQQLV----TLQSMKSADDNEIEDFNRDDTKRPSLRHQKSTIDMTPKKLAQDKKEEIKEEEKGEKEEEV 353
Cdd:TIGR00957  844 SYQELLQRDGAFAEFLrtyaPDEQQGHLEDSWTALVSGEGKEAKLIENGMLVTDVVGKQLQRQLSASSSDSGDQSRHHGS 923
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  354 DASL---------GRILKLNKSEAPFIVMGCFASLVNG-GAMPAFAVIF-------SEILGVF--------AILDEGEQE 408
Cdd:TIGR00957  924 SAELqkaeakeetWKLMEADKAQTGQVELSVYWDYMKAiGLFITFLSIFlfvcnhvSALASNYwlslwtddPMVNGTQNN 1003
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  409 RKIIQYVlmFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRLATDASQVQGAA 488
Cdd:TIGR00957 1004 TSLRLSV--YGALGILQGFAVFGYSMAVSIGGIQASRVLHQDLLHNKLRSPMSFFE--RTPSGNLVNRFSKELDTVDSMI 1079
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  489 GIKLGSSLMAFCSVVTGIVIgFVFSWKITLLVIafLPFVMIggALEMQMMQGAAGKNKEALESAGKIAIES-IENIRTVA 567
Cdd:TIGR00957 1080 PPVIKMFMGSLFNVIGALIV-ILLATPIAAVII--PPLGLL--YFFVQRFYVASSRQLKRLESVSRSPVYShFNETLLGV 1154
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  568 SLTREDMFQKKFNHELQM----------PYNIAlKKAHLIGIGFSLSQAVMF---FAYAASFWLGAYLIKQSeVDYVDVF 634
Cdd:TIGR00957 1155 SVIRAFEEQERFIHQSDLkvdenqkayyPSIVA-NRWLAVRLECVGNCIVLFaalFAVISRHSLSAGLVGLS-VSYSLQV 1232
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  635 KAFSAILFGGMAIGNASAFAPDAAKA-EQSAKEIFKLIDKKPDIDNESEKGEqlhtftanLSFANIIFRYptRPDTT-IL 712
Cdd:TIGR00957 1233 TFYLNWLVRMSSEMETNIVAVERLKEySETEKEAPWQIQETAPPSGWPPRGR--------VEFRNYCLRY--REDLDlVL 1302
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  713 KGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENI-A 791
Cdd:TIGR00957 1303 RHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNLdP 1382
                          810       820       830
                   ....*....|....*....|....*....|.
gi 2119559688  792 YGDNSREvtmdEIIDAARKANIHNFIASLPD 822
Cdd:TIGR00957 1383 FSQYSDE----EVWWALELAHLKTFVSALPD 1409
ABC_6TM_TAP_ABCB8_10_like cd18557
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...
400-660 1.60e-39

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: 148.09  E-value: 1.60e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 400 AILDEGEQERkIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDHNnsVGALTTRLAT 479
Cdd:cd18557    25 TIIKGGDLDV-LNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLLRQEIAFFDKHK--TGELTSRLSS 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 480 DASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIES 559
Cdd:cd18557   102 DTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEES 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 560 IENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLIKQSEvdyVDVFKAFSA 639
Cdd:cd18557   182 LSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQ---LTVGELTSF 258
                         250       260
                  ....*....|....*....|....
gi 2119559688 640 ILFGGM---AIGNASAFAPDAAKA 660
Cdd:cd18557   259 ILYTIMvasSVGGLSSLLADIMKA 282
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
59-286 2.00e-39

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: 146.81  E-value: 2.00e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDI-NLKWWRENI 137
Cdd:TIGR04520   1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 GIVSQEP--VLFGTTIEENIRYG--HLDVTKEDI----EQAAKMANAHDFImdlpqKYETlvgergAQLSGGQKQRIAIA 209
Cdd:TIGR04520  80 GMVFQNPdnQFVGATVEDDVAFGleNLGVPREEMrkrvDEALKLVGMEDFR-----DREP------HLLSGGQKQRVAIA 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 210 RALVRNPKILLLDEATSALDTES-EGIVQDALE-KASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQ 286
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDPKGrKEVLETIRKlNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQV 227
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
59-282 5.16e-39

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 145.20  E-value: 5.16e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPEAkiLYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVN---LKDINLKWWRE 135
Cdd:COG3638     3 LELRNLSKRYPGGTPA--LDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDvtaLRGRALRRLRR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEPVLFG-TTIEENIRYGHLD-----------VTKEDIEQAakmanahdfimdlpqkYETL--VG------ERG 195
Cdd:COG3638    81 RIGMIFQQFNLVPrLSVLTNVLAGRLGrtstwrsllglFPPEDRERA----------------LEALerVGladkayQRA 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 196 AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKAS--HGRTTIVIAHRLSTIKT-ADMIAGFKDGV 272
Cdd:COG3638   145 DQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAreDGITVVVNLHQVDLARRyADRIIGLRDGR 224
                         250
                  ....*....|
gi 2119559688 273 VAEQGTHNEL 282
Cdd:COG3638   225 VVFDGPPAEL 234
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
59-285 6.09e-39

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: 144.26  E-value: 6.09e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRP-EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN---LKWWR 134
Cdd:cd03258     2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSgkeLRKAR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 135 ENIGIVSQEPVLFGT-TIEENIRYGhLDVTKEDIEQAAKMANAHDFIMDLPQKYETlvgeRGAQLSGGQKQRIAIARALV 213
Cdd:cd03258    82 RRIGMIFQHFNLLSSrTVFENVALP-LEIAGVPKAEIEERVLELLELVGLEDKADA----YPAQLSGGQKQRVGIARALA 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 214 RNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGTHNELMSK 285
Cdd:cd03258   157 NNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFAN 231
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
696-822 9.35e-39

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: 143.77  E-value: 9.35e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 696 FANIIFRYPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIV 775
Cdd:cd03248    14 FQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLV 93
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2119559688 776 SQEPVLFDRTIAENIAYGDNSreVTMDEIIDAARKANIHNFIASLPD 822
Cdd:cd03248    94 GQEPVLFARSLQDNIAYGLQS--CSFECVKEAAQKAHAHSFISELAS 138
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
59-271 1.45e-38

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: 142.22  E-value: 1.45e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPE--AKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlkdinlkwwreN 136
Cdd:cd03250     1 ISVEDASFTWDSGEQetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-------------S 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLFGTTIEENIRYGH-------LDVTK-----EDIEQaakmanahdfimdLPQKYETLVGERGAQLSGGQKQ 204
Cdd:cd03250    68 IAYVSQEPWIQNGTIRENILFGKpfdeeryEKVIKacalePDLEI-------------LPDGDLTEIGEKGINLSGGQKQ 134
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 205 RIAIARALVRNPKILLLDEATSALDTE-SEGIVQDAL-EKASHGRTTIVIAHRLSTIKTADMIAGFKDG 271
Cdd:cd03250   135 RISLARAVYSDADIYLLDDPLSAVDAHvGRHIFENCIlGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
401-822 1.88e-38

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 151.71  E-value: 1.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 401 ILDEG--EQERKIIQYV-LMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRL 477
Cdd:PRK11176   51 LLDDGfgKADRSVLKWMpLVVIGLMILRGITSFISSYCISWVSGKVVMTMRRRLFGHMMGMPVSFFD--KQSTGTLLSRI 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 478 ATDASQVQGAAG------IKLGSSLMAFCSVVtgivigFVFSWKITLLVIAFLPFVMIG-------------------GA 532
Cdd:PRK11176  129 TYDSEQVASSSSgalitvVREGASIIGLFIMM------FYYSWQLSLILIVIAPIVSIAirvvskrfrnisknmqntmGQ 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 533 LEM---QMMQGaagkNKEALESAGkiaiESIENIRtvasltredmFQKKFNHELQ--MPYNIALKKAHLIgIGFSLSQAV 607
Cdd:PRK11176  203 VTTsaeQMLKG----HKEVLIFGG----QEVETKR----------FDKVSNRMRQqgMKMVSASSISDPI-IQLIASLAL 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 608 MFFAYAASFwlgaYLIKQ--SEVDYVDVFKAFSAILFGGMAIGNASAFAPDAAKAEQSakeIFKLIDKKPDIDNESEKGE 685
Cdd:PRK11176  264 AFVLYAASF----PSVMDtlTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQT---LFAILDLEQEKDEGKRVIE 336
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 686 QLhtfTANLSFANIIFRYPTRpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNL 765
Cdd:PRK11176  337 RA---KGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTL 412
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 766 QWLRSQIGIVSQEPVLFDRTIAENIAYGDN---SREvtmdEIIDAARKANIHNFIASLPD 822
Cdd:PRK11176  413 ASLRNQVALVSQNVHLFNDTIANNIAYARTeqySRE----QIEEAARMAYAMDFINKMDN 468
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
59-283 6.18e-38

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: 142.05  E-value: 6.18e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPEAkiLYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIG 138
Cdd:cd03295     1 IEFENVTKRYGGGKKA--VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLF-GTTIEENIRY--GHLDVTKEDIEQAAKMANAhdfIMDLPQkyETLVGERGAQLSGGQKQRIAIARALVRN 215
Cdd:cd03295    79 YVIQQIGLFpHMTVEENIALvpKLLKWPKEKIRERADELLA---LVGLDP--AEFADRYPHELSGGQQQRVGVARALAAD 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 216 PKILLLDEATSALDTESEGIVQDALEKASH--GRTTIVIAHRL-STIKTADMIAGFKDGVVAEQGTHNELM 283
Cdd:cd03295   154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
59-253 8.44e-38

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 140.96  E-value: 8.44e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPEAkiLYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLK---WWRE 135
Cdd:COG2884     2 IRFENVSKRYPGGREA--LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipYLRR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQE-PVLFGTTIEENIRYGhLDVTKEDIEQAAKMANAhdfIMD---LPQKYETLVgergAQLSGGQKQRIAIARA 211
Cdd:COG2884    80 RIGVVFQDfRLLPDRTVYENVALP-LRVTGKSRKEIRRRVRE---VLDlvgLSDKAKALP----HELSGGEQQRVAIARA 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2119559688 212 LVRNPKILLLDEATSALDTE-SEGIVqDALEKASHGRTTIVIA 253
Cdd:COG2884   152 LVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRRGTTVLIA 193
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
59-278 1.04e-37

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 144.06  E-value: 1.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPEA-KILYGVNLQIKRGQTVALVGSSGCGKSTIVQ---LLQRfydPEEGQILIDGVNLKDIN---LK 131
Cdd:COG1135     2 IELENLSKTFPTKGGPvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRcinLLER---PTSGSVLVDGVDLTALSereLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 132 WWRENIGIVSQEPVLFGT-TIEENIRYG--HLDVTKEDIEQ-AAKMANahdfimdlpqkyetLVG--ERG----AQLSGG 201
Cdd:COG1135    79 AARRKIGMIFQHFNLLSSrTVAENVALPleIAGVPKAEIRKrVAELLE--------------LVGlsDKAdaypSQLSGG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 202 QKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGT 278
Cdd:COG1135   145 QKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDinRELGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
60-282 2.15e-37

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: 140.40  E-value: 2.15e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHFRYPSrpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGV---NLKDINLKWWREN 136
Cdd:cd03256     2 EVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinKLKGKALRQLRRQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLFG-TTIEENIRYGHLD-----------VTKEDIEQAAKMANAhdfiMDLPQKYETlvgeRGAQLSGGQKQ 204
Cdd:cd03256    80 IGMIFQQFNLIErLSVLENVLSGRLGrrstwrslfglFPKEEKQRALAALER----VGLLDKAYQ----RADQLSGGQQQ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 205 RIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKA--SHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGTHNE 281
Cdd:cd03256   152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGPPAE 231

                  .
gi 2119559688 282 L 282
Cdd:cd03256   232 L 232
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
59-273 5.26e-37

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: 138.05  E-value: 5.26e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG--VNLKDINLKWWREN 136
Cdd:cd03262     1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGlkLTDDKKNINELRQK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLFG-TTIEENIRYGHLDVTKEDIEQAAKMAnahdfiMDLPQKyetlVG------ERGAQLSGGQKQRIAIA 209
Cdd:cd03262    78 VGMVFQQFNLFPhLTVLENITLAPIKVKGMSKAEAEERA------LELLEK----VGladkadAYPAQLSGGQQQRVAIA 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 210 RALVRNPKILLLDEATSALDTESEGIVQDALEKASH-GRTTIVIAHRLSTI-KTADMIAGFKDGVV 273
Cdd:cd03262   148 RALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEeGMTMVVVTHEMGFArEVADRVIFMDDGRI 213
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
57-293 6.17e-37

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: 139.66  E-value: 6.17e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  57 GNVQIRGVHFRYPS--RPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWR 134
Cdd:cd03288    18 GEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 135 ENIGIVSQEPVLFGTTIEENIRyGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVR 214
Cdd:cd03288    95 SRLSIILQDPILFSGSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVR 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 215 NPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQ-GIYQQLV 293
Cdd:cd03288   174 KSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVFASLV 253
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
694-790 6.95e-37

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: 136.36  E-value: 6.95e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRPdTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIG 773
Cdd:cd03228     1 IEFKNVSFSYPGRP-KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
                          90
                  ....*....|....*..
gi 2119559688 774 IVSQEPVLFDRTIAENI 790
Cdd:cd03228    80 YVPQDPFLFSGTIRENI 96
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
59-282 1.83e-36

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: 140.19  E-value: 1.83e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRP-EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDP---EEGQILIDGVNL-----KDIN 129
Cdd:COG0444     2 LEVRNLKVYFPTRRgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLlklseKELR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 130 LKWWREnIGIVSQEP---------VlfGTTIEENIRYgHLDVTKEDIEQAAK-------MANAHDFIMDLPQkyetlvge 193
Cdd:COG0444    82 KIRGRE-IQMIFQDPmtslnpvmtV--GDQIAEPLRI-HGGLSKAEARERAIellervgLPDPERRLDRYPH-------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 194 rgaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTesegIVQ-DALE-----KASHGRTTIVIAHRLSTIK-TADMIA 266
Cdd:COG0444   150 ---ELSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQaQILNllkdlQRELGLAILFITHDLGVVAeIADRVA 222
                         250
                  ....*....|....*.
gi 2119559688 267 GFKDGVVAEQGTHNEL 282
Cdd:COG0444   223 VMYAGRIVEEGPVEEL 238
PLN03130 PLN03130
ABC transporter C family member; Provisional
57-287 2.19e-36

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 148.73  E-value: 2.19e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   57 GNVQIRGVHFRYpsRPE-AKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRE 135
Cdd:PLN03130  1236 GSIKFEDVVLRY--RPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  136 NIGIVSQEPVLFGTTIEENiryghLDVTKE----DIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARA 211
Cdd:PLN03130  1314 VLGIIPQAPVLFSGTVRFN-----LDPFNEhndaDLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARA 1388
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688  212 LVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQG 287
Cdd:PLN03130  1389 LLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
77-285 2.81e-36

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: 137.08  E-value: 2.81e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  77 LYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDI-NLKWWRENIGIVSQEPVLF-GTTIEEN 154
Cdd:cd03299    15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG---KDItNLPPEKRDISYVPQNYALFpHMTVYKN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 155 IRYG--HLDVTKEDIE----QAAKMAN-AHdfimdlpqkyetLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 227
Cdd:cd03299    92 IAYGlkKRKVDKKEIErkvlEIAEMLGiDH------------LLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 228 LDTESEGIVQDALEKASH--GRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGTHNELMSK 285
Cdd:cd03299   160 LDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
692-822 4.74e-36

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: 136.20  E-value: 4.74e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 692 ANLSFANIIFRYptRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQ 771
Cdd:cd03254     1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 772 IGIVSQEPVLFDRTIAENIAYGDNsrEVTMDEIIDAARKANIHNFIASLPD 822
Cdd:cd03254    79 IGVVLQDTFLFSGTIMENIRLGRP--NATDEEVIEAAKEAGAHDFIMKLPN 127
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
59-277 6.23e-36

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 136.71  E-value: 6.23e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYD--PE---EGQILIDGVNL--KDINLK 131
Cdd:COG1117    12 IEVRNLNVYYGDK---QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLDGEDIydPDVDVV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 132 WWRENIGIVSQEPVLFGTTIEENIRYG---HLDVTKEDI----EQAAKMANAHDfimdlpqkyEtlVGER----GAQLSG 200
Cdd:COG1117    89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlHGIKSKSELdeivEESLRKAALWD---------E--VKDRlkksALGLSG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 201 GQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKAShGRTTIVI-------AHRLStiktaDMIAGFKDGVV 273
Cdd:COG1117   158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELK-KDYTIVIvthnmqqAARVS-----DYTAFFYLGEL 231

                  ....
gi 2119559688 274 AEQG 277
Cdd:COG1117   232 VEFG 235
ABC_6TM_AtABCB27_like cd18780
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...
374-623 6.39e-36

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: 137.77  E-value: 6.39e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 374 GCFASLVNGGAMPAFAVIFSEIL-GVFAILDEGEQE--RKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSM 450
Cdd:cd18780     1 GTIALLVSSGTNLALPYFFGQVIdAVTNHSGSGGEEalRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 451 SFKAMLRQEIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIG 530
Cdd:cd18780    81 LFSAIIAQEIAFFD--VTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 531 GALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFF 610
Cdd:cd18780   159 AVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQL 238
                         250
                  ....*....|...
gi 2119559688 611 AYAASFWLGAYLI 623
Cdd:cd18780   239 AIVLVLWYGGRLV 251
ABC_6TM_exporters cd07346
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...
371-667 1.44e-35

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: 136.53  E-value: 1.44e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 371 IVMGCFASLVNGGAMPAFAVIFSeilgvfAILDEGEQERK---IIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRL 447
Cdd:cd07346     1 LLLALLLLLLATALGLALPLLTK------LLIDDVIPAGDlslLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 448 RSMSFKAMLRQEIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFV 527
Cdd:cd07346    75 RRDLFRHLQRLSLSFFD--RNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLY 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 528 MIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAV 607
Cdd:cd07346   153 VLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLL 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 608 MFFAYAASFWLGAYLIKQSEV---DYVdVFKAFSAILFGgmAIGNASAFAPDAAKAEQSAKEI 667
Cdd:cd07346   233 TALGTALVLLYGGYLVLQGSLtigELV-AFLAYLGMLFG--PIQRLANLYNQLQQALASLERI 292
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
59-286 1.68e-35

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 134.83  E-value: 1.68e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDINLKWWRenIG 138
Cdd:COG1121     7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG---KPPRRARRR--IG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVL---FGTTIEENI---RYGHL----DVTKED---IEQAAKMANAHDFImdlpqkyETLVGErgaqLSGGQKQR 205
Cdd:COG1121    79 YVPQRAEVdwdFPITVRDVVlmgRYGRRglfrRPSRADreaVDEALERVGLEDLA-------DRPIGE----LSGGQQQR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 206 IAIARALVRNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEqGTHNELM 283
Cdd:COG1121   148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GPPEEVL 226

                  ...
gi 2119559688 284 SKQ 286
Cdd:COG1121   227 TPE 229
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
59-229 5.83e-35

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 136.74  E-value: 5.83e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDIN-LKWWRENI 137
Cdd:COG3839     4 LELENVSKSYGGVE---ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG---RDVTdLPPKDRNI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 GIVSQEPVLFGT-TIEENIRYGhL---DVTKEDIEQ----AAKManahdfiMDLpqkyETLVGERGAQLSGGQKQRIAIA 209
Cdd:COG3839    78 AMVFQSYALYPHmTVYENIAFP-LklrKVPKAEIDRrvreAAEL-------LGL----EDLLDRKPKQLSGGQRQRVALG 145
                         170       180
                  ....*....|....*....|
gi 2119559688 210 RALVRNPKILLLDEATSALD 229
Cdd:COG3839   146 RALVREPKVFLLDEPLSNLD 165
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
59-273 1.35e-34

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: 129.83  E-value: 1.35e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDiNLKWWRENIG 138
Cdd:cd03230     1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFGT-TIEENIRYghldvtkedieqaakmanahdfimdlpqkyetlvgergaqlSGGQKQRIAIARALVRNPK 217
Cdd:cd03230    77 YLPEEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPE 115
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 218 ILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVV 273
Cdd:cd03230   116 LLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAeRLCDRVAILNNGRI 173
PLN03232 PLN03232
ABC transporter C family member; Provisional
57-287 2.91e-34

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 142.04  E-value: 2.91e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   57 GNVQIRGVHFRYpsRPE-AKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRE 135
Cdd:PLN03232  1233 GSIKFEDVHLRY--RPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRR 1310
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  136 NIGIVSQEPVLFGTTIEENIR--YGHLDVtkeDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALV 213
Cdd:PLN03232  1311 VLSIIPQSPVLFSGTVRFNIDpfSEHNDA---DLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALL 1387
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119559688  214 RNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQG 287
Cdd:PLN03232  1388 RRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
59-282 3.44e-34

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 134.12  E-value: 3.44e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLkDINLKWWRENIG 138
Cdd:COG1118     3 IEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPPRERRVG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFG-TTIEENIRYG--HLDVTKEDIEqaakmANAHDFI--MDLpqkyETLVGERGAQLSGGQKQRIAIARALV 213
Cdd:COG1118    79 FVFQHYALFPhMTVAENIAFGlrVRPPSKAEIR-----ARVEELLelVQL----EGLADRYPSQLSGGQRQRVALARALA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 214 RNPKILLLDEATSALDTEsegiVQDALEK---ASH---GRTTIVIAH------RLstiktADMIAGFKDGVVAEQGTHNE 281
Cdd:COG1118   150 VEPEVLLLDEPFGALDAK----VRKELRRwlrRLHdelGGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVGTPDE 220

                  .
gi 2119559688 282 L 282
Cdd:COG1118   221 V 221
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
80-283 3.66e-34

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: 132.00  E-value: 3.66e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRE----NIGIVSQEPVLF-GTTIEEN 154
Cdd:cd03294    43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTVLEN 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 155 IRYGhLDVT----KEDIEQAAK---MANAHDFIMDLPQkyetlvgergaQLSGGQKQRIAIARALVRNPKILLLDEATSA 227
Cdd:cd03294   123 VAFG-LEVQgvprAEREERAAEaleLVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSA 190
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 228 LDTESEGIVQDALEK--ASHGRTTIVIAHRLS-TIKTADMIAGFKDGVVAEQGTHNELM 283
Cdd:cd03294   191 LDPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249
cbiO PRK13650
energy-coupling factor transporter ATPase;
59-292 3.95e-34

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 132.16  E-value: 3.95e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIG 138
Cdd:PRK13650    5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEP--VLFGTTIEENIRYG------HLDVTKEDIEQAAKMANAHDFIMDLPqkyetlvgergAQLSGGQKQRIAIAR 210
Cdd:PRK13650   85 MVFQNPdnQFVGATVEDDVAFGlenkgiPHEEMKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 211 ALVRNPKILLLDEATSALDTESE----GIVQDAleKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQ 286
Cdd:PRK13650  154 AVAMRPKIIILDEATSMLDPEGRleliKTIKGI--RDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRG 231

                  ....*.
gi 2119559688 287 GIYQQL 292
Cdd:PRK13650  232 NDLLQL 237
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
52-283 5.04e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 131.65  E-value: 5.04e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  52 LDNFQGNVQIRGVHFRYPSRpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLK 131
Cdd:PRK13632    1 IKNKSVMIKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLK 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 132 WWRENIGIVSQEP--VLFGTTIEENIRYG------HLDVTKEDIEQAAKMANAHDFIMDLPQKyetlvgergaqLSGGQK 203
Cdd:PRK13632   80 EIRKKIGIIFQNPdnQFIGATVEDDIAFGlenkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQN-----------LSGGQK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 204 QRIAIARALVRNPKILLLDEATSALD----TESEGIVQDALEKAShgRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTH 279
Cdd:PRK13632  149 QRVAIASVLALNPEIIIFDESTSMLDpkgkREIKKIMVDLRKTRK--KTLISITHDMDEAILADKVIVFSEGKLIAQGKP 226

                  ....
gi 2119559688 280 NELM 283
Cdd:PRK13632  227 KEIL 230
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
60-277 1.50e-33

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: 127.17  E-value: 1.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGI 139
Cdd:cd03214     1 EVENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 VSqepvlfgttieeniryghldvtkedieQAAKMANAHDFImdlpqkyetlvgERG-AQLSGGQKQRIAIARALVRNPKI 218
Cdd:cd03214    78 VP---------------------------QALELLGLAHLA------------DRPfNELSGGERQRVLLARALAQEPPI 118
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 219 LLLDEATSALD--TESE--GIVQDalEKASHGRTTIVIAHRLS-TIKTADMIAGFKDGVVAEQG 277
Cdd:cd03214   119 LLLDEPTSHLDiaHQIEllELLRR--LARERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
79-285 1.79e-33

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 131.78  E-value: 1.79e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  79 GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN---LKWWRENIGIVSQEP---------Vl 146
Cdd:COG4608    36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDPyaslnprmtV- 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 147 fGTTIEENIRYgHLDVTKEDIEQAAKmanahdFIMDlpqkyetLVGERGA-------QLSGGQKQRIAIARALVRNPKIL 219
Cdd:COG4608   115 -GDIIAEPLRI-HGLASKAERRERVA------ELLE-------LVGLRPEhadryphEFSGGQRQRIGIARALALNPKLI 179
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 220 LLDEATSALDTeSegiVQdA-----LE--KASHGRTTIVIAHRLSTIK-TADMIAGFKDGVVAEQGTHNELMSK 285
Cdd:COG4608   180 VCDEPVSALDV-S---IQ-AqvlnlLEdlQDELGLTYLFISHDLSVVRhISDRVAVMYLGKIVEIAPRDELYAR 248
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
60-254 2.11e-33

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: 127.76  E-value: 2.11e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHFRYpsRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDINLKWWRENIGI 139
Cdd:cd03226     1 RIENISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 VSQEP--VLFGTTIEENIRYG--HLDVTKEDIEQAAKMANAHDFIMDLPQkyetlvgergaQLSGGQKQRIAIARALVRN 215
Cdd:cd03226    76 VMQDVdyQLFTDSVREELLLGlkELDAGNEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSG 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2119559688 216 PKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAH 254
Cdd:cd03226   145 KDLLIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITH 184
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
75-277 4.06e-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: 127.03  E-value: 4.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  75 KILYGVNLQIK---RGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKD----INLKWWRENIGIVSQEPVLF 147
Cdd:cd03297     8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 148 -GTTIEENIRYG-HLDVTKEDIEQAAKMANAhdfiMDLPQkyetLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEAT 225
Cdd:cd03297    88 pHLNVRENLAFGlKRKRNREDRISVDELLDL----LGLDH----LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 226 SALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQG 277
Cdd:cd03297   160 SALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
358-822 7.76e-33

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 134.70  E-value: 7.76e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 358 GRILKLNKSEAPFIVMGCFASLVNGGAMPAFAVIFSEILGVFAILDEgeqerkIIQYVLMFVGVGVISLIAY-FVqgymf 436
Cdd:PRK13657    8 ARVLQYLGAEKRLGILLAVANVLLAAATFAEPILFGRIIDAISGKGD------IFPLLAAWAGFGLFNIIAGvLV----- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 437 GRSGEYLTLRLR----SMSFKAMLRQEIAFfddH--NNSVGALTTRL-ATDAsqvqgAAGIKLG---SSLMAFCSVVTGI 506
Cdd:PRK13657   77 ARHADRLAHRRRlavlTEYFERIIQLPLAW---HsqRGSGRALHTLLrGTDA-----LFGLWLEfmrEHLATLVALVVLL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 507 VIGFVFSWKITLLVIAF-LPFVMIGgALEMQM---MQGAAGKNKEALESAgkiAIESIENIRTVASLTR---EDMFQKKF 579
Cdd:PRK13657  149 PLALFMNWRLSLVLVVLgIVYTLIT-TLVMRKtkdGQAAVEEHYHDLFAH---VSDAIGNVSVVQSYNRieaETQALRDI 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 580 NHEL---QMPyniALKKAHLIGIgfsLSQAVMFFAYAASFWLGAYLIKQSEVDYVDV--FKAFSAILFGgmAIGNASAFA 654
Cdd:PRK13657  225 ADNLlaaQMP---VLSWWALASV---LNRAASTITMLAILVLGAALVQKGQLRVGEVvaFVGFATLLIG--RLDQVVAFI 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 655 PDAAKAEQSAKEIFKLIDKKPDIdNESEKGEQLHTFTANLSFANIIFRYPTRPDTtiLKGLDLEVPQGQTVALVGSSGCG 734
Cdd:PRK13657  297 NQVFMAAPKLEEFFEVEDAVPDV-RDPPGAIDLGRVKGAVEFDDVSFSYDNSRQG--VEDVSFEAKPGQTVAIVGPTGAG 373
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 735 KSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENIAYGdnsRE-VTMDEIIDAARKANI 813
Cdd:PRK13657  374 KSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVG---RPdATDEEMRAAAERAQA 450

                  ....*....
gi 2119559688 814 HNFIASLPD 822
Cdd:PRK13657  451 HDFIERKPD 459
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
694-822 1.71e-32

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: 126.06  E-value: 1.71e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYptRPDTT-ILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQI 772
Cdd:cd03252     1 ITFEHVRFRY--KPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2119559688 773 GIVSQEPVLFDRTIAENIAYGDNSreVTMDEIIDAARKANIHNFIASLPD 822
Cdd:cd03252    79 GVVLQENVLFNRSIRDNIALADPG--MSMERVIEAAKLAGAHDFISELPE 126
PLN03232 PLN03232
ABC transporter C family member; Provisional
59-821 1.89e-32

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 136.26  E-value: 1.89e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   59 VQIRGVHFRYPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQ-LLQRFYDPEEGQILIDGvnlkdinlkwwreNI 137
Cdd:PLN03232   615 ISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRG-------------SV 681
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  138 GIVSQEPVLFGTTIEENIRYGHlDVTKEDIEQAAKM-ANAHDFIMdLPQKYETLVGERGAQLSGGQKQRIAIARALVRNP 216
Cdd:PLN03232   682 AYVPQVSWIFNATVRENILFGS-DFESERYWRAIDVtALQHDLDL-LPGRDLTEIGERGVNISGGQKQRVSMARAVYSNS 759
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  217 KILLLDEATSALDTESEGIVQDALEKAS-HGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLvtl 295
Cdd:PLN03232   760 DIYIFDDPLSALDAHVAHQVFDSCMKDElKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKL--- 836
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  296 qsMKSAddNEIEDFNRDDTKRPSLRHQ--KSTIDMTPKKLA--QDKKEEIKEEEKGEKEEEVDASLGRILKLNKSEAP-F 370
Cdd:PLN03232   837 --MENA--GKMDATQEVNTNDENILKLgpTVTIDVSERNLGstKQGKRGRSVLVKQEERETGIISWNVLMRYNKAVGGlW 912
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  371 IVMGCFASLVnggAMPAFAVIFSEILGVFAILDEGEQERK---IIQYVLMfvGVGVISLIayFVQGYMFGRSGEYLTLRL 447
Cdd:PLN03232   913 VVMILLVCYL---TTEVLRVSSSTWLSIWTDQSTPKSYSPgfyIVVYALL--GFGQVAVT--FTNSFWLISSSLHAAKRL 985
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  448 RSMSFKAMLRQEIAFFddHNNSVGALTTRLATDASQVQGAAGIKLGSSL-MAFCSVVTGIVIGFVFS---WKITLLVIAF 523
Cdd:PLN03232   986 HDAMLNSILRAPMLFF--HTNPTGRVINRFSKDIGDIDRNVANLMNMFMnQLWQLLSTFALIGTVSTislWAIMPLLILF 1063
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  524 LPFVMIGGALEMQMMQGAAGKNKEALESAGKiAIESIENIRTVASLTREDMFQKKFnhelqMPYNIALKKAHLIGIGF-- 601
Cdd:PLN03232  1064 YAAYLYYQSTSREVRRLDSVTRSPIYAQFGE-ALNGLSSIRAYKAYDRMAKINGKS-----MDNNIRFTLANTSSNRWlt 1137
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  602 --SLSQAVMFFAYAASFWLGAYLIKQSEVDYVDVFKAFSAILFGGMAIgnASAFAPDAAKAEQSAKEIFKL---ID---K 673
Cdd:PLN03232  1138 irLETLGGVMIWLTATFAVLRNGNAENQAGFASTMGLLLSYTLNITTL--LSGVLRQASKAENSLNSVERVgnyIDlpsE 1215
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  674 KPDIDnESEKGEQLHTFTANLSFANIIFRYptRPD-TTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGI 752
Cdd:PLN03232  1216 ATAII-ENNRPVSGWPSRGSIKFEDVHLRY--RPGlPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGR 1292
                          730       740       750       760       770       780
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688  753 VSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENIaygDNSREVTMDEIIDAARKANIHNFIASLP 821
Cdd:PLN03232  1293 IMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI---DPFSEHNDADLWEALERAHIKDVIDRNP 1358
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
60-274 3.65e-32

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: 124.18  E-value: 3.65e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDInlkwwRENIGI 139
Cdd:cd03235     1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGY 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 VSQEPVL---FGTTIEENI---RYGHL-------DVTKEDIEQAAKMANAHDFImdlpqkyETLVGErgaqLSGGQKQRI 206
Cdd:cd03235    73 VPQRRSIdrdFPISVRDVVlmgLYGHKglfrrlsKADKAKVDEALERVGLSELA-------DRQIGE----LSGGQQQRV 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 207 AIARALVRNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVA 274
Cdd:cd03235   142 LLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLLNRTVVA 211
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
59-253 4.15e-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: 124.06  E-value: 4.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPsrPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGV---NLKDINLKWWRE 135
Cdd:cd03292     1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQdvsDLRGRAIPYLRR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEPVLFGT-TIEENIRYGhLDVTKEDIEQAAKMANAHDFIMDLPQKYETLvgerGAQLSGGQKQRIAIARALVR 214
Cdd:cd03292    79 KIGVVFQDFRLLPDrNVYENVAFA-LEVTGVPPREIRKRVPAALELVGLSHKHRAL----PAELSGGEQQRVAIARAIVN 153
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2119559688 215 NPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIA 253
Cdd:cd03292   154 SPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVA 192
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
59-229 5.18e-32

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: 124.66  E-value: 5.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLkdINLKWWRENIG 138
Cdd:cd03300     1 IELENVSKFYGGFV---ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLF-GTTIEENIRYGhLDVTKEDI-EQAAKMANAHDFImdlpqKYETLVGERGAQLSGGQKQRIAIARALVRNP 216
Cdd:cd03300    76 TVFQNYALFpHLTVFENIAFG-LRLKKLPKaEIKERVAEALDLV-----QLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
                         170
                  ....*....|...
gi 2119559688 217 KILLLDEATSALD 229
Cdd:cd03300   150 KVLLLDEPLGALD 162
cbiO PRK13637
energy-coupling factor transporter ATPase;
59-298 5.66e-32

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 126.32  E-value: 5.66e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRY-PSRP-EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNL--KDINLKWWR 134
Cdd:PRK13637    3 IKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 135 ENIGIVSQEP--VLFGTTIEENIRYG--HLDVTKEDIEQAAKMAnahdfiMDLPQ-KYETLVGERGAQLSGGQKQRIAIA 209
Cdd:PRK13637   83 KKVGLVFQYPeyQLFEETIEKDIAFGpiNLGLSEEEIENRVKRA------MNIVGlDYEDYKDKSPFELSGGQKRRVAIA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 210 RALVRNPKILLLDEATSALDTESEgivQDALEKAS-----HGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNElm 283
Cdd:PRK13637  157 GVVAMEPKILILDEPTAGLDPKGR---DEILNKIKelhkeYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPRE-- 231
                         250
                  ....*....|....*
gi 2119559688 284 skqgIYQQLVTLQSM 298
Cdd:PRK13637  232 ----VFKEVETLESI 242
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
59-284 6.03e-32

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 125.90  E-value: 6.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLkwW--REN 136
Cdd:PRK13635    6 IRVEHISFRYPDA-ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETV--WdvRRQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEP--VLFGTTIEENIRYG--HLDVTKED----IEQAAKMANAHDFIMDLPqkyetlvgergAQLSGGQKQRIAI 208
Cdd:PRK13635   83 VGMVFQNPdnQFVGATVQDDVAFGleNIGVPREEmverVDQALRQVGMEDFLNREP-----------HRLSGGQKQRVAI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 209 ARALVRNPKILLLDEATSALDTESEgivQDALE-----KASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELM 283
Cdd:PRK13635  152 AGVLALQPDIIILDEATSMLDPRGR---REVLEtvrqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIF 228

                  .
gi 2119559688 284 S 284
Cdd:PRK13635  229 K 229
ABC_6TM_ABCB10_like cd18573
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...
413-627 7.77e-32

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: 126.09  E-value: 7.77e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 413 QYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDhnNSVGALTTRLATDASQVQGAAGIKL 492
Cdd:cd18573    42 TFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRLFKSILRQDAAFFDK--NKTGELVSRLSSDTSVVGKSLTQNL 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 493 GSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTRE 572
Cdd:cd18573   120 SDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAE 199
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 573 DMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLIKQSE 627
Cdd:cd18573   200 RKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGE 254
ABC_6TM_bac_exporter_ABCB8_10_like cd18576
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
411-654 1.13e-30

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: 122.21  E-value: 1.13e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 411 IIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFddHNNSVGALTTRLATDASQVQGAagi 490
Cdd:cd18576    35 LNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQRLPLSFF--HERRVGELTSRLSNDVTQIQDT--- 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 491 kLGSSLMAFCS----VVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTV 566
Cdd:cd18576   110 -LTTTLAEFLRqiltLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVV 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 567 ASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLIKQSEVDYVDVFkAFsaILFGGMA 646
Cdd:cd18576   189 KAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLV-AF--LLYTLFI 265

                  ....*...
gi 2119559688 647 IGNASAFA 654
Cdd:cd18576   266 AGSIGSLA 273
PLN03130 PLN03130
ABC transporter C family member; Provisional
59-790 2.15e-30

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 129.47  E-value: 2.15e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   59 VQIRGVHFRYPSRPEAKILYGVNLQIKRGQTVALVGSSGCGK-STIVQLLQRFYDPEEGQILIDGvnlkdinlkwwreNI 137
Cdd:PLN03130   615 ISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKtSLISAMLGELPPRSDASVVIRG-------------TV 681
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  138 GIVSQEPVLFGTTIEENIRYGhLDVTKEDIEQAAKMAN-AHDFIMdLPQKYETLVGERGAQLSGGQKQRIAIARALVRNP 216
Cdd:PLN03130   682 AYVPQVSWIFNATVRDNILFG-SPFDPERYERAIDVTAlQHDLDL-LPGGDLTEIGERGVNISGGQKQRVSMARAVYSNS 759
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  217 KILLLDEATSALDTESEGIVQDA-LEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLV-T 294
Cdd:PLN03130   760 DVYIFDDPLSALDAHVGRQVFDKcIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMeN 839
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  295 LQSMKSADDNEIEdFNRDDT-------KRPSLRHQKSTIDMTPKKlaqdkKEEIKEEEKGEKEEEVDAslgRILKLNKSE 367
Cdd:PLN03130   840 AGKMEEYVEENGE-EEDDQTsskpvanGNANNLKKDSSSKKKSKE-----GKSVLIKQEERETGVVSW---KVLERYKNA 910
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  368 --APFIVMGCFASLVnggAMPAFAVIFSEILGVFAilDEGE-QERKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLT 444
Cdd:PLN03130   911 lgGAWVVMILFLCYV---LTEVFRVSSSTWLSEWT--DQGTpKTHGPLFYNLIYALLSFGQVLVTLLNSYWLIMSSLYAA 985
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  445 LRLRSMSFKAMLRQEIAFFddHNNSVGALTTRLATDASQ----VQGAAGIKLGSslmAFCSVVTGIVIGFVFS---WKIT 517
Cdd:PLN03130   986 KRLHDAMLGSILRAPMSFF--HTNPLGRIINRFAKDLGDidrnVAVFVNMFLGQ---IFQLLSTFVLIGIVSTislWAIM 1060
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  518 LLVIAFLpfvmiGGALEMQmmqgaagknkealesagkiaiESIENIRTVASLTREDMFqKKFNHELQMPYNIALKKAH-- 595
Cdd:PLN03130  1061 PLLVLFY-----GAYLYYQ---------------------STAREVKRLDSITRSPVY-AQFGEALNGLSTIRAYKAYdr 1113
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  596 LIGI-GFSLSQAVMF--FAYAASFWLGaylIKQSEVDYVDVFKAFSAILFGGMAIGNASAFAPD---------------- 656
Cdd:PLN03130  1114 MAEInGRSMDNNIRFtlVNMSSNRWLA---IRLETLGGLMIWLTASFAVMQNGRAENQAAFASTmglllsyalnitsllt 1190
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  657 -----AAKAEQSakeiFKLIDKKPD-IDNESEKGEQLHT--------FTANLSFANIIFRYptRPD-TTILKGLDLEVPQ 721
Cdd:PLN03130  1191 avlrlASLAENS----LNAVERVGTyIDLPSEAPLVIENnrpppgwpSSGSIKFEDVVLRY--RPElPPVLHGLSFEISP 1264
                          730       740       750       760       770       780
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688  722 GQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENI 790
Cdd:PLN03130  1265 SEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNL 1333
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
59-278 3.05e-30

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 123.52  E-value: 3.05e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKwwRENIG 138
Cdd:PRK09452   15 VELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVN 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLF-GTTIEENIRYGhL---DVTKEDIE----QAAKMAnahdfimdlpqKYETLVGERGAQLSGGQKQRIAIAR 210
Cdd:PRK09452   90 TVFQSYALFpHMTVFENVAFG-LrmqKTPAAEITprvmEALRMV-----------QLEEFAQRKPHQLSGGQQQRVAIAR 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 211 ALVRNPKILLLDEATSALDTESEGIVQDALeKASH---GRTTIVIAH-RLSTIKTADMIAGFKDGVVAEQGT 278
Cdd:PRK09452  158 AVVNKPKVLLLDESLSALDYKLRKQMQNEL-KALQrklGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
59-277 3.49e-30

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: 118.51  E-value: 3.49e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKwwRENIG 138
Cdd:cd03301     1 VELENVTKRFGNV---TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLF-GTTIEENIRYG------HLDVTKEDIEQAAKMAnahdfimdlpqKYETLVGERGAQLSGGQKQRIAIARA 211
Cdd:cd03301    76 MVFQNYALYpHMTVYDNIAFGlklrkvPKDEIDERVREVAELL-----------QIEHLLDRKPKQLSGGQRQRVALGRA 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 212 LVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAH-RLSTIKTADMIAGFKDGVVAEQG 277
Cdd:cd03301   145 IVREPKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
369-822 3.64e-30

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: 125.86  E-value: 3.64e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 369 PFIVMGCFASLVNGGAMPAFAVIFSEIL-GVFAildEGEQERKIIQYVLMFVGVGVI-SLIAYFvQGYMFGRSGEYLTLR 446
Cdd:TIGR02857   3 RALALLALLGVLGALLIIAQAWLLARVVdGLIS---AGEPLAELLPALGALALVLLLrALLGWL-QERAAARAAAAVKSQ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 447 LRSMSFKAMLRQEIAffDDHNNSVGALTTRLATDASQVQG-AAGIKLGSSLMAFCSVVTGIVIgFVFSWKITLLVIAFLP 525
Cdd:TIGR02857  79 LRERLLEAVAALGPR--WLQGRPSGELATLALEGVEALDGyFARYLPQLVLAVIVPLAILAAV-FPQDWISGLILLLTAP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 526 FVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQmpyniALKKAHL--IGIGFsL 603
Cdd:TIGR02857 156 LIPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSE-----EYRERTMrvLRIAF-L 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 604 SQAVMFFAYAASfwlgaylikqseVDYVDVFKAFSaILFGGMAIGNA--------SAFAP---------DAAKAEQSAKE 666
Cdd:TIGR02857 230 SSAVLELFATLS------------VALVAVYIGFR-LLAGDLDLATGlfvlllapEFYLPlrqlgaqyhARADGVAAAEA 296
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 667 IFKLIDKKPDIdnESEKGEQLHTFTANLSFANIIFRYPTRpdTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFY 746
Cdd:TIGR02857 297 LFAVLDAAPRP--LAGKAPVTAAPASSLEFSGVSVAYPGR--RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFV 372
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 747 DPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENIAYGDnsREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:TIGR02857 373 DPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLAR--PDASDAEIREALERAGLDEFVAALPQ 446
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
59-278 5.66e-30

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 121.83  E-value: 5.66e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPEAKI-LYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVN---LKDINLKWWR 134
Cdd:PRK11153    2 IELKNISKVFPQGGRTIHaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDltaLSEKELRKAR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 135 ENIGIVSQE-PVLFGTTIEENIRY-----GhldVTKEDIEqaAKMANAHDF--IMDLPQKYEtlvgergAQLSGGQKQRI 206
Cdd:PRK11153   82 RQIGMIFQHfNLLSSRTVFDNVALplelaG---TPKAEIK--ARVTELLELvgLSDKADRYP-------AQLSGGQKQRV 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 207 AIARALVRNPKILLLDEATSALDTESEGIVQDALEKASH--GRTTIVIAHRLSTIK-TADMIAGFKDGVVAEQGT 278
Cdd:PRK11153  150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKrICDRVAVIDAGRLVEQGT 224
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
59-283 5.78e-30

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: 119.03  E-value: 5.78e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQ---IL---IDGVNLKDInlkw 132
Cdd:COG1119     4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvrLFgerRGGEDVWEL---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 133 wRENIGIVS---QEPVLFGTTIEENI---------RYGHldVTKEDIEQAAKMANAhdfiMDLpqkyETLVGERGAQLSG 200
Cdd:COG1119    77 -RKRIGLVSpalQLRFPRDETVLDVVlsgffdsigLYRE--PTDEQRERARELLEL----LGL----AHLADRPFGTLSQ 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 201 GQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIV-IAHRLStiktaDMIAGF------KDGV 272
Cdd:COG1119   146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVE-----EIPPGIthvlllKDGR 220
                         250
                  ....*....|.
gi 2119559688 273 VAEQGTHNELM 283
Cdd:COG1119   221 VVAAGPKEEVL 231
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
59-254 6.73e-30

ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 117.58  E-value: 6.73e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWwRENIG 138
Cdd:COG4133     3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFGT-TIEENIRY----GHLDVTKEDIEQAAKmanahdfIMDLpQKYETLvgeRGAQLSGGQKQRIAIARALV 213
Cdd:COG4133    79 YLGHADGLKPElTVRENLRFwaalYGLRADREAIDEALE-------AVGL-AGLADL---PVRQLSAGQKRRVALARLLL 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2119559688 214 RNPKILLLDEATSALDTESEGIVQDAL-EKASHGRTTIVIAH 254
Cdd:COG4133   148 SPAPLWLLDEPFTALDAAGVALLAELIaAHLARGGAVLLTTH 189
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
79-284 1.01e-29

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: 124.41  E-value: 1.01e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  79 GVNLQIKRGQTVALVGSSGCGKST----IVQLLqrfydPEEGQILIDGVNLKDIN---LKWWRENIGIVSQEPvlFGT-- 149
Cdd:COG4172   304 GVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--FGSls 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 150 ---TIEENIRYG----HLDVTKEDIEQAAKMAnahdfiMD---LP----QKYEtlvgergAQLSGGQKQRIAIARALVRN 215
Cdd:COG4172   377 prmTVGQIIAEGlrvhGPGLSAAERRARVAEA------LEevgLDpaarHRYP-------HEFSGGQRQRIAIARALILE 443
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 216 PKILLLDEATSALDTesegIVQ----DALEK--ASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGTHNELMS 284
Cdd:COG4172   444 PKLLVLDEPTSALDV----SVQaqilDLLRDlqREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTEQVFD 515
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
73-284 1.08e-29

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 118.27  E-value: 1.08e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  73 EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKD--INLKWWRENIGIVSQEPVLF-GT 149
Cdd:PRK09493   13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkVDERLIRQEAGMVFQQFYLFpHL 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 150 TIEENIRYGHLDVtkedieQAAKMANAHDFIMDLPQKyetlVG--ERG----AQLSGGQKQRIAIARALVRNPKILLLDE 223
Cdd:PRK09493   93 TALENVMFGPLRV------RGASKEEAEKQARELLAK----VGlaERAhhypSELSGGQQQRVAIARALAVKPKLMLFDE 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 224 ATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLS-TIKTADMIAGFKDGVVAEQGTHNELMS 284
Cdd:PRK09493  163 PTSALDPELRHEVLKVMQDlAEEGMTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQVLIK 225
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
59-282 2.66e-29

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 122.82  E-value: 2.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSrpeAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG--VNLKDInLKWWREN 136
Cdd:COG1129     5 LEMRGISKSFGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSP-RDAQAAG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLFGT-TIEENIRYGHLDVT------KEDIEQAAKMANAHDFIMDLpqkyETLVGErgaqLSGGQKQRIAIA 209
Cdd:COG1129    81 IAIIHQELNLVPNlSVAENIFLGREPRRgglidwRAMRRRARELLARLGLDIDP----DTPVGD----LSVAQQQLVEIA 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 210 RALVRNPKILLLDEATSAL-DTESE---GIVQDaLekASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGTHNEL 282
Cdd:COG1129   153 RALSRDARVLILDEPTASLtEREVErlfRIIRR-L--KAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
58-284 4.73e-29

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 116.01  E-value: 4.73e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  58 NVQIRGVHFRYPSRP-EAkilygvNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKwwREN 136
Cdd:COG3840     1 MLRLDDLTYRYGDFPlRF------DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--ERP 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLFG-TTIEENIRYG-----HLDVT-KEDIEQAAKMANAHDFIMDLPqkyetlvgergAQLSGGQKQRIAIA 209
Cdd:COG3840    73 VSMLFQENNLFPhLTVAQNIGLGlrpglKLTAEqRAQVEQALERVGLAGLLDRLP-----------GQLSGGQRQRVALA 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 210 RALVRNPKILLLDEATSALD----TESEGIVQDALekASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGTHNELMS 284
Cdd:COG3840   142 RCLVRKRPILLLDEPFSALDpalrQEMLDLVDELC--RERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLD 219
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
59-282 5.32e-29

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: 115.90  E-value: 5.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSrpeAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKwwRENIG 138
Cdd:cd03296     3 IEVRNVSKRFGD---FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFG-TTIEENIRYGhLDVTK--EDIEQAAKMANAHDfIMDLPQkYETLVGERGAQLSGGQKQRIAIARALVRN 215
Cdd:cd03296    78 FVFQHYALFRhMTVFDNVAFG-LRVKPrsERPPEAEIRAKVHE-LLKLVQ-LDWLADRYPAQLSGGQRQRVALARALAVE 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 216 PKILLLDEATSALDTESEGIVQDALEKASH--GRTTIVIAHRLS-TIKTADMIAGFKDGVVAEQGTHNEL 282
Cdd:cd03296   155 PKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
59-274 5.91e-29

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: 113.29  E-value: 5.91e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSrpeAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlkdinlkwwrenig 138
Cdd:cd03216     1 LELRGITKRFGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG---------------- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 ivsqEPVLFGTTIEEniryghldvtkedieQAAKMANAHdfimdlpqkyetlvgergaQLSGGQKQRIAIARALVRNPKI 218
Cdd:cd03216    62 ----KEVSFASPRDA---------------RRAGIAMVY-------------------QLSVGERQMVEIARALARNARL 103
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 219 LLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVA 274
Cdd:cd03216   104 LILDEPTAALTPAEVERLFKVIRRlRAQGVAVIFISHRLDEVfEIADRVTVLRDGRVV 161
ABC_6TM_TAP cd18572
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...
398-628 9.67e-29

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: 116.87  E-value: 9.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 398 VFAILDEGEQErKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDhnNSVGALTTRL 477
Cdd:cd18572    23 IDAVVADGSRE-AFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLLRQDIAFFDA--TKTGELTSRL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 478 ATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAI 557
Cdd:cd18572   100 TSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAE 179
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 558 ESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLIKQSEV 628
Cdd:cd18572   180 EALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRM 250
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
80-229 1.80e-28

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 117.51  E-value: 1.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKwwRENIGIVSQEPVLF-GTTIEENIRYG 158
Cdd:PRK11432   25 LNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSLGENVGYG 102
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 159 --HLDVTKEDIEQAAKMANAhdfIMDLPQKYETLVGergaQLSGGQKQRIAIARALVRNPKILLLDEATSALD 229
Cdd:PRK11432  103 lkMLGVPKEERKQRVKEALE---LVDLAGFEDRYVD----QISGGQQQRVALARALILKPKVLLFDEPLSNLD 168
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
69-278 2.41e-28

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: 112.64  E-value: 2.41e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  69 PSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLL--QRFYDPEEGQILIDGVNLKdinLKWWRENIGIVSQEPVL 146
Cdd:cd03213    17 PSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---KRSFRKIIGYVPQDDIL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 147 FGT-TIEENIRYghldvtkedieqAAKManahdfimdlpqkyetlvgeRGaqLSGGQKQRIAIARALVRNPKILLLDEAT 225
Cdd:cd03213    94 HPTlTVRETLMF------------AAKL--------------------RG--LSGGERKRVSIALELVSNPSLLFLDEPT 139
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 226 SALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTiktaDMIAGFKDGVVAEQGT 278
Cdd:cd03213   140 SGLDSSSALQVMSLLRRlADTGRTIICSIHQPSS----EIFELFDKLLLLSQGR 189
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
59-277 7.01e-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: 111.90  E-value: 7.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRpeaKILYGVNLQIKRGQTvALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDiNLKWWRENIG 138
Cdd:cd03264     1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLF-GTTIEENIRYGHL--DVTKEDIEQAAKMANAHdfiMDLPQKYETLVGergaQLSGGQKQRIAIARALVRN 215
Cdd:cd03264    76 YLPQEFGVYpNFTVREFLDYIAWlkGIPSKEVKARVDEVLEL---VNLGDRAKKKIG----SLSGGMRRRVGIAQALVGD 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 216 PKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIK-TADMIAGFKDGVVAEQG 277
Cdd:cd03264   149 PSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVEsLCNQVAVLNKGKLVFEG 211
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
59-286 7.23e-28

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 113.33  E-value: 7.23e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYD--PE---EGQILIDGVNL-----KDI 128
Cdd:PRK14239    6 LQVSDLSVYYNKK---KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIysprtDTV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 129 NLkwwRENIGIVSQEPVLFGTTIEENIRYG-------HLDVTKEDIEQAAKMANAHDFIMDlpQKYETLVGergaqLSGG 201
Cdd:PRK14239   83 DL---RKEIGMVFQQPNPFPMSIYENVVYGlrlkgikDKQVLDEAVEKSLKGASIWDEVKD--RLHDSALG-----LSGG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 202 QKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQG-TH 279
Cdd:PRK14239  153 QQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNdTK 232

                  ....*..
gi 2119559688 280 NELMSKQ 286
Cdd:PRK14239  233 QMFMNPK 239
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
59-286 9.91e-28

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 113.31  E-value: 9.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSrPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIG 138
Cdd:PRK13648    8 IVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEP--VLFGTTIEENIRYG---HL---DVTKEDIEQAAKMANAHDFIMDLPQkyetlvgergaQLSGGQKQRIAIAR 210
Cdd:PRK13648   87 IVFQNPdnQFVGSIVKYDVAFGlenHAvpyDEMHRRVSEALKQVDMLERADYEPN-----------ALSGGQKQRVAIAG 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 211 ALVRNPKILLLDEATSALDTESEGIVQDALE--KASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQ 286
Cdd:PRK13648  156 VLALNPSVIILDEATSMLDPDARQNLLDLVRkvKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
60-263 1.14e-27

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 111.73  E-value: 1.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGI 139
Cdd:PRK10247    9 QLQNVGYLAGDA---KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSY 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 VSQEPVLFGTTIEENIRYGHLdVTKEDIEQAAKMANAHDFimDLPqkyETLVGERGAQLSGGQKQRIAIARALVRNPKIL 219
Cdd:PRK10247   86 CAQTPTLFGDTVYDNLIFPWQ-IRNQQPDPAIFLDDLERF--ALP---DTILTKNIAELSGGEKQRISLIRNLQFMPKVL 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2119559688 220 LLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTIKTAD 263
Cdd:PRK10247  160 LLDEITSALDESNKHNVNEIIHRyvREQNIAVLWVTHDKDEINHAD 205
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
59-282 2.31e-27

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: 110.67  E-value: 2.31e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPEaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDiNLKWWRENIG 138
Cdd:cd03263     1 LQIRNLTKTYKKGTK-PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFGT-TIEENIRY------GHLDVTKEDIEQAAKManahdfiMDLPQKYETLVGergaQLSGGQKQRIAIARA 211
Cdd:cd03263    79 YCPQFDALFDElTVREHLRFyarlkgLPKSEIKEEVELLLRV-------LGLTDKANKRAR----TLSGGMKRKLSLAIA 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 212 LVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAH------RLstiktADMIAGFKDGVVAEQGTHNEL 282
Cdd:cd03263   148 LIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHsmdeaeAL-----CDRIAIMSDGKLRCIGSPQEL 219
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
60-284 2.46e-27

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: 110.60  E-value: 2.46e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHFRYPsrpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLK-----DINlkwwR 134
Cdd:cd03224     2 EVENLNAGYG---KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITglpphERA----R 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 135 ENIGIVSQEPVLFGT-TIEENIRYGHLDVTKEDIEQAAkmanahDFIMDL-PQKYETLvGERGAQLSGGQKQRIAIARAL 212
Cdd:cd03224    75 AGIGYVPEGRRIFPElTVEENLLLGAYARRRAKRKARL------ERVYELfPRLKERR-KQLAGTLSGGEQQMLAIARAL 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 213 VRNPKILLLDEATSALdteSEGIVQ---DALEK-ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNELMS 284
Cdd:cd03224   148 MSRPKLLLLDEPSEGL---APKIVEeifEAIRElRDEGVTILLVEQNARFAlEIADRAYVLERGRVVLEGTAAELLA 221
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
59-254 2.55e-27

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: 110.99  E-value: 2.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPEA-KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN----LKWW 133
Cdd:COG4181     9 IELRGLTKTVGTGAGElTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarARLR 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 134 RENIGIVSQEPVLFGT-TIEENI-----RYGHldvtKEDIEQAAKMANAhdfiMDLpqkyetlvGERG----AQLSGGQK 203
Cdd:COG4181    89 ARHVGFVFQSFQLLPTlTALENVmlpleLAGR----RDARARARALLER----VGL--------GHRLdhypAQLSGGEQ 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 204 QRIAIARALVRNPKILLLDEATSALDTESEGIVQDALE--KASHGRTTIVIAH 254
Cdd:COG4181   153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFelNRERGTTLVLVTH 205
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
80-254 2.89e-27

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 114.55  E-value: 2.89e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDInlKWWRENIGIVSQEPVLF-GTTIEENIRYG 158
Cdd:PRK11607   38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHV--PPYQRPINMMFQSYALFpHMTVEQNIAFG 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 159 hldvTKEDIEQAAKMANAHDFIMDLPQKYEtLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQ- 237
Cdd:PRK11607  116 ----LKQDKLPKAEIASRVNEMLGLVHMQE-FAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQl 190
                         170       180
                  ....*....|....*....|
gi 2119559688 238 ---DALEKAshGRTTIVIAH 254
Cdd:PRK11607  191 evvDILERV--GVTCVMVTH 208
cbiO PRK13640
energy-coupling factor transporter ATPase;
59-292 3.93e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 111.82  E-value: 3.93e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPEAkILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEE---GQILIDGVNLKDINLKWWRE 135
Cdd:PRK13640    6 VEFKHVSFTYPDSKKP-ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVWDIRE 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEP--VLFGTTIEENIRYG--HLDVTKED----IEQAAKMANAHDFIMDLPQkyetlvgergaQLSGGQKQRIA 207
Cdd:PRK13640   85 KVGIVFQNPdnQFVGATVGDDVAFGleNRAVPRPEmikiVRDVLADVGMLDYIDSEPA-----------NLSGGQKQRVA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 208 IARALVRNPKILLLDEATSALDTESE----GIVQDALEKasHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELM 283
Cdd:PRK13640  154 IAGILAVEPKIIILDESTSMLDPAGKeqilKLIRKLKKK--NNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIF 231

                  ....*....
gi 2119559688 284 SKQGIYQQL 292
Cdd:PRK13640  232 SKVEMLKEI 240
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
59-271 4.39e-27

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: 109.73  E-value: 4.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPsrPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWW----R 134
Cdd:cd03290     1 VQVTNGYFSWG--SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 135 ENIGIVSQEPVLFGTTIEENIRYGHlDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVR 214
Cdd:cd03290    79 YSVAYAAQKPWLLNATVEENITFGS-PFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQ 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 215 NPKILLLDEATSALDTE-SEGIVQDALEK--ASHGRTTIVIAHRLSTIKTADMIAGFKDG 271
Cdd:cd03290   158 NTNIVFLDDPFSALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
60-257 8.57e-27

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 110.55  E-value: 8.57e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHFRYPS------RPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN---L 130
Cdd:PRK10419    5 NVSGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 131 KWWRENIGIVSQEPV-------LFGTTIEENIRygHLdvtkEDIEQAAKMANAHDFI--MDLPqkyETLVGERGAQLSGG 201
Cdd:PRK10419   85 KAFRRDIQMVFQDSIsavnprkTVREIIREPLR--HL----LSLDKAERLARASEMLraVDLD---DSVLDKRPPQLSGG 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 202 QKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTT--IVIAHRLS 257
Cdd:PRK10419  156 QLQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTacLFITHDLR 213
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
76-284 8.59e-27

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 109.84  E-value: 8.59e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  76 ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQI-----LIDG---VNLKDINLKWWRENIGIVSQEPVLF 147
Cdd:PRK11264   18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTarsLSQQKGLIRQLRQHVGFVFQNFNLF 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 148 -GTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKyETLVGERgaqLSGGQKQRIAIARALVRNPKILLLDEATS 226
Cdd:PRK11264   98 pHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGK-ETSYPRR---LSGGQQQRVAIARALAMRPEVILFDEPTS 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 227 ALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTIK-TADMIAGFKDGVVAEQGTHNELMS 284
Cdd:PRK11264  174 ALDPELVGEVLNTIRQlAQEKRTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAKALFA 233
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
59-286 8.71e-27

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 111.09  E-value: 8.71e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPEAkiLYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG--VNLKDINLKWWREN 136
Cdd:PRK13636    6 LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMKLRES 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEP--VLFGTTIEENIRYG--HLDVTKEDIEQAAKMANAHDFIMDLPQKYETLvgergaqLSGGQKQRIAIARAL 212
Cdd:PRK13636   84 VGMVFQDPdnQLFSASVYQDVSFGavNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHC-------LSFGQKKRVAIAGVL 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 213 VRNPKILLLDEATSALDTE--SEgIVQDALEKASHGRTTIVIA-HRLSTIKT-ADMIAGFKDGVVAEQGTHNELMSKQ 286
Cdd:PRK13636  157 VMEPKVLVLDEPTAGLDPMgvSE-IMKLLVEMQKELGLTIIIAtHDIDIVPLyCDNVFVMKEGRVILQGNPKEVFAEK 233
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
59-284 1.47e-26

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: 109.89  E-value: 1.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPS------RPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN--- 129
Cdd:TIGR02769   3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkq 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 130 LKWWRENIGIVSQE-PVLFG--TTIEENIR--YGHLDVTKEDiEQAAKMANAHDfIMDLPqkyETLVGERGAQLSGGQKQ 204
Cdd:TIGR02769  83 RRAFRRDVQLVFQDsPSAVNprMTVRQIIGepLRHLTSLDES-EQKARIAELLD-MVGLR---SEDADKLPRQLSGGQLQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 205 RIAIARALVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNE 281
Cdd:TIGR02769 158 RINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVEECDVAQ 237

                  ...
gi 2119559688 282 LMS 284
Cdd:TIGR02769 238 LLS 240
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
61-285 1.54e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 110.49  E-value: 1.54e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  61 IRGVHFRY-PSRP-EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILI------DGVNLKDinLKW 132
Cdd:PRK13634    5 FQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKK--LKP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 133 WRENIGIVSQ--EPVLFGTTIEENIRYGHLD--VTKEDIEQAAKMANAhdfIMDLPqkyETLVGERGAQLSGGQKQRIAI 208
Cdd:PRK13634   83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMNfgVSEEDAKQKAREMIE---LVGLP---EELLARSPFELSGGQMRRVAI 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 209 ARALVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNELMSK 285
Cdd:PRK13634  157 AGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQGTPREIFAD 236
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
59-284 1.64e-26

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 109.74  E-value: 1.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPE-----EGQILIDGVNL--KDINLK 131
Cdd:PRK14258    8 IKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIyeRRVNLN 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 132 WWRENIGIVSQEPVLFGTTIEENIRYG------HLDVTKEDI-EQAAKMANAHDFIMDLPQKyetlvgeRGAQLSGGQKQ 204
Cdd:PRK14258   85 RLRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIvESALKDADLWDEIKHKIHK-------SALDLSGGQQQ 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 205 RIAIARALVRNPKILLLDEATSALDTES----EGIVQDALEKAShgRTTIVIAHRLSTI-KTADMIAGFKD-----GVVA 274
Cdd:PRK14258  158 RLCIARALAVKPKVLLMDEPCFGLDPIAsmkvESLIQSLRLRSE--LTMVIVSHNLHQVsRLSDFTAFFKGnenriGQLV 235
                         250
                  ....*....|
gi 2119559688 275 EQGTHNELMS 284
Cdd:PRK14258  236 EFGLTKKIFN 245
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
59-291 2.12e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 109.44  E-value: 2.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPEAkiLYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIG 138
Cdd:PRK13647    5 IEVEDLHFRYKDGTKA--LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEP--VLFGTTIEENIRYG--HLDVTKEDI----EQAAKMANAHDFIMDLPQkyetlvgergaQLSGGQKQRIAIAR 210
Cdd:PRK13647   83 LVFQDPddQVFSSTVWDDVAFGpvNMGLDKDEVerrvEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 211 ALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIA-HRLS-TIKTADMIAGFKDGVVAEQGThNELMSKQGI 288
Cdd:PRK13647  152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVAtHDVDlAAEWADQVIVLKEGRVLAEGD-KSLLTDEDI 230

                  ...
gi 2119559688 289 YQQ 291
Cdd:PRK13647  231 VEQ 233
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
80-284 3.26e-26

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: 110.97  E-value: 3.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKD----INLKWWRENIGIVSQEPVLFG-TTIEEN 154
Cdd:TIGR02142  16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFPhLSVRGN 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 155 IRYGHLDVTKEDIEQAakmanaHDFIMDLpQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEG 234
Cdd:TIGR02142  96 LRYGMKRARPSERRIS------FERVIEL-LGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 235 IVQDALEK--ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNELMS 284
Cdd:TIGR02142 169 EILPYLERlhAEFGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWA 221
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
80-232 5.04e-26

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: 110.58  E-value: 5.04e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  80 VNLQIKRGQTVALVGSSGCGKSTIVQL---LQRfydPEEGQILIDGVNLKD----INLKWWRENIGIVSQEPVLFGT-TI 151
Cdd:COG4148    18 VDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEVLQDsargIFLPPHRRRIGYVFQEARLFPHlSV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 152 EENIRYGH----LDVTKEDIEQAAKManahdfiMDLpqkyETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 227
Cdd:COG4148    95 RGNLLYGRkrapRAERRISFDEVVEL-------LGI----GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAA 163

                  ....*
gi 2119559688 228 LDTES 232
Cdd:COG4148   164 LDLAR 168
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
59-284 6.01e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 108.24  E-value: 6.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPEAkiLYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN--LKWWREN 136
Cdd:PRK13639    2 LETRDLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKksLLEVRKT 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEP--VLFGTTIEENIRYG--HLDVTKEDIEQAAKMANAHdfimdlpqkyetlVGERGAQ------LSGGQKQRI 206
Cdd:PRK13639   80 VGIVFQNPddQLFAPTVEEDVAFGplNLGLSKEEVEKRVKEALKA-------------VGMEGFEnkpphhLSGGQKKRV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 207 AIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIA-HRLSTIKT-ADMIAGFKDGVVAEQGTHNELMS 284
Cdd:PRK13639  147 AIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIIStHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFS 226
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
59-279 8.21e-26

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 107.02  E-value: 8.21e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSrpeAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG--------VNLKDINL 130
Cdd:PRK11124    3 IQLNGINCFYGA---HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktPSDKAIRE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 131 kwWRENIGIVSQE----PVLfgtTIEENIRYGHLDVTKEDIEQAAKMANAH-------DFIMDLPQkyetlvgergaQLS 199
Cdd:PRK11124   80 --LRRNVGMVFQQynlwPHL---TVQQNLIEAPCRVLGLSKDQALARAEKLlerlrlkPYADRFPL-----------HLS 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 200 GGQKQRIAIARALVRNPKILLLDEATSALDTE-SEGIVQDALEKASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQG 277
Cdd:PRK11124  144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVArKTASRVVYMENGHIVEQG 223

                  ..
gi 2119559688 278 TH 279
Cdd:PRK11124  224 DA 225
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
82-277 9.46e-26

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: 105.65  E-value: 9.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  82 LQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKwwRENIGIVSQEPVLFG-TTIEENIRYG-- 158
Cdd:cd03298    19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAhLTVEQNVGLGls 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 159 -HLDVTKEDiEQAAKMANAHdfiMDLPQKYETLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQ 237
Cdd:cd03298    97 pGLKLTAED-RQAIEVALAR---VGLAGLEKRLPGE----LSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEML 168
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2119559688 238 DALEK--ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQG 277
Cdd:cd03298   169 DLVLDlhAETKMTVLMVTHQPEDAkRLAQRVVFLDNGRIAAQG 211
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
663-791 1.81e-25

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 111.84  E-value: 1.81e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 663 SAKEIFKLIDKKPDIDNESEKGEQLHTftANLSFANIIFRYPTRPDTtILKGLDLEVPQGQTVALVGSSGCGKSTTVQLT 742
Cdd:PRK11160  310 SARRINEITEQKPEVTFPTTSTAAADQ--VSLTLNNVSFTYPDQPQP-VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2119559688 743 ERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENIA 791
Cdd:PRK11160  387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLL 435
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
58-286 2.10e-25

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 105.87  E-value: 2.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  58 NVQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG--------VNLKDIN 129
Cdd:COG4161     2 SIQLKNINCFYGSHQ---ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsqkPSEKAIR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 130 LkwWRENIGIVSQE----PVLfgtTIEENIRYGHLDVTKEDIEQAAKMANAH-------DFIMDLPQkyetlvgergaQL 198
Cdd:COG4161    79 L--LRQKVGMVFQQynlwPHL---TVMENLIEAPCKVLGLSKEQAREKAMKLlarlrltDKADRFPL-----------HL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 199 SGGQKQRIAIARALVRNPKILLLDEATSALDTE-SEGIVQDALEKASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQ 276
Cdd:COG4161   143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFArKVASQVVYMEKGRIIEQ 222
                         250
                  ....*....|
gi 2119559688 277 GTHNELMSKQ 286
Cdd:COG4161   223 GDASHFTQPQ 232
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
61-273 2.10e-25

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 106.30  E-value: 2.10e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  61 IRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDInlkwwRENIGIV 140
Cdd:PRK11247   15 LNAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLM 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 141 SQEPVLFG-TTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPqkyetlvgergAQLSGGQKQRIAIARALVRNPKIL 219
Cdd:PRK11247   87 FQDARLLPwKKVIDNVGLGLKGQWRDAALQALAAVGLADRANEWP-----------AALSGGQKQRVALARALIHRPGLL 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 220 LLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLS-TIKTADMIAGFKDGVV 273
Cdd:PRK11247  156 LLDEPLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
423-822 2.67e-25

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: 111.38  E-value: 2.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 423 VISLIAYFVQGY-------MFGRSGEYLTLRLRSMSFKAMLRQeiAFFDDHNNSVGALTtrlatDASQVQGAAGiklGSS 495
Cdd:COG4618    64 LLALGLYAVMGLldavrsrILVRVGARLDRRLGPRVFDAAFRA--ALRGGGGAAAQALR-----DLDTLRQFLT---GPG 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 496 LMAFC----SVVTgIVIGFVFSWKITLLVIAFLpFVMIGGALEMQMMqgaagkNKEALESAGKIAIESIE-------NIR 564
Cdd:COG4618   134 LFALFdlpwAPIF-LAVLFLFHPLLGLLALVGA-LVLVALALLNERL------TRKPLKEANEAAIRANAfaeaalrNAE 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 565 TVASL-TREDMFQK--KFNHELQMPYNIALKKAHLIGigfSLSQAVMFFAYAASFWLGAYLIKQSEvdyvdvfkafsaiL 641
Cdd:COG4618   206 VIEAMgMLPALRRRwqRANARALALQARASDRAGGFS---ALSKFLRLLLQSAVLGLGAYLVIQGE-------------I 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 642 FGGMAIGnAS-----AFAP-DAA--------KAEQSAKEIFKLIDKKPdidnESEKGEQLHTFTANLSFANIIFRYPTRp 707
Cdd:COG4618   270 TPGAMIA-ASilmgrALAPiEQAiggwkqfvSARQAYRRLNELLAAVP----AEPERMPLPRPKGRLSVENLTVVPPGS- 343
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIA 787
Cdd:COG4618   344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIA 423
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 2119559688 788 ENIAygdnsR--EVTMDEIIDAARKANIHNFIASLPD 822
Cdd:COG4618   424 ENIA-----RfgDADPEKVVAAAKLAGVHEMILRLPD 455
PTZ00243 PTZ00243
ABC transporter; Provisional
67-790 3.77e-25

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 112.56  E-value: 3.77e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   67 RYPSRPEaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQIlidgvnlkdinlkWWRENIGIVSQEPVL 146
Cdd:PTZ00243   667 FFELEPK-VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWI 732
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  147 FGTTIEENIryghLDVTKEDIEQAAKMANAHDFIMDLPQ---KYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDE 223
Cdd:PTZ00243   733 MNATVRGNI----LFFDEEDAARLADAVRVSQLEADLAQlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDD 808
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  224 ATSALDTE-SEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMsKQGIYQQLVTlQSMKSAD 302
Cdd:PTZ00243   809 PLSALDAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFM-RTSLYATLAA-ELKENKD 886
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  303 DNEiEDFNRDDTKRPSLRHQKSTIDMTPKKlaqdkkeeIKEEEKGEKEEEVDASLGRILKLNKSEAPFIVMGCFASLVN- 381
Cdd:PTZ00243   887 SKE-GDADAEVAEVDAAPGGAVDHEPPVAK--------QEGNAEGGDGAALDAAAGRLMTREEKASGSVPWSTYVAYLRf 957
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  382 -GGAMPAFAVI----FSEILGVFAIL-----DEGEQERKIIQYVLMFVGVGVISLIAY---FVQGYMFGRSGEYLTLR-- 446
Cdd:PTZ00243   958 cGGLHAAGFVLatfaVTELVTVSSGVwlsmwSTRSFKLSAATYLYVYLGIVLLGTFSVplrFFLSYEAMRRGSRNMHRdl 1037
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  447 LRSMSfkamlRQEIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIgfvfswkitllVIAFLPF 526
Cdd:PTZ00243  1038 LRSVS-----RGTMSFFD--TTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFSICSSILV-----------TSASQPF 1099
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  527 VMIG----GALEMQMMQGAAGKNKEA--LESAGKIAI-----ESIENIRTVASLTREDMFQKKFNHELQMPY-------- 587
Cdd:PTZ00243  1100 VLVAlvpcGYLYYRLMQFYNSANREIrrIKSVAKSPVftlleEALQGSATITAYGKAHLVMQEALRRLDVVYscsylenv 1179
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  588 -------------NIALKKAHLIGIG-------------FSLSQAVMFFAYAASFWLG----------------AYLIKQ 625
Cdd:PTZ00243  1180 anrwlgvrveflsNIVVTVIALIGVIgtmlratsqeiglVSLSLTMAMQTTATLNWLVrqvatveadmnsverlLYYTDE 1259
                          650       660       670       680       690       700       710       720
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  626 SEVDYVDVFKAFSAILFG--GMAIGNASAFAPDAAKAEQSAKeifklidkkpdidnesekgeqlHTFTA-NLSFANIIFR 702
Cdd:PTZ00243  1260 VPHEDMPELDEEVDALERrtGMAADVTGTVVIEPASPTSAAP----------------------HPVQAgSLVFEGVQMR 1317
                          730       740       750       760       770       780       790       800
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  703 Y----PtrpdtTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQE 778
Cdd:PTZ00243  1318 YreglP-----LVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQD 1392
                          810
                   ....*....|..
gi 2119559688  779 PVLFDRTIAENI 790
Cdd:PTZ00243  1393 PVLFDGTVRQNV 1404
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
59-289 3.83e-25

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 107.36  E-value: 3.83e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSR-----PEA--KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN-- 129
Cdd:PRK11308    6 LQAIDLKKHYPVKrglfkPERlvKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpe 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 130 -LKWWRENIGIVSQEPV-------LFGTTIEENIRYgHLDVTK-EDIEQAAKManahdfiMdlpqkyeTLVGERGAQ--- 197
Cdd:PRK11308   86 aQKLLRQKIQIVFQNPYgslnprkKVGQILEEPLLI-NTSLSAaERREKALAM-------M-------AKVGLRPEHydr 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 198 ----LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIV-------QDALekashGRTTIVIAHRLSTIK-TAD-- 263
Cdd:PRK11308  151 yphmFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVlnlmmdlQQEL-----GLSYVFISHDLSVVEhIADev 225
                         250       260
                  ....*....|....*....|....*.
gi 2119559688 264 MIAGFkdGVVAEQGthnelmSKQGIY 289
Cdd:PRK11308  226 MVMYL--GRCVEKG------TKEQIF 243
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
64-285 5.89e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 105.55  E-value: 5.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  64 VHFRYPSRPEAKILYG---VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKW-WRENIGI 139
Cdd:PRK13633   10 VSYKYESNEESTEKLAlddVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIRNKAGM 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 VSQEP--VLFGTTIEENIRYG--HLDVTKEDI----EQAAKMANAHDFIMDLPQkyetlvgergaQLSGGQKQRIAIARA 211
Cdd:PRK13633   90 VFQNPdnQIVATIVEEDVAFGpeNLGIPPEEIrervDESLKKVGMYEYRRHAPH-----------LLSGGQKQRVAIAGI 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 212 LVRNPKILLLDEATSALDTESEGIVQDALEKAS--HGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSK 285
Cdd:PRK13633  159 LAMRPECIIFDEPTAMLDPSGRREVVNTIKELNkkYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFKE 234
cbiO PRK13649
energy-coupling factor transporter ATPase;
73-297 1.11e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 104.83  E-value: 1.11e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  73 EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNL----KDINLKWWRENIGIVSQ--EPVL 146
Cdd:PRK13649   19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQIRKKVGLVFQfpESQL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 147 FGTTIEENIRYG--HLDVTKEDIEQAAKMAnahdfiMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEA 224
Cdd:PRK13649   99 FEETVLKDVAFGpqNFGVSQEEAEALAREK------LALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 225 TSALDTESEGIVQDALEKASHGRTTIVIAHRLstiktADMIAGFKDGV-VAEQGTHNELMSKQGIYQQLVTLQS 297
Cdd:PRK13649  173 TAGLDPKGRKELMTLFKKLHQSGMTIVLVTHL-----MDDVANYADFVyVLEKGKLVLSGKPKDIFQDVDFLEE 241
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
73-256 1.56e-24

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 103.63  E-value: 1.56e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  73 EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDI-NLKWWR--ENIGIVSQEPVLfGT 149
Cdd:COG1101    18 EKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDG---KDVtKLPEYKraKYIGRVFQDPMM-GT 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 150 ----TIEENI--------RYG-HLDVTKEDI----EQAAKMAnahdfiMDLPQKYETLVGergaQLSGGQKQRIAIARAL 212
Cdd:COG1101    94 apsmTIEENLalayrrgkRRGlRRGLTKKRRelfrELLATLG------LGLENRLDTKVG----LLSGGQRQALSLLMAT 163
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2119559688 213 VRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRL 256
Cdd:COG1101   164 LTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNM 209
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
79-268 2.06e-24

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 103.32  E-value: 2.06e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  79 GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYD-----PEEGQILIDGVNL--KDINLKWWRENIGIVSQEPVLFGTTI 151
Cdd:PRK14243   28 NVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPKSI 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 152 EENIRYG--------HLDvtkEDIEQAAKMANAHDFIMDLpqkyetlVGERGAQLSGGQKQRIAIARALVRNPKILLLDE 223
Cdd:PRK14243  108 YDNIAYGaringykgDMD---ELVERSLRQAALWDEVKDK-------LKQSGLSLSGGQQQRLCIARAIAVQPEVILMDE 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2119559688 224 ATSALDTESEGIVQDALEKASHGRTTIVIAHRL-STIKTADMIAGF 268
Cdd:PRK14243  178 PCSALDPISTLRIEELMHELKEQYTIIIVTHNMqQAARVSDMTAFF 223
cbiO PRK13645
energy-coupling factor transporter ATPase;
54-286 2.12e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 104.32  E-value: 2.12e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  54 NFQGNVQIRGVHFRYPSRP--EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG----VNLKD 127
Cdd:PRK13645    2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 128 IN-LKWWRENIGIVSQEP--VLFGTTIEENIRYGHLDVTKEDIEQAAKMANAHDFImDLPQKYetlVGERGAQLSGGQKQ 204
Cdd:PRK13645   82 IKeVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLV-QLPEDY---VKRSPFELSGGQKR 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 205 RIAIARALVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNE 281
Cdd:PRK13645  158 RVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERlnKEYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGSPFE 237

                  ....*
gi 2119559688 282 LMSKQ 286
Cdd:PRK13645  238 IFSNQ 242
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
60-229 2.28e-24

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 103.40  E-value: 2.28e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHFRYPSRPEAK-ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLK----DinlkwwR 134
Cdd:COG4525     5 TVRHVSVRYPGGGQPQpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTgpgaD------R 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 135 eniGIVSQEPVLFG-TTIEENIRYGhLDVTKedIEQAAKMANAHDFImdlpqkyeTLVGERGA------QLSGGQKQRIA 207
Cdd:COG4525    79 ---GVVFQKDALLPwLNVLDNVAFG-LRLRG--VPKAERRARAEELL--------ALVGLADFarrriwQLSGGMRQRVG 144
                         170       180
                  ....*....|....*....|..
gi 2119559688 208 IARALVRNPKILLLDEATSALD 229
Cdd:COG4525   145 IARALAADPRFLLMDEPFGALD 166
cbiO PRK13644
energy-coupling factor transporter ATPase;
59-284 3.13e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 103.14  E-value: 3.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPEAkiLYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN-LKWWRENI 137
Cdd:PRK13644    2 IRLENVSYSYPDGTPA--LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 GIVSQEP--VLFGTTIEENIRYG--HLDVTKEDIEQAAKMANAHDFImdlpQKYETlvgERGAQLSGGQKQRIAIARALV 213
Cdd:PRK13644   80 GIVFQNPetQFVGRTVEEDLAFGpeNLCLPPIEIRKRVDRALAEIGL----EKYRH---RSPKTLSGGQGQCVALAGILT 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 214 RNPKILLLDEATSALDTESEGIVQDALEKA-SHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMS 284
Cdd:PRK13644  153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
56-254 3.17e-24

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 101.74  E-value: 3.17e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  56 QGNVQIRGVHfrypsrpeakilyGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILID----GVNLKD---- 127
Cdd:COG4778    19 QGGKRLPVLD-------------GVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhdggWVDLAQaspr 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 128 --INLKwwRENIGIVSQepvlFGTTIEeniRYGHLDVTKED-IEQAAKMANAHDFIMDLPQKYEtlVGERGAQL-----S 199
Cdd:COG4778    86 eiLALR--RRTIGYVSQ----FLRVIP---RVSALDVVAEPlLERGVDREEARARARELLARLN--LPERLWDLppatfS 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 200 GGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIV-IAH 254
Cdd:COG4778   155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFH 210
ABC_6TM_LmrA_like cd18551
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...
387-623 3.20e-24

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: 103.67  E-value: 3.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 387 AFAVIFSeILGVFA----------ILDEGEQERKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAML 456
Cdd:cd18551     2 ILALLLS-LLGTAAslaqpllvknLIDALSAGGSSGGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRRLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 457 RQEIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQ 536
Cdd:cd18551    81 RLPVSFFD--RRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 537 MMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAASF 616
Cdd:cd18551   159 RIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVL 238

                  ....*..
gi 2119559688 617 WLGAYLI 623
Cdd:cd18551   239 GVGGARV 245
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
81-229 4.34e-24

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 101.58  E-value: 4.34e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  81 NLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKwwRENIGIVSQEPVLFG-TTIEENIRYG- 158
Cdd:PRK10771   19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGl 96
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 159 ----HLDVT-KEDIEQAAKMANAHDFIMDLPqkyetlvgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 229
Cdd:PRK10771   97 npglKLNAAqREKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
cbiO PRK13646
energy-coupling factor transporter ATPase;
73-285 5.37e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 102.94  E-value: 5.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  73 EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNL----KDINLKWWRENIGIVSQ--EPVL 146
Cdd:PRK13646   19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktKDKYIRPVRKRIGMVFQfpESQL 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 147 FGTTIEENIRYGHLDVtKEDIEQAAkmANAHDFIMDLpqKYETLVGERGA-QLSGGQKQRIAIARALVRNPKILLLDEAT 225
Cdd:PRK13646   99 FEDTVEREIIFGPKNF-KMNLDEVK--NYAHRLLMDL--GFSRDVMSQSPfQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 226 SALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNELMSK 285
Cdd:PRK13646  174 AGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
PTZ00243 PTZ00243
ABC transporter; Provisional
57-293 6.38e-24

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 108.71  E-value: 6.38e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   57 GNVQIRGVHFRY----PSrpeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKW 132
Cdd:PTZ00243  1307 GSLVFEGVQMRYreglPL-----VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRE 1381
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  133 WRENIGIVSQEPVLFGTTIEENIRyGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARAL 212
Cdd:PTZ00243  1382 LRRQFSMIPQDPVLFDGTVRQNVD-PFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARAL 1460
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  213 V-RNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNEL-MSKQGIYQ 290
Cdd:PTZ00243  1461 LkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFH 1540

                   ...
gi 2119559688  291 QLV 293
Cdd:PTZ00243  1541 SMV 1543
cbiO PRK13642
energy-coupling factor transporter ATPase;
59-284 6.80e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 102.48  E-value: 6.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIG 138
Cdd:PRK13642    5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEP--VLFGTTIEENIRYG--HLDVTKED----IEQAAKMANAHDFIMDLPqkyetlvgergAQLSGGQKQRIAIAR 210
Cdd:PRK13642   85 MVFQNPdnQFVGATVEDDVAFGmeNQGIPREEmikrVDEALLAVNMLDFKTREP-----------ARLSGGQKQRVAVAG 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 211 ALVRNPKILLLDEATSALDTESEGIVQDALE--KASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMS 284
Cdd:PRK13642  154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHeiKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
60-225 7.38e-24

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


Pssm-ID: 440179 [Multi-domain]  Cd Length: 236  Bit Score: 101.21  E-value: 7.38e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHFRYPsrpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLkdINLKWW---REN 136
Cdd:COG0410     5 EVENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI--TGLPPHriaRLG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLFGT-TIEENIR---YGHLDvtKEDIEQAAkmanahDFIMDL-PQKYETLvGERGAQLSGGQKQRIAIARA 211
Cdd:COG0410    80 IGYVPEGRRIFPSlTVEENLLlgaYARRD--RAEVRADL------ERVYELfPRLKERR-RQRAGTLSGGEQQMLAIGRA 150
                         170
                  ....*....|....
gi 2119559688 212 LVRNPKILLLDEAT 225
Cdd:COG0410   151 LMSRPKLLLLDEPS 164
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
59-283 9.97e-24

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 100.93  E-value: 9.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIG 138
Cdd:COG4604     2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEP-----------VLFGttieeniRY----GHLdvTKEDieqAAKMANAHDFiMDLpqkyETLVGERGAQLSGGQK 203
Cdd:COG4604    79 ILRQENhinsrltvrelVAFG-------RFpyskGRL--TAED---REIIDEAIAY-LDL----EDLADRYLDELSGGQR 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 204 QRIAIARALVRNPKILLLDEATSALDTE-SEGIVQdALEKAS--HGRTTIVIAHRLS-TIKTADMIAGFKDGVVAEQGTH 279
Cdd:COG4604   142 QRAFIAMVLAQDTDYVLLDEPLNNLDMKhSVQMMK-LLRRLAdeLGKTVVIVLHDINfASCYADHIVAMKDGRVVAQGTP 220

                  ....
gi 2119559688 280 NELM 283
Cdd:COG4604   221 EEII 224
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
81-284 1.18e-23

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 104.34  E-value: 1.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  81 NLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRE----NIGIVSQEPVLF-GTTIEENI 155
Cdd:PRK10070   48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMpHMTVLDNT 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 156 RYGhldVTKEDIEQAAKMANAHDFIMDLpqKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGI 235
Cdd:PRK10070  128 AFG---MELAGINAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 236 VQDALEK--ASHGRTTIVIAHRL-STIKTADMIAGFKDGVVAEQGTHNELMS 284
Cdd:PRK10070  203 MQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILN 254
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
693-822 1.34e-23

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: 99.97  E-value: 1.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 693 NLSFANIIFRYPTRPDTTiLKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQI 772
Cdd:cd03245     2 RIEFRNVSFSYPNQEIPA-LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNI 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2119559688 773 GIVSQEPVLFDRTIAENIAYGDnsREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:cd03245    81 GYVPQDVTLFYGTLRDNITLGA--PLADDERILRAAELAGVTDFVNKHPN 128
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
59-277 1.73e-23

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: 99.21  E-value: 1.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRenIG 138
Cdd:cd03268     1 LKTNDLTKTYGKKR---VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR--IG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLFGT-TIEENIRYGH--LDVTKEDIEQAAKMANAHDFimdlpqkyetlVGERGAQLSGGQKQRIAIARALVRN 215
Cdd:cd03268    76 ALIEAPGFYPNlTARENLRLLArlLGIRKKRIDEVLDVVGLKDS-----------AKKKVKGFSLGMKQRLGIALALLGN 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 216 PKILLLDEATSALDTesEGI--VQDAL-EKASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQG 277
Cdd:cd03268   145 PDLLILDEPTNGLDP--DGIkeLRELIlSLRDQGITVLISSHLLSEIqKVADRIGIINKGKLIEEG 208
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
57-294 2.27e-23

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: 100.70  E-value: 2.27e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  57 GNVQIRGVHFRYPSRPEAkILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDpEEGQILIDGVNLKDINLKWWREN 136
Cdd:cd03289     1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLFGTTIEENIR-YGHLdvTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRN 215
Cdd:cd03289    79 FGVIPQKVFIFSGTFRKNLDpYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSK 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 216 PKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQGIYQQLVT 294
Cdd:cd03289   157 AKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAIS 235
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
63-260 2.84e-23

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 101.71  E-value: 2.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  63 GVHF------RYPSRPEA--KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWR 134
Cdd:PRK15079   15 KVHFdikdgkQWFWQPPKtlKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWR 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 135 E---NIGIVSQEPV-------LFGTTIEENIRYGHLDVTKEDIEQAAKManahdfIMD----LPQkyetLVGERGAQLSG 200
Cdd:PRK15079   95 AvrsDIQMIFQDPLaslnprmTIGEIIAEPLRTYHPKLSRQEVKDRVKA------MMLkvglLPN----LINRYPHEFSG 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 201 GQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTIK 260
Cdd:PRK15079  165 GQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQlqREMGLSLIFIAHDLAVVK 226
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
415-821 3.89e-23

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 104.41  E-value: 3.89e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 415 VLMFVGVG-----VISLIAYFVQGYMFGRSGEyLTLRLRSMSFKAMLRQEIAFFDDHNNsvGALTTRLATDASQVQGAAG 489
Cdd:PRK10789   35 ILMWIGTMvliavVVYLLRYVWRVLLFGASYQ-LAVELREDFYRQLSRQHPEFYLRHRT--GDLMARATNDVDRVVFAAG 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 490 ---IKLGSSLMAFCSVVtgIVIGFVFSWKITLLVIAFLPFVMI-----GGALEMQMMQGAAgknkeALESAGKIAIESIE 561
Cdd:PRK10789  112 egvLTLVDSLVMGCAVL--IVMSTQISWQLTLLALLPMPVMAImikryGDQLHERFKLAQA-----AFSSLNDRTQESLT 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 562 NIRTVASLTREDMFQKKFNhelQMPYNIALKKAHL------------IGIGFSlsqavMFFAYAASFWLgaylikqsevd 629
Cdd:PRK10789  185 SIRMIKAFGLEDRQSALFA---ADAEDTGKKNMRVaridarfdptiyIAIGMA-----NLLAIGGGSWM----------- 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 630 yvdvfkafsaILFGGMAIGNASAFA--------PDAAKA-------EQSA--KEIFKLIDKKPDIDNESEK-GEQLHTFT 691
Cdd:PRK10789  246 ----------VVNGSLTLGQLTSFVmylglmiwPMLALAwmfniveRGSAaySRIRAMLAEAPVVKDGSEPvPEGRGELD 315
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 692 ANLSfaniIFRYPTRpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQ 771
Cdd:PRK10789  316 VNIR----QFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSR 390
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|
gi 2119559688 772 IGIVSQEPVLFDRTIAENIAYGdnSREVTMDEIIDAARKANIHNFIASLP 821
Cdd:PRK10789  391 LAVVSQTPFLFSDTVANNIALG--RPDATQQEIEHVARLASVHDDILRLP 438
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
61-232 4.17e-23

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 103.99  E-value: 4.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  61 IRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDgvnlkdinlKWWRenIGIV 140
Cdd:COG0488     1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------KGLR--IGYL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 141 SQEPVLF-GTTIEENIRYGH--LDVTKEDIEQA-AKMANAHDFIM---------------DLPQKYETLVGERG------ 195
Cdd:COG0488    67 PQEPPLDdDLTVLDTVLDGDaeLRALEAELEELeAKLAEPDEDLErlaelqeefealggwEAEARAEEILSGLGfpeedl 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2119559688 196 ----AQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 232
Cdd:COG0488   147 drpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES 187
ABC_6TM_bac_exporter_ABCB8_10_like cd18575
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...
396-620 4.45e-23

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: 350019 [Multi-domain]  Cd Length: 289  Bit Score: 100.25  E-value: 4.45e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 396 LGVFAILDEG---EQERKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGA 472
Cdd:cd18575    17 QGLRLLIDQGfaaGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLLRLSPSFFE--TTRTGE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 473 LTTRLATDASQVQGAagikLGSSL-MAFCSVVT---GIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEA 548
Cdd:cd18575    95 VLSRLTTDTTLIQTV----VGSSLsIALRNLLLligGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDR 170
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 549 LESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGA 620
Cdd:cd18575   171 LADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWLGA 242
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
471-822 5.01e-23

thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.


Pssm-ID: 274331 [Multi-domain]  Cd Length: 530  Bit Score: 103.98  E-value: 5.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 471 GALTTRLATDASQVQGA---AGIKLGSSLMAFCSVVTGIvigFVFSWKITLLVIAFLpfvMIGGALeMQMMQGAAGKNKE 547
Cdd:TIGR02868 110 GDLLGRLGADVDALQDLyvrVIVPAGVALVVGAAAVAAI---AVLSVPAALILAAGL---LLAGFV-APLVSLRAARAAE 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 548 ALE--SAGKIAIESIENIRTVASLT---REDMFQKKF---NHELQmpyNIALKKAHLIGIGFSLSQAVMFFAYAASFWLG 619
Cdd:TIGR02868 183 QALarLRGELAAQLTDALDGAAELVasgALPAALAQVeeaDRELT---RAERRAAAATALGAALTLLAAGLAVLGALWAG 259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 620 AYLIKQSEVDYVdvfkAFSAILFGGMAIGNASAFAPDAA----KAEQSAKEIFKLIDKKPDI-DNESEKGEQLHTFTANL 694
Cdd:TIGR02868 260 GPAVADGRLAPV----TLAVLVLLPLAAFEAFAALPAAAqqltRVRAAAERIVEVLDAAGPVaEGSAPAAGAVGLGKPTL 335
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 695 SFANIIFRYPTRPDttILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGI 774
Cdd:TIGR02868 336 ELRDLSAGYPGAPP--VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSV 413
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 2119559688 775 VSQEPVLFDRTIAENIAYGdnSREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:TIGR02868 414 CAQDAHLFDTTVRENLRLA--RPDATDEELWAALERVGLADWLRALPD 459
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
712-822 5.08e-23

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: 95.79  E-value: 5.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDR-TIAENI 790
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRlTVRENL 80
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2119559688 791 AYG----DNSREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:pfam00005  81 RLGlllkGLSKREKDARAEEALEKLGLGDLADRPVG 116
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
64-284 6.66e-23

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 98.89  E-value: 6.66e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  64 VHFRYPsrpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDI-------------NL 130
Cdd:PRK10619   11 LHKRYG---EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 131 KWWRENIGIVSQEPVLFG-TTIEENIRYGHLDV----TKEDIEQAAKMANAHDFIMDLPQKYEtlvgergAQLSGGQKQR 205
Cdd:PRK10619   88 RLLRTRLTMVFQHFNLWShMTVLENVMEAPIQVlglsKQEARERAVKYLAKVGIDERAQGKYP-------VHLSGGQQQR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 206 IAIARALVRNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTIK-TADMIAGFKDGVVAEQGTHNELM 283
Cdd:PRK10619  161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARhVSSHVIFLHQGKIEEEGAPEQLF 240

                  .
gi 2119559688 284 S 284
Cdd:PRK10619  241 G 241
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
79-278 9.08e-23

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: 103.23  E-value: 9.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  79 GVNLQIKRGQTVALVGSSGCGKS----TIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRE----NIGIVSQEPV----- 145
Cdd:COG4172    28 GVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPMtslnp 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 146 LFgtTIE----ENIRYgHLDVTKED-------------IEQAAKMANA--HdfimdlpqkyetlvgergaQLSGGQKQRI 206
Cdd:COG4172   108 LH--TIGkqiaEVLRL-HRGLSGAAararalellervgIPDPERRLDAypH-------------------QLSGGQRQRV 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 207 AIARALVRNPKILLLDEATSALDTesegIVQ----DALE--KASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGT 278
Cdd:COG4172   166 MIAMALANEPDLLIADEPTTALDV----TVQaqilDLLKdlQRELGMALLLITHDLGVVrRFADRVAVMRQGEIVEQGP 240
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
694-790 9.20e-23

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 96.23  E-value: 9.20e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwLRSQIG 773
Cdd:cd03247     1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
                          90
                  ....*....|....*..
gi 2119559688 774 IVSQEPVLFDRTIAENI 790
Cdd:cd03247    79 VLNQRPYLFDTTLRNNL 95
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
79-257 1.19e-22

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: 97.51  E-value: 1.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  79 GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDinlkwWREN----IGIVS--QEPVLFGT-TI 151
Cdd:cd03219    18 DVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITG-----LPPHeiarLGIGRtfQIPRLFPElTV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 152 EENIRYGHLDVTKEDI-------EQAAKMANAHDFI--MDLPQKYETLVGErgaqLSGGQKQRIAIARALVRNPKILLLD 222
Cdd:cd03219    93 LENVMVAAQARTGSGLllararrEEREARERAEELLerVGLADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLD 168
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2119559688 223 EATSAL-DTESEGIVQDALEKASHGRTTIVIAHRLS 257
Cdd:cd03219   169 EPAAGLnPEETEELAELIRELRERGITVLLVEHDMD 204
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
59-265 1.51e-22

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 102.03  E-value: 1.51e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSrpeAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG--VNLKD----INLKw 132
Cdd:COG3845     6 LELRGITKRFGG---VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSprdaIALG- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 133 wrenIGIVSQEPVLFGT-TIEENIRYGH--LDVTKEDIEQAAKManahdfIMDLPQKY------ETLVGergaQLSGGQK 203
Cdd:COG3845    82 ----IGMVHQHFMLVPNlTVAENIVLGLepTKGGRLDRKAARAR------IRELSERYgldvdpDAKVE----DLSVGEQ 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 204 QRIAIARALVRNPKILLLDEATSALdTESEgiVQ---DALEK-ASHGRTTIVIAHRLSTIKT-ADMI 265
Cdd:COG3845   148 QRVEILKALYRGARILILDEPTAVL-TPQE--ADelfEILRRlAAEGKSIIFITHKLREVMAiADRV 211
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
693-822 1.62e-22

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: 96.79  E-value: 1.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 693 NLSFANIIFRYptRPDT-TILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQ 771
Cdd:cd03244     2 DIEFKNVSLRY--RPNLpPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSR 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 772 IGIVSQEPVLFDRTIAENIaygDNSREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:cd03244    80 ISIIPQDPVLFSGTIRSNL---DPFGEYSDEELWQALERVGLKEFVESLPG 127
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
56-285 2.02e-22

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 97.29  E-value: 2.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  56 QGNVQIRGVHFRYPSrpeAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYD--PE---EGQILIDGVNLKDINL 130
Cdd:PRK14247    1 MNKIEIRDLKVSFGQ---VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 131 KWWRENIGIVSQEPVLFGT-TIEENIRYG----HLDVTKEDIEQAAKMAnahdfiMDLPQKYETL---VGERGAQLSGGQ 202
Cdd:PRK14247   78 IELRRRVQMVFQIPNPIPNlSIFENVALGlklnRLVKSKKELQERVRWA------LEKAQLWDEVkdrLDAPAGKLSGGQ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 203 KQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAH-RLSTIKTADMIAGFKDGVVAEQGTHNE 281
Cdd:PRK14247  152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTRE 231

                  ....
gi 2119559688 282 LMSK 285
Cdd:PRK14247  232 VFTN 235
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
61-229 2.05e-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: 96.84  E-value: 2.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  61 IRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINL-KWWRENIGI 139
Cdd:cd03218     3 AENLSKRYGKR---KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMhKRARLGIGY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 VSQEPVLF-GTTIEENIRyGHLDVTKEDIEQAAKMANA--HDFimdlpqKYETLVGERGAQLSGGQKQRIAIARALVRNP 216
Cdd:cd03218    80 LPQEASIFrKLTVEENIL-AVLEIRGLSKKEREEKLEEllEEF------HITHLRKSKASSLSGGERRRVEIARALATNP 152
                         170
                  ....*....|...
gi 2119559688 217 KILLLDEATSALD 229
Cdd:cd03218   153 KFLLLDEPFAGVD 165
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
59-277 2.63e-22

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: 95.90  E-value: 2.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRY-PSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDiNLKWWRENI 137
Cdd:cd03266     2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 GIVSQEPVLFG-TTIEENIRY-GHLdvtkedieQAAKMANAHDFIMDLPQKY--ETLVGERGAQLSGGQKQRIAIARALV 213
Cdd:cd03266    81 GFVSDSTGLYDrLTARENLEYfAGL--------YGLKGDELTARLEELADRLgmEELLDRRVGGFSTGMRQKVAIARALV 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 214 RNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQG 277
Cdd:cd03266   153 HDPPVLLLDEPTTGLDVMATRALREFIRQlRALGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
75-298 3.99e-22

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 96.62  E-value: 3.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  75 KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVL-FGTTIEE 153
Cdd:PRK11231   16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVRE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 154 NIRYG---HLD----VTKED---IEQAakMANAHdfimdlpqkYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDE 223
Cdd:PRK11231   96 LVAYGrspWLSlwgrLSAEDnarVNQA--MEQTR---------INHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 224 ATSALDTESEGIVQDAL-EKASHGRTTIVIAHRLS-TIKTADMIAGFKDGVVAEQGTHNELMSkQGIYQQLVTLQSM 298
Cdd:PRK11231  165 PTTYLDINHQVELMRLMrELNTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMT-PGLLRTVFDVEAE 240
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
16-256 5.21e-22

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: 102.30  E-value: 5.21e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   16 MPHLQTLATARGAAYYLYQLITMDPPidsystEGKKLDNFQGNVQIRGVHFRYPSRPEAkILYGVNLQIKRGQTVALVGS 95
Cdd:TIGR01271 1181 LPQEEPRPSGGGGKYQLSTVLVIENP------HAQKCWPSGGQMDVQGLTAKYTEAGRA-VLQDLSFSVEGGQRVGLLGR 1253
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   96 SGCGKSTIVQLLQRFYDpEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIEENIRyGHLDVTKEDIEQAAKMAN 175
Cdd:TIGR01271 1254 TGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVG 1331
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  176 AHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHR 255
Cdd:TIGR01271 1332 LKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHR 1411

                   .
gi 2119559688  256 L 256
Cdd:TIGR01271 1412 V 1412
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
58-282 5.91e-22

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 98.56  E-value: 5.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  58 NVQIRGVhfrYPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKwwRENI 137
Cdd:PRK11000    3 SVTLRNV---TKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGV 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 GIVSQEPVLF-GTTIEENIRYGhLDVTKEDIEQAAKMANAHDFIMDLpqkyETLVGERGAQLSGGQKQRIAIARALVRNP 216
Cdd:PRK11000   78 GMVFQSYALYpHLSVAENMSFG-LKLAGAKKEEINQRVNQVAEVLQL----AHLLDRKPKALSGGQRQRVAIGRTLVAEP 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 217 KILLLDEATSALDTESEgiVQDALEKAS-H---GRTTIVIAH-RLSTIKTADMIAGFKDGVVAEQGTHNEL 282
Cdd:PRK11000  153 SVFLLDEPLSNLDAALR--VQMRIEISRlHkrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGKPLEL 221
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
56-255 7.91e-22

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 100.27  E-value: 7.91e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  56 QGNVQIRGVHFRYPS-RPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILI-DGvnlkdinlkww 133
Cdd:COG4178   360 DGALALEDLTLRTPDgRP---LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAG----------- 425
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 134 rENIGIVSQEPVLFGTTIEENIRY--GHLDVTKEDIEQAAKMANAHDFIMDLPQkyetlVGERGAQLSGGQKQRIAIARA 211
Cdd:COG4178   426 -ARVLFLPQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVGLGHLAERLDE-----EADWDQVLSLGEQQRLAFARL 499
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2119559688 212 LVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHR 255
Cdd:COG4178   500 LLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR 543
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
73-290 8.95e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 97.23  E-value: 8.95e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  73 EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGV---------------NLKDI-NLKWWREN 136
Cdd:PRK13631   38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIyigdkknnhelitnpYSKKIkNFKELRRR 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEP--VLFGTTIEENIRYG--HLDVTKEDieqAAKMANAHDFIMDLpqKYETLvgERGA-QLSGGQKQRIAIARA 211
Cdd:PRK13631  118 VSMVFQFPeyQLFKDTIEKDIMFGpvALGVKKSE---AKKLAKFYLNKMGL--DDSYL--ERSPfGLSGGQKRRVAIAGI 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 212 LVRNPKILLLDEATSALDTESEG-IVQDALEKASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNELMSKQGIY 289
Cdd:PRK13631  191 LAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIFTDQHII 270

                  .
gi 2119559688 290 Q 290
Cdd:PRK13631  271 N 271
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
76-231 1.09e-21

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 94.09  E-value: 1.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  76 ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPE---EGQILIDGVNLKDINLKwwRENIGIVSQEPVLFG-TTI 151
Cdd:COG4136    16 LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE--QRRIGILFQDDLLFPhLSV 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 152 EENIRYGhL--DVTKED----IEQAAKMANAHDFimdlpqkyetlvGERG-AQLSGGQKQRIAIARALVRNPKILLLDEA 224
Cdd:COG4136    94 GENLAFA-LppTIGRAQrrarVEQALEEAGLAGF------------ADRDpATLSGGQRARVALLRALLAEPRALLLDEP 160

                  ....*..
gi 2119559688 225 TSALDTE 231
Cdd:COG4136   161 FSKLDAA 167
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
708-807 1.30e-21

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: 94.17  E-value: 1.30e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYD-----PADGIVSLDGHNLKDLNLQ--WLRSQIGIVSQEPV 780
Cdd:cd03260    12 DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvlELRRRVGMVFQKPN 91
                          90       100
                  ....*....|....*....|....*..
gi 2119559688 781 LFDRTIAENIAYGDNSREVTMDEIIDA 807
Cdd:cd03260    92 PFPGSIYDNVAYGLRLHGIKLKEELDE 118
ABC_6TM_MsbA_like cd18552
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...
371-642 1.31e-21

Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. 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: 349996 [Multi-domain]  Cd Length: 292  Bit Score: 95.95  E-value: 1.31e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 371 IVMGCFASLVNGGAMPAFAVIfseILGVFAILDEGEQERKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSM 450
Cdd:cd18552     1 LALAILGMILVAATTAALAWL---LKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRND 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 451 SFKAMLRQEIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIG 530
Cdd:cd18552    78 LFDKLLRLPLSFFD--RNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 531 GALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFF 610
Cdd:cd18552   156 IRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAI 235
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2119559688 611 AYAASFWLGAYLIKQSEVDyVDVFKAFSAILF 642
Cdd:cd18552   236 AIALVLWYGGYQVISGELT-PGEFISFITALL 266
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
60-254 1.34e-21

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 95.15  E-value: 1.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWwreniGI 139
Cdd:PRK11248    3 QISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GV 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 VSQ-EPVLFGTTIEENIRYGhldVTKEDIEQAAKMANAHDFImdlpqkyeTLVGERGA------QLSGGQKQRIAIARAL 212
Cdd:PRK11248   75 VFQnEGLLPWRNVQDNVAFG---LQLAGVEKMQRLEIAHQML--------KKVGLEGAekryiwQLSGGQRQRVGIARAL 143
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2119559688 213 VRNPKILLLDEATSALDTESEGIVQDALEKASH--GRTTIVIAH 254
Cdd:PRK11248  144 AANPQLLLLDEPFGALDAFTREQMQTLLLKLWQetGKQVLLITH 187
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
77-254 1.37e-21

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: 94.45  E-value: 1.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  77 LYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG-----------VNLKDINLKWWRenigivsqepv 145
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGkqitepgpdrmVVFQNYSLLPWL----------- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 146 lfgtTIEENIrYGHLDVTKEDIEQAAKMANAHDFImdlpqkyeTLVG------ERGAQLSGGQKQRIAIARALVRNPKIL 219
Cdd:TIGR01184  70 ----TVRENI-ALAVDRVLPDLSKSERRAIVEEHI--------ALVGlteaadKRPGQLSGGMKQRVAIARALSIRPKVL 136
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2119559688 220 LLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAH 254
Cdd:TIGR01184 137 LLDEPFGALDALTRGNLQEELMQiwEEHRVTVLMVTH 173
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
75-271 2.06e-21

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 98.85  E-value: 2.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  75 KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYdPE---EGQILIDGVNLKDINLK-WWRENIGIVSQEPVLF-GT 149
Cdd:PRK13549   19 KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRdTERAGIAIIHQELALVkEL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 150 TIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLpqKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALd 229
Cdd:PRK13549   98 SVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQL--KLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASL- 174
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2119559688 230 TESE-----GIVQDAlekASHGRTTIVIAHRLSTIKT-ADMIAGFKDG 271
Cdd:PRK13549  175 TESEtavllDIIRDL---KAHGIACIYISHKLNEVKAiSDTICVIRDG 219
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
76-286 2.83e-21

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: 99.98  E-value: 2.83e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   76 ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlkdinlkwwreNIGIVSQEPVLFGTTIEENI 155
Cdd:TIGR01271  441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKDNI 507
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  156 RYGhLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD--TESE 233
Cdd:TIGR01271  508 IFG-LSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDvvTEKE 586
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2119559688  234 gIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQ 286
Cdd:TIGR01271  587 -IFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKR 638
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
58-229 4.51e-21

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 95.68  E-value: 4.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  58 NVQIRGVHFRYPSRPEAkiLYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG--VNlkdiNLKWWRE 135
Cdd:PRK11650    3 GLKLQAVRKSYDGKTQV--IKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvVN----ELEPADR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEPVLF-GTTIEENIRYGhLD---VTKEDIEQ----AAKmanahdfIMDLpqkyETLVGERGAQLSGGQKQRIA 207
Cdd:PRK11650   77 DIAMVFQNYALYpHMSVRENMAYG-LKirgMPKAEIEErvaeAAR-------ILEL----EPLLDRKPRELSGGQRQRVA 144
                         170       180
                  ....*....|....*....|..
gi 2119559688 208 IARALVRNPKILLLDEATSALD 229
Cdd:PRK11650  145 MGRAIVREPAVFLFDEPLSNLD 166
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
60-278 7.10e-21

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 92.91  E-value: 7.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDinlkWWRE---- 135
Cdd:PRK13548    4 EARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLAD----WSPAelar 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEPVL-FGTTIEENI---RYGHLDVTKED---IEQAakMANAhdfimDLpqkyETLVGERGAQLSGGQKQRIAI 208
Cdd:PRK13548   77 RRAVLPQHSSLsFPFTVEEVVamgRAPHGLSRAEDdalVAAA--LAQV-----DL----AHLAGRDYPQLSGGEQQRVQL 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 209 ARALVR------NPKILLLDEATSALD-TESEGIVQDALEKA-SHGRTTIVIAHRLS-TIKTADMIAGFKDGVVAEQGT 278
Cdd:PRK13548  146 ARVLAQlwepdgPPRWLLLDEPTSALDlAHQHHVLRLARQLAhERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGT 224
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
68-285 8.46e-21

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 93.33  E-value: 8.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  68 YPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEP--V 145
Cdd:PRK13652   11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQ 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 146 LFGTTIEENIRYGHLDV------TKEDIEQAAKMANAHDFIMDLPQkyetlvgergaQLSGGQKQRIAIARALVRNPKIL 219
Cdd:PRK13652   91 IFSPTVEQDIAFGPINLgldeetVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVIAMEPQVL 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 220 LLDEATSALDTESEGIVQDALEKAS--HGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNELMSK 285
Cdd:PRK13652  160 VLDEPTAGLDPQGVKELIDFLNDLPetYGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
71-254 9.60e-21

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: 91.56  E-value: 9.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  71 RPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLL---QRFYDPEEGQILIDGVNLKDinlKWWRENIGIVSQEPVLF 147
Cdd:cd03234    17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrVEGGGTTSGQILFNGQPRKP---DQFQKCVAYVRQDDILL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 148 -GTTIEENIRY-GHLDVTKEdieQAAKMANAHDFIMDLPQKYETLVG-ERGAQLSGGQKQRIAIARALVRNPKILLLDEA 224
Cdd:cd03234    94 pGLTVRETLTYtAILRLPRK---SSDAIRKKRVEDVLLRDLALTRIGgNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2119559688 225 TSALDTESE-GIVQDALEKASHGRTTIVIAH 254
Cdd:cd03234   171 TSGLDSFTAlNLVSTLSQLARRNRIVILTIH 201
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
73-282 1.02e-20

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 93.61  E-value: 1.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  73 EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQI--------------LIDGVNLKDI---------- 128
Cdd:PRK13651   19 ELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktkEKEKVLEKLViqktrfkkik 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 129 NLKWWRENIGIVSQ--EPVLFGTTIEENIRYG--HLDVTKEDIEQ-AAKMANahdfIMDLPQKYEtlvgERGA-QLSGGQ 202
Cdd:PRK13651   99 KIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGpvSMGVSKEEAKKrAAKYIE----LVGLDESYL----QRSPfELSGGQ 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 203 KQRIAIARALVRNPKILLLDEATSALDTESegiVQDALEKASH----GRTTIVIAHRL-STIKTADMIAGFKDG-VVAEQ 276
Cdd:PRK13651  171 KRRVALAGILAMEPDFLVFDEPTAGLDPQG---VKEILEIFDNlnkqGKTIILVTHDLdNVLEWTKRTIFFKDGkIIKDG 247

                  ....*.
gi 2119559688 277 GTHNEL 282
Cdd:PRK13651  248 DTYDIL 253
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
76-277 1.03e-20

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 92.60  E-value: 1.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  76 ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPE-----EGQILIDGVNL--KDINLKWWRENIGIVSQEPVLF- 147
Cdd:PRK14267   19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPNPFp 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 148 GTTIEENI----RYGHLDVTKEDI----EQAAKMANAHDFIMDLPQKYEtlvgergAQLSGGQKQRIAIARALVRNPKIL 219
Cdd:PRK14267   99 HLTIYDNVaigvKLNGLVKSKKELdervEWALKKAALWDEVKDRLNDYP-------SNLSGGQRQRLVIARALAMKPKIL 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 220 LLDEATSALDTESEGIVQDALEKASHGRTTIVIAHR-LSTIKTADMIAGFKDGVVAEQG 277
Cdd:PRK14267  172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
74-286 1.08e-20

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: 93.00  E-value: 1.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  74 AKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlkdinlkwwreNIGIVSQEPVLFGTTIEE 153
Cdd:cd03291    50 APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIKE 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 154 NIRYGhLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD--TE 231
Cdd:cd03291   117 NIIFG-VSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDvfTE 195
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 232 SEgIVQDALEKASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGTHNELMSKQ 286
Cdd:cd03291   196 KE-IFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLR 249
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
60-223 1.38e-20

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 91.63  E-value: 1.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKST----IVQLLQrfydPEEGQILIDGvnlKDI-NLKWW- 133
Cdd:COG1137     5 EAENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTtfymIVGLVK----PDSGRIFLDG---EDItHLPMHk 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 134 --RENIGIVSQEPVLF-GTTIEENIRyGHLDVTKEDIEQAAkmanahdfimdlpQKYETLVGE---------RGAQLSGG 201
Cdd:COG1137    75 raRLGIGYLPQEASIFrKLTVEDNIL-AVLELRKLSKKERE-------------ERLEELLEEfgithlrksKAYSLSGG 140
                         170       180
                  ....*....|....*....|..
gi 2119559688 202 QKQRIAIARALVRNPKILLLDE 223
Cdd:COG1137   141 ERRRVEIARALATNPKFILLDE 162
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
79-282 1.54e-20

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: 90.89  E-value: 1.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  79 GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNL----KDInlkwwRENIGIVSQEPVL-FGTTIEE 153
Cdd:cd03265    18 GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVvrepREV-----RRRIGIVFQDLSVdDELTGWE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 154 NIR-----YGHL-DVTKEDIEQAAKManahdfiMDLPQKYETLVGergaQLSGGQKQRIAIARALVRNPKILLLDEATSA 227
Cdd:cd03265    93 NLYiharlYGVPgAERRERIDELLDF-------VGLLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEPTIG 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 228 LDTESEGIVQDALEK--ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNEL 282
Cdd:cd03265   162 LDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
60-235 1.78e-20

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: 91.05  E-value: 1.78e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHFRYPsrpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLkdinLKW-----WR 134
Cdd:TIGR03410   2 EVSNLNVYYG---QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDI----TKLppherAR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 135 ENIGIVSQEPVLFGT-TIEENIRYGhLDVtkedieQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALV 213
Cdd:TIGR03410  75 AGIAYVPQGREIFPRlTVEENLLTG-LAA------LPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALV 147
                         170       180
                  ....*....|....*....|..
gi 2119559688 214 RNPKILLLDEATsaldtesEGI 235
Cdd:TIGR03410 148 TRPKLLLLDEPT-------EGI 162
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
60-283 2.18e-20

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 91.77  E-value: 2.18e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGI 139
Cdd:PRK10575   13 ALRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 VSQE-PVLFGTTIEENI------------RYGHLDvtKEDIEQAAKMANAHDFIMDLPQkyetlvgergaQLSGGQKQRI 206
Cdd:PRK10575   90 LPQQlPAAEGMTVRELVaigrypwhgalgRFGAAD--REKVEEAISLVGLKPLAHRLVD-----------SLSGGERQRA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 207 AIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAhRLSTIKTA----DMIAGFKDGVVAEQGTHNEL 282
Cdd:PRK10575  157 WIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRGGEMIAQGTPAEL 235

                  .
gi 2119559688 283 M 283
Cdd:PRK10575  236 M 236
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
76-284 2.90e-20

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 91.26  E-value: 2.90e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  76 ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRF---YDPE---EGQILIDGVNLKDINLKWWRENIGIVSQEPVLF-G 148
Cdd:PRK14246   25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSKikvDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFpH 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 149 TTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 228
Cdd:PRK14246  105 LSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 229 DTESEGIVQDALEKASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNELMS 284
Cdd:PRK14246  185 DIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIFT 241
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
60-281 3.30e-20

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 95.56  E-value: 3.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHFRYPSRPEA-KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN----LKWWR 134
Cdd:PRK10535    6 ELKDIRRSYPSGEEQvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadalAQLRR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 135 ENIGIVSQE-PVLFGTTIEENIRyghLDVTKEDIEQAAKMANAHDFIMDLpqKYETLVGERGAQLSGGQKQRIAIARALV 213
Cdd:PRK10535   86 EHFGFIFQRyHLLSHLTAAQNVE---VPAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALM 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 214 RNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTIKTADMIAGFKDG-VVAEQGTHNE 281
Cdd:PRK10535  161 NGGQVILADEPTGALDSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAAQAERVIEIRDGeIVRNPPAQEK 230
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
63-297 3.59e-20

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 91.22  E-value: 3.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  63 GVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG--VNLKDINLKWWRENIGIV 140
Cdd:PRK13638    6 DLWFRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGLLALRQQVATV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 141 SQEP--VLFGTTIEENIRYG--HLDVTKEDI----EQAAKMANAHDFIMDLPQkyetlvgergaQLSGGQKQRIAIARAL 212
Cdd:PRK13638   83 FQDPeqQIFYTDIDSDIAFSlrNLGVPEAEItrrvDEALTLVDAQHFRHQPIQ-----------CLSHGQKKRVAIAGAL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 213 VRNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQG------THNELMS 284
Cdd:PRK13638  152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGapgevfACTEAME 231
                         250
                  ....*....|....
gi 2119559688 285 KQGIYQQ-LVTLQS 297
Cdd:PRK13638  232 QAGLTQPwLVKLHT 245
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
694-811 5.35e-20

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 90.53  E-value: 5.35e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRP-DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDlnlqwLRSQI 772
Cdd:COG1116     8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG-----PGPDR 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2119559688 773 GIVSQEPVLFD-RTIAENIAYGDNSREVTMDEIIDAARKA 811
Cdd:COG1116    83 GVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERAREL 122
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
80-299 5.48e-20

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 90.67  E-value: 5.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPvlfGTTIEENIRYGH 159
Cdd:COG4167    32 VSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQDP---NTSLNPRLNIGQ 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 160 -LDV-----TKEDIEQAAKMANahdfimdlpqkyETL--VGERGAQ-------LSGGQKQRIAIARALVRNPKILLLDEA 224
Cdd:COG4167   109 iLEEplrlnTDLTAEEREERIF------------ATLrlVGLLPEHanfyphmLSSGQKQRVALARALILQPKIIIADEA 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 225 TSALDTESEG-IVQDALE-KASHGRTTIVIAHRLSTIK-TADMIAGFKDGVVAEQGTHNELMS--KQGIYQQLVTLQSMK 299
Cdd:COG4167   177 LAALDMSVRSqIINLMLElQEKLGISYIYVSQHLGIVKhISDKVLVMHQGEVVEYGKTAEVFAnpQHEVTKRLIESHFGE 256
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
694-811 6.04e-20

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: 89.31  E-value: 6.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPtrPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIG 773
Cdd:COG1122     1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2119559688 774 IVSQEPV--LFDRTIAENIAYGDNSREVTMDEIIDAARKA 811
Cdd:COG1122    79 LVFQNPDdqLFAPTVEEDVAFGPENLGLPREEIRERVEEA 118
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
67-263 7.03e-20

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 88.06  E-value: 7.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  67 RYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlkdinlkwwRENIGIVSQ---E 143
Cdd:NF040873    1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQrseV 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 144 PVLFGTTIEENI---RYGHLD----VTKEDIEQAAKMANAhdfiMDLpqkyETLVGERGAQLSGGQKQRIAIARALVRNP 216
Cdd:NF040873   67 PDSLPLTVRDLVamgRWARRGlwrrLTRDDRAAVDDALER----VGL----ADLAGRQLGELSGGQRQRALLAQGLAQEA 138
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2119559688 217 KILLLDEATSALDTESEGIVQDAL-EKASHGRTTIVIAHRLSTIKTAD 263
Cdd:NF040873  139 DLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRAD 186
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
75-231 8.19e-20

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 92.07  E-value: 8.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  75 KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDINLKWWRE-NIGIVSQEPVLF-GTTIE 152
Cdd:PRK10851   16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG---TDVSRLHARDrKVGFVFQHYALFrHMTVF 92
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 153 ENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQkYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 231
Cdd:PRK10851   93 DNIAFGLTVLPRRERPNAAAIKAKVTQLLEMVQ-LAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
79-257 1.00e-19

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: 89.71  E-value: 1.00e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  79 GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDIN-LK-WWRENIGIVS--QEPVLFGT-TIEE 153
Cdd:COG0411    22 DVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDG---RDITgLPpHRIARLGIARtfQNPRLFPElTVLE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 154 NIRYGHLDVTKEDIEQA--------AKMANAHDFIMD------LPQKYETLVGErgaqLSGGQKQRIAIARALVRNPKIL 219
Cdd:COG0411    99 NVLVAAHARLGRGLLAAllrlprarREEREARERAEEllervgLADRADEPAGN----LSYGQQRRLEIARALATEPKLL 174
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2119559688 220 LLDEATSAL-DTESEGIVQ--DALeKASHGRTTIVIAHRLS 257
Cdd:COG0411   175 LLDEPAAGLnPEETEELAEliRRL-RDERGITILLIEHDMD 214
cbiO PRK13643
energy-coupling factor transporter ATPase;
59-285 1.07e-19

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 90.18  E-value: 1.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRY-PSRPEA-KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNL----KDINLKW 132
Cdd:PRK13643    2 IKFEKVNYTYqPNSPFAsRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVsstsKQKEIKP 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 133 WRENIGIVSQEP--VLFGTTIEENIRYG--HLDVTKEDIEqaaKMANAHDFIMDLPQKYETlvgERGAQLSGGQKQRIAI 208
Cdd:PRK13643   82 VRKKVGVVFQFPesQLFEETVLKDVAFGpqNFGIPKEKAE---KIAAEKLEMVGLADEFWE---KSPFELSGGQMRRVAI 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 209 ARALVRNPKILLLDEATSALDTESEGIVQDALEKASH-GRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGTHNELMSK 285
Cdd:PRK13643  156 AGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQE 234
cbiO PRK13641
energy-coupling factor transporter ATPase;
59-277 1.86e-19

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 89.50  E-value: 1.86e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRY-PSRP-EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG----VNLKDINLKW 132
Cdd:PRK13641    3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGyhitPETGNKNLKK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 133 WRENIGIVSQ--EPVLFGTTIEENIRYGHLDV---TKEDIEQAAKMANAhdfiMDLPqkyETLVGERGAQLSGGQKQRIA 207
Cdd:PRK13641   83 LRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFgfsEDEAKEKALKWLKK----VGLS---EDLISKSPFELSGGQMRRVA 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 208 IARALVRNPKILLLDEATSALDTES-EGIVQDALEKASHGRTTIVIAHRLstiktaDMIAGFKDGV-VAEQG 277
Cdd:PRK13641  156 IAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNM------DDVAEYADDVlVLEHG 221
ABC_6TM_ABCB9_like cd18784
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ...
410-623 2.07e-19

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: 89.29  E-value: 2.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 410 KIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRLATDASQVQGAAG 489
Cdd:cd18784    34 KFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIVSQEIGFFD--TVKTGDITSRLTSDTTTMSDTVS 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 490 IKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASL 569
Cdd:cd18784   112 LNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSF 191
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 570 TREDMFQKKFNHELQMPYNIALKKAHLIGiGFSLSQAVMFFAYAAS-FWLGAYLI 623
Cdd:cd18784   192 ANEDGEANRYSEKLKDTYKLKIKEALAYG-GYVWSNELTELALTVStLYYGGHLV 245
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
73-277 2.96e-19

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: 86.95  E-value: 2.96e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  73 EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINlkwwRENIGIVSQEPVLF-GTTI 151
Cdd:cd03269    12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYpKMKV 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 152 EENIRY-GHL-DVTKEDIEqaakmANAHDFI--MDLPQKYEtlvgERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 227
Cdd:cd03269    88 IDQLVYlAQLkGLKKEEAR-----RRIDEWLerLELSEYAN----KRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 228 LDTESEGIVQDAL-EKASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQG 277
Cdd:cd03269   159 LDPVNVELLKDVIrELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
76-254 3.03e-19

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 87.53  E-value: 3.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  76 ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN----LKWWRENIGIVSQEPVLFGT-T 150
Cdd:PRK10584   25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeearAKLRAKHVGFVFQSFMLIPTlN 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 151 IEENIRYGHLdVTKEDIEQAAKMANAHDFIMDLPQKYETLvgerGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 230
Cdd:PRK10584  105 ALENVELPAL-LRGESSRQSRNGAKALLEQLGLGKRLDHL----PAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR 179
                         170       180
                  ....*....|....*....|....*.
gi 2119559688 231 ESEGIVQDALEKAS--HGRTTIVIAH 254
Cdd:PRK10584  180 QTGDKIADLLFSLNreHGTTLILVTH 205
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
694-811 4.19e-19

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: 86.76  E-value: 4.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPT-RPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNlqwlrSQI 772
Cdd:cd03293     1 LEVRNVSKTYGGgGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-----PDR 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2119559688 773 GIVSQEPVLFD-RTIAENIAYGDNSREVTMDEIIDAARKA 811
Cdd:cd03293    76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEARERAEEL 115
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
70-265 5.42e-19

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: 84.90  E-value: 5.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  70 SRPEAKILYG-VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDgvnlkdinlkwWRENIGIVSQEPVLFG 148
Cdd:cd03223     9 ATPDGRVLLKdLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMP-----------EGEDLLFLPQRPYLPL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 149 TTIEENIRYGHLDVtkedieqaakmanahdfimdlpqkyetlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSAL 228
Cdd:cd03223    78 GTLREQLIYPWDDV-----------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSAL 122
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2119559688 229 DTESEGIVQDALEKasHGRTTIVIAHRLSTIKTADMI 265
Cdd:cd03223   123 DEESEDRLYQLLKE--LGITVISVGHRPSLWKFHDRV 157
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
80-302 7.14e-19

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 87.35  E-value: 7.14e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFG-TTIEENI--- 155
Cdd:PRK10253   26 LTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTPGdITVQELVarg 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 156 RYGHLDV----TKEDIEQAAKMANAHDFIMDLPQKYETlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 231
Cdd:PRK10253  106 RYPHQPLftrwRKEDEEAVTKAMQATGITHLADQSVDT--------LSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 232 SEgivQDALEKASH-----GRTTIVIAHRLS-TIKTADMIAGFKDGVVAEQGTHNELMSKQGIyQQLVTLQSMKSAD 302
Cdd:PRK10253  178 HQ---IDLLELLSElnrekGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVTAELI-ERIYGLRCMIIDD 250
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
31-295 9.37e-19

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 90.53  E-value: 9.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  31 YLYQLITMDP-----PIDSYSTEGKKLDNFQGNVQIRGVHFRYpSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQ 105
Cdd:PRK15134  252 YTQKLLNSEPsgdpvPLPEPASPLLDVEQLQVAFPIRKGILKR-TVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGL 330
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 106 LLQRFYdPEEGQILIDGVNLKDINLKW---WRENIGIVSQEP---------VLfgTTIEENIRYGHLDVTKEDIEQAAKM 173
Cdd:PRK15134  331 ALLRLI-NSQGEIWFDGQPLHNLNRRQllpVRHRIQVVFQDPnsslnprlnVL--QIIEEGLRVHQPTLSAAQREQQVIA 407
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 174 AnAHDFIMD--LPQKYEtlvgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTT 249
Cdd:PRK15134  408 V-MEEVGLDpeTRHRYP-------AEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSlqQKHQLAY 479
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 2119559688 250 IVIAHRLSTIKT-ADMIAGFKDGVVAEQGTHNELMS--KQGIYQQLVTL 295
Cdd:PRK15134  480 LFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFAapQQEYTRQLLAL 528
ABC_6TM_TmrB_like cd18541
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...
387-627 1.51e-18

Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-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. 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. However, 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: 349985 [Multi-domain]  Cd Length: 293  Bit Score: 87.08  E-value: 1.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 387 AFAVIFSEILGVF--AILDEGEQERKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFd 464
Cdd:cd18541    13 LLQLLIPRIIGRAidALTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLFAHLLTLSPSFY- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 465 dHNNSVGALTTRLATDASQVQGAAGIKLgssLMAFCSVVTGI-VIGFVF--SWKITLLVIAFLPFVMIGGALEMQMMQGA 541
Cdd:cd18541    92 -QKNRTGDLMARATNDLNAVRMALGPGI---LYLVDALFLGVlVLVMMFtiSPKLTLIALLPLPLLALLVYRLGKKIHKR 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 542 AGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGAY 621
Cdd:cd18541   168 FRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFLIVLWYGGR 247

                  ....*.
gi 2119559688 622 LIKQSE 627
Cdd:cd18541   248 LVIRGT 253
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
70-253 1.71e-18

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: 84.47  E-value: 1.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  70 SRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGT 149
Cdd:cd03231     9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 150 TIEENIRYGHLDVTKEDIEQAAKMANAHDFiMDLPqkyetlvgerGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 229
Cdd:cd03231    89 SVLENLRFWHADHSDEQVEEALARVGLNGF-EDRP----------VAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
                         170       180
                  ....*....|....*....|....*
gi 2119559688 230 TESEGIVQDALekASH-GRTTIVIA 253
Cdd:cd03231   158 KAGVARFAEAM--AGHcARGGMVVL 180
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
694-791 1.84e-18

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: 85.43  E-value: 1.84e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRPdtTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIG 773
Cdd:cd03295     1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
                          90
                  ....*....|....*....
gi 2119559688 774 IVSQEPVLF-DRTIAENIA 791
Cdd:cd03295    79 YVIQQIGLFpHMTVEENIA 97
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
60-285 2.14e-18

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 85.50  E-value: 2.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHFRypsrPEAK-ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLL--QRFYDPEEGQILIDGVNLKDinlkwW--- 133
Cdd:COG0396     2 EIKNLHVS----VEGKeILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILE-----Lspd 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 134 ---RENIGIVSQEPVLF-GTTIEENIR--YGHLDVTKEDIEQAAKMANAHDFIMDLPQKYetlvGERG--AQLSGGQKQR 205
Cdd:COG0396    73 eraRAGIFLAFQYPVEIpGVSVSNFLRtaLNARRGEELSAREFLKLLKEKMKELGLDEDF----LDRYvnEGFSGGEKKR 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 206 IAIARALVRNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAH--RLSTIKTADMIAGFKDGVVAEQGTHnEL 282
Cdd:COG0396   149 NEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKlRSPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGK-EL 227

                  ...
gi 2119559688 283 MSK 285
Cdd:COG0396   228 ALE 230
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
60-277 3.34e-18

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: 83.73  E-value: 3.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHFrypSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPE--EGQILIDGVNLKDINL-KWWREN 136
Cdd:cd03217     2 EIKDLHV---SVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITDLPPeERARLG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLF-GTTIEENIRYghldvtkedieqaakmanahdfimdlpqkyetlVGErgaQLSGGQKQRIAIARALVRN 215
Cdd:cd03217    79 IFLAFQYPPEIpGVKNADFLRY---------------------------------VNE---GFSGGEKKRNEILQLLLLE 122
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 216 PKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAH--RLSTIKTADMIAGFKDGVVAEQG 277
Cdd:cd03217   123 PDLAILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
694-811 4.35e-18

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: 88.42  E-value: 4.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRP--DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN---LQWL 768
Cdd:COG1123   261 LEVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSrrsLREL 340
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2119559688 769 RSQIGIVSQEPV--LFDR-TIAENIAYG-DNSREVTMDEIIDAARKA 811
Cdd:COG1123   341 RRRVQMVFQDPYssLNPRmTVGDIIAEPlRLHGLLSRAERRERVAEL 387
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
59-254 5.21e-18

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 81.34  E-value: 5.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDgvnlkdinlkwwrenig 138
Cdd:cd03221     1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG----------------- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 ivsqepvlfgttieENIRYGHLDvtkedieqaakmanahdfimdlpqkyetlvgergaQLSGGQKQRIAIARALVRNPKI 218
Cdd:cd03221    61 --------------STVKIGYFE-----------------------------------QLSGGEKMRLALAKLLLENPNL 91
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2119559688 219 LLLDEATSALDTESegivQDALEKA--SHGRTTIVIAH 254
Cdd:cd03221    92 LLLDEPTNHLDLES----IEALEEAlkEYPGTVILVSH 125
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
694-790 9.44e-18

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: 81.49  E-value: 9.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIG 773
Cdd:cd03246     1 LEVENVSFRYPGA-EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
                          90
                  ....*....|....*..
gi 2119559688 774 IVSQEPVLFDRTIAENI 790
Cdd:cd03246    80 YLPQDDELFSGSIAENI 96
ABC_6TM_YknU_like cd18542
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...
388-623 1.26e-17

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD 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 and a various type of lipids. 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. However, 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: 349986 [Multi-domain]  Cd Length: 292  Bit Score: 84.02  E-value: 1.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 388 FAVIFSEILGVFA------ILDE---GEQERKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQ 458
Cdd:cd18542     6 LALLLATALNLLIpllirrIIDSvigGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYDHLQRL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 459 EIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMM 538
Cdd:cd18542    86 SFSFHD--KARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFFKKV 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 539 QGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAASFWL 618
Cdd:cd18542   164 RPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLVLWV 243

                  ....*
gi 2119559688 619 GAYLI 623
Cdd:cd18542   244 GGYLV 248
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
77-259 1.35e-17

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 82.62  E-value: 1.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  77 LYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVN---LKDINLKWWRENIGIVSQEP-VLFGTTIE 152
Cdd:PRK10908   18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrLKNREVPFLRRQIGMIFQDHhLLMDRTVY 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 153 ENIRYGHL--DVTKEDIEQAAKMANAHDFIMDLPQKYETlvgergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 230
Cdd:PRK10908   98 DNVAIPLIiaGASGDDIRRRVSAALDKVGLLDKAKNFPI-------QLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
                         170       180       190
                  ....*....|....*....|....*....|
gi 2119559688 231 E-SEGIVQDALEKASHGRTTIVIAHRLSTI 259
Cdd:PRK10908  171 AlSEGILRLFEEFNRVGVTVLMATHDIGLI 200
ABC_6TM_TmrA_like cd18544
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...
411-628 1.35e-17

Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-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. 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. However, 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: 349988 [Multi-domain]  Cd Length: 294  Bit Score: 83.98  E-value: 1.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 411 IIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRLATDASQV-----Q 485
Cdd:cd18544    40 LLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLFSHIQRLPLSFFD--RTPVGRLVTRVTNDTEALnelftS 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 486 GAAGIkLGSSLMafcsvVTGIVIG-FVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEAL-ESAGKIAiESIENI 563
Cdd:cd18544   118 GLVTL-IGDLLL-----LIGILIAmFLLNWRLALISLLVLPLLLLATYLFRKKSRKAYREVREKLsRLNAFLQ-ESISGM 190
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 564 RTVASLTREDMFQKKFNHelqmpYNIALKKAHLIGI-GFSLSQAVMFFAYAAS----FWLGAYLIKQSEV 628
Cdd:cd18544   191 SVIQLFNREKREFEEFDE-----INQEYRKANLKSIkLFALFRPLVELLSSLAlalvLWYGGGQVLSGAV 255
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
59-286 1.55e-17

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 83.66  E-value: 1.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN---LKWWRE 135
Cdd:PRK11831    8 VDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrLYTVRK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 136 NIGIVSQEPVLF-GTTIEENIRY---GHLDVTKEDIEQAAKManahdfimdlpqKYETlVGERGA------QLSGGQKQR 205
Cdd:PRK11831   85 RMSMLFQSGALFtDMNVFDNVAYplrEHTQLPAPLLHSTVMM------------KLEA-VGLRGAaklmpsELSGGMARR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 206 IAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASH--GRTTIVIAHR----LSTIKTADMIAGFKdgVVAEqGTH 279
Cdd:PRK11831  152 AALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDvpevLSIADHAYIVADKK--IVAH-GSA 228

                  ....*..
gi 2119559688 280 NELMSKQ 286
Cdd:PRK11831  229 QALQANP 235
GguA NF040905
sugar ABC transporter ATP-binding protein;
72-271 1.81e-17

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 86.38  E-value: 1.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  72 PEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYdPE---EGQILIDG--VNLKDINLKwwrENIGIV--SQE- 143
Cdd:NF040905   12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGevCRFKDIRDS---EALGIViiHQEl 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 144 ---PVLfgtTIEENIRYGHldvtkediEQAAKManahdfIMDLPQKY----------------ETLVGERGAqlsgGQKQ 204
Cdd:NF040905   88 aliPYL---SIAENIFLGN--------ERAKRG------VIDWNETNrrarellakvgldespDTLVTDIGV----GKQQ 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 205 RIAIARALVRNPKILLLDEATSAL-DTESEGIVQDALEKASHGRTTIVIAHRLSTI-KTADMIAGFKDG 271
Cdd:NF040905  147 LVEIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDG 215
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
370-784 1.98e-17

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: 86.39  E-value: 1.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 370 FIVMGCFASLVNGGAMpafAVIFSEILGVFAILDegeqerkiiQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRS 449
Cdd:COG4615    18 ALLLGLLSGLANAGLI---ALINQALNATGAALA---------RLLLLFAGLLVLLLLSRLASQLLLTRLGQHAVARLRL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 450 MSFKAMLRQEIAFFDdhnnSVGA--LTTRLATDASQVQGAAgiklgSSLMAFCSVVTGIVIGFVF----SWKITLLVIAF 523
Cdd:COG4615    86 RLSRRILAAPLERLE----RIGAarLLAALTEDVRTISQAF-----VRLPELLQSVALVLGCLAYlawlSPPLFLLTLVL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 524 LPFVMIGGALEMQMMQ---GAAGKNKEALesagkiaiesIENIRTVA---------SLTREDMFQKKFNH--ELQMPYNI 589
Cdd:COG4615   157 LGLGVAGYRLLVRRARrhlRRAREAEDRL----------FKHFRALLegfkelklnRRRRRAFFDEDLQPtaERYRDLRI 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 590 alkKAHLI-GIGFSLSQAVMFFAYAASFWLGAYLikqSEVDYVDVFKAFSAILFGGMAIGNASAFAPDAAKAEQSAKEIF 668
Cdd:COG4615   227 ---RADTIfALANNWGNLLFFALIGLILFLLPAL---GWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKIE 300
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 669 KL---IDKKPDIDNESEKGEQLHTFTAnLSFANIIFRYPTRPDTT--ILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTE 743
Cdd:COG4615   301 ELelaLAAAEPAAADAAAPPAPADFQT-LELRGVTYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLT 379
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 2119559688 744 RFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDR 784
Cdd:COG4615   380 GLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFDR 420
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
705-811 1.99e-17

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: 81.80  E-value: 1.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 705 TRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwlRSQIGIVSQEPVLFD- 783
Cdd:cd03259     9 TYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVFQDYALFPh 86
                          90       100
                  ....*....|....*....|....*...
gi 2119559688 784 RTIAENIAYGDNSREVTMDEIIDAARKA 811
Cdd:cd03259    87 LTVAENIAFGLKLRGVPKAEIRARVREL 114
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
72-271 3.13e-17

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 85.73  E-value: 3.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  72 PEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRE-NIGIVSQE----PVL 146
Cdd:PRK11288   15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAaGVAIIYQElhlvPEM 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 147 fgtTIEENIRYGHLD-----VTKEDIEQAAKMANAH---DFIMDLPQKYetlvgergaqLSGGQKQRIAIARALVRNPKI 218
Cdd:PRK11288   95 ---TVAENLYLGQLPhkggiVNRRLLNYEAREQLEHlgvDIDPDTPLKY----------LSIGQRQMVEIAKALARNARV 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 219 LLLDEATSALDT-ESEGI--VQDALEkaSHGRTTIVIAHRLSTI-KTADMIAGFKDG 271
Cdd:PRK11288  162 IAFDEPTSSLSArEIEQLfrVIRELR--AEGRVILYVSHRMEEIfALCDAITVFKDG 216
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
59-282 4.01e-17

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 82.85  E-value: 4.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINlkwwRENIG 138
Cdd:COG4152     2 LELKGLTKRFGDK---TAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLF-GTTIEENIRY-GHL-DVTKEDIEQAAKmanahDFI--MDLPQKYETLVGErgaqLSGGQKQRIAIARALV 213
Cdd:COG4152    75 YLPEERGLYpKMKVGEQLVYlARLkGLSKAEAKRRAD-----EWLerLGLGDRANKKVEE----LSKGNQQKVQLIAALL 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 214 RNPKILLLDEATSALDTESEGIVQDAL-EKASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNEL 282
Cdd:COG4152   146 HDPELLILDEPFSGLDPVNVELLKDVIrELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
60-271 4.86e-17

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 85.06  E-value: 4.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHfryPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDINLKWWREN--- 136
Cdd:PRK10762    6 QLKGID---KAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLG---KEVTFNGPKSSqea 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 -IGIVSQEPVLFGT-TIEENIRYGHLDVTKEDIEQAAKM-ANAHDFIMDLPQKY--ETLVGErgaqLSGGQKQRIAIARA 211
Cdd:PRK10762   80 gIGIIHQELNLIPQlTIAENIFLGREFVNRFGRIDWKKMyAEADKLLARLNLRFssDKLVGE----LSIGEQQMVEIAKV 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 212 LVRNPKILLLDEATSAL-DTESEGIVQDALEKASHGRTTIVIAHRLSTI-KTADMIAGFKDG 271
Cdd:PRK10762  156 LSFESKVIIMDEPTDALtDTETESLFRVIRELKSQGRGIVYISHRLKEIfEICDDVTVFRDG 217
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
71-257 4.93e-17

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 85.48  E-value: 4.93e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  71 RPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQrFYDPE----EGQILIDGvnlKDINLKWWRENIGIVSQEPVL 146
Cdd:TIGR00955  35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNG---MPIDAKEMRAISAYVQQDDLF 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 147 FGT-TIEENIRY-GHLDVtKEDIEQAAKMANAHDFI--MDLPQKYETLVGERGAQ--LSGGQKQRIAIARALVRNPKILL 220
Cdd:TIGR00955 111 IPTlTVREHLMFqAHLRM-PRRVTKKEKRERVDEVLqaLGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLF 189
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2119559688 221 LDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLS 257
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPS 227
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
80-229 7.17e-17

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 83.00  E-value: 7.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNL----KDINLKWWRENIGIVSQEPVLF-GTTIEEN 154
Cdd:PRK11144   17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdaeKGICLPPEKRRIGYVFQDARLFpHYKVRGN 96
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 155 IRYGhldvtkedieQAAKMANAHDFIMDLpQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 229
Cdd:PRK11144   97 LRYG----------MAKSMVAQFDKIVAL-LGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
75-228 7.78e-17

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 80.69  E-value: 7.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  75 KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDINlKW-----WRENIGIVSQEPVLFG- 148
Cdd:PRK11614   19 QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDG---KDIT-DWqtakiMREAVAIVPEGRRVFSr 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 149 TTIEENIRYGHLDVTKEDIEQaaKMANAHDFimdLPQKYETLVgERGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL 228
Cdd:PRK11614   95 MTVEENLAMGGFFAERDQFQE--RIKWVYEL---FPRLHERRI-QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL 168
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
76-284 8.09e-17

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 81.68  E-value: 8.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  76 ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDP-----EEGQILIDG---VNLKDInlKWWRENIGIVSQEPVLF 147
Cdd:PRK14271   36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGrsiFNYRDV--LEFRRRVGMLFQRPNPF 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 148 GTTIEENIRYG---HLDVTKEDIEQAAKmanAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEA 224
Cdd:PRK14271  114 PMSIMDNVLAGvraHKLVPRKEFRGVAQ---ARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEP 190
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 225 TSALDTESEGIVQDALEKASHGRTTIVIAHRLS-TIKTADMIAGFKDGVVAEQGTHNELMS 284
Cdd:PRK14271  191 TSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFS 251
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
77-271 9.10e-17

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 84.07  E-value: 9.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  77 LYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWREN-IGIVSQE-PVLFGTTIEEN 154
Cdd:PRK09700   21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLgIGIIYQElSVIDELTVLEN 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 155 IRYGHLDVTKE------DIEQAAKMANAHDFIMDLPQKYETLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSAL 228
Cdd:PRK09700  101 LYIGRHLTKKVcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2119559688 229 -DTESEGIVQDALEKASHGRTTIVIAHRLSTIK-TADMIAGFKDG 271
Cdd:PRK09700  177 tNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRrICDRYTVMKDG 221
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
33-234 1.00e-16

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 84.52  E-value: 1.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  33 YQLITM-DPPIDSYSTEGKKLDNFQGNVQIRGVHFRYPSRP--------EAKILYGVNLQIKRGQTVALVGSSGCGKSTI 103
Cdd:PRK10261  287 FPLISLeHPAKQEPPIEQDTVVDGEPILQVRNLVTRFPLRSgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTT 366
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 104 VQLLQRFYDPEEGQILIDGV---NLKDINLKWWRENIGIVSQEPV-------LFGTTIEENIRYGHLDVTKEDIEQAAKM 173
Cdd:PRK10261  367 GRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDPYasldprqTVGDSIMEPLRVHGLLPGKAAAARVAWL 446
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 174 ANAHDFIMDLPQKYEtlvgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEG 234
Cdd:PRK10261  447 LERVGLLPEHAWRYP-------HEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRG 500
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
708-813 1.08e-16

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 80.85  E-value: 1.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYD--P---ADGIVSLDGHNL--KDLNLQWLRSQIGIVSQEPV 780
Cdd:COG1117    23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDIydPDVDVVELRRRVGMVFQKPN 102
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2119559688 781 LFDRTIAENIAYG-----DNSREVtMDEIIDAA-RKANI 813
Cdd:COG1117   103 PFPKSIYDNVAYGlrlhgIKSKSE-LDEIVEESlRKAAL 140
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
59-275 1.20e-16

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 83.96  E-value: 1.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIdGVNLKdinlkwwrenIG 138
Cdd:COG0488   316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IG 381
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVLF--GTTIEENIRYGHLDVTKEDIEQAAKmanahDFimdL--PQKYETLVGErgaqLSGGQKQRIAIARALVR 214
Cdd:COG0488   382 YFDQHQEELdpDKTVLDELRDGAPGGTEQEVRGYLG-----RF---LfsGDDAFKPVGV----LSGGEKARLALAKLLLS 449
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 215 NPKILLLDEATSALDTESEGIVQDALEKAShGrTTIVIAH-R--LSTIktADMIAGFKDGVVAE 275
Cdd:COG0488   450 PPNVLLLDEPTNHLDIETLEALEEALDDFP-G-TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
694-811 1.22e-16

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 82.45  E-value: 1.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPtrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwlRSQIG 773
Cdd:COG3842     6 LELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVG 80
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2119559688 774 IVSQEPVLF-DRTIAENIAYGDNSREVTMDEIIDAARKA 811
Cdd:COG3842    81 MVFQDYALFpHLTVAENVAFGLRMRGVPKAEIRARVAEL 119
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
59-254 1.40e-16

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 81.80  E-value: 1.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDiNLKWWRENIG 138
Cdd:PRK13536   42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIG 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQEPVL---FgtTIEEN-IRYG-HLDVTKEDIEqaAKMANAHDFimdlpQKYETLVGERGAQLSGGQKQRIAIARALV 213
Cdd:PRK13536  118 VVPQFDNLdleF--TVRENlLVFGrYFGMSTREIE--AVIPSLLEF-----ARLESKADARVSDLSGGMKRRLTLARALI 188
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2119559688 214 RNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAH 254
Cdd:PRK13536  189 NDPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTH 230
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
695-811 1.41e-16

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: 79.05  E-value: 1.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 695 SFANIIFRYPTRpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGI 774
Cdd:cd03225     1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2119559688 775 VSQEP--VLFDRTIAENIAYGDNSREVTMDEIIDAARKA 811
Cdd:cd03225    80 VFQNPddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEA 118
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
708-792 2.52e-16

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: 79.25  E-value: 2.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN---LQWLRSQIGIVSQEPVLFD- 783
Cdd:COG1127    17 DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRRRIGMLFQGGALFDs 96

                  ....*....
gi 2119559688 784 RTIAENIAY 792
Cdd:COG1127    97 LTVFENVAF 105
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
62-277 2.83e-16

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: 78.73  E-value: 2.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  62 RGVHFRYPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlkdiNLKWWRE-NIGIv 140
Cdd:cd03220    23 LGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------RVSSLLGlGGGF- 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 141 sqEPVLfgtTIEENIRYGH--LDVTKEDIEQaaKMANAHDFiMDLPQKYETLVGErgaqLSGGQKQRIAIARALVRNPKI 218
Cdd:cd03220    96 --NPEL---TGRENIYLNGrlLGLSRKEIDE--KIDEIIEF-SELGDFIDLPVKT----YSSGMKARLAFAIATALEPDI 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 219 LLLDEATSALDTESEGIVQDAL-EKASHGRTTIVIAHRLSTIK-TADMIAGFKDGVVAEQG 277
Cdd:cd03220   164 LLIDEVLAVGDAAFQEKCQRRLrELLKQGKTVILVSHDPSSIKrLCDRALVLEKGKIRFDG 224
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
76-278 3.09e-16

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 78.70  E-value: 3.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  76 ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN----LKWWRENIGIVSQ-EPVLFGTT 150
Cdd:PRK11629   24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaakAELRNQKLGFIYQfHHLLPDFT 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 151 IEENIRYGHL---DVTKEDIEQAAKMANAhdfiMDLPQKyetlVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSA 227
Cdd:PRK11629  104 ALENVAMPLLigkKKPAEINSRALEMLAA----VGLEHR----ANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 228 LDTESEGIVQDALEK--ASHGRTTIVIAHRLSTIKTADMIAGFKDGVVAEQGT 278
Cdd:PRK11629  176 LDARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAELS 228
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
59-282 3.76e-16

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 82.41  E-value: 3.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN-LKWWRENI 137
Cdd:PRK15439   12 LCARSISKQYSGVE---VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKAHQLGI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 GIVSQEPVLFGT-TIEENIRYG---HLDvTKEDIEQAAKMANAHdfiMDLPQKYETL-VGERgaqlsggqkQRIAIARAL 212
Cdd:PRK15439   89 YLVPQEPLLFPNlSVKENILFGlpkRQA-SMQKMKQLLAALGCQ---LDLDSSAGSLeVADR---------QIVEILRGL 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 213 VRNPKILLLDEATSALD-TESEGIVQDALEKASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNEL 282
Cdd:PRK15439  156 MRDSRILILDEPTASLTpAETERLFSRIRELLAQGVGIVFISHKLPEIrQLADRISVMRDGTIALSGKTADL 227
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
694-809 3.89e-16

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: 77.84  E-value: 3.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYptRPD-TTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQI 772
Cdd:cd03369     7 IEVENLSVRY--APDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2119559688 773 GIVSQEPVLFDRTIAENIaygDNSREVTMDEIIDAAR 809
Cdd:cd03369    85 TIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGALR 118
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
695-777 5.46e-16

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: 76.13  E-value: 5.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 695 SFANIIFRYPTRPdttILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGI 774
Cdd:cd00267     1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77

                  ...
gi 2119559688 775 VSQ 777
Cdd:cd00267    78 VPQ 80
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
70-273 6.25e-16

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 80.66  E-value: 6.25e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  70 SRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVL-FG 148
Cdd:PRK09536   12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 149 TTIEENIRYG---HL-------DVTKEDIEQAAKMANAHDFImDLPQkyetlvgergAQLSGGQKQRIAIARALVRNPKI 218
Cdd:PRK09536   92 FDVRQVVEMGrtpHRsrfdtwtETDRAAVERAMERTGVAQFA-DRPV----------TSLSGGERQRVLLARALAQATPV 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 219 LLLDEATSALDTESE----GIVQDALEKashGRTTIVIAHRLstiktaDMIAGFKDGVV 273
Cdd:PRK09536  161 LLLDEPTASLDINHQvrtlELVRRLVDD---GKTAVAAIHDL------DLAARYCDELV 210
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
70-253 7.35e-16

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: 76.63  E-value: 7.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  70 SRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWwRENIGIVSQEPVLFGT 149
Cdd:TIGR01189   9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-HENILYLGHLPGLKPE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 150 -TIEENIRYGH--LDVTKEDIEQAAKMANAHDFiMDLPqkyetlvgerGAQLSGGQKQRIAIARALVRNPKILLLDEATS 226
Cdd:TIGR01189  88 lSALENLHFWAaiHGGAQRTIEDALAAVGLTGF-EDLP----------AAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156
                         170       180
                  ....*....|....*....|....*...
gi 2119559688 227 ALDTESEGIVQDALekASH-GRTTIVIA 253
Cdd:TIGR01189 157 ALDKAGVALLAGLL--RAHlARGGIVLL 182
ABC_6TM_Tm287_like cd18548
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...
401-667 7.53e-16

Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD 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: 349992 [Multi-domain]  Cd Length: 292  Bit Score: 78.98  E-value: 7.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 401 ILDEGEQER---KIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDHnnSVGALTTRL 477
Cdd:cd18548    25 IIDEGIANGdlsYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEKIQSFSFAEIDKF--GTSSLITRL 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 478 ATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAI 557
Cdd:cd18548   103 TNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVR 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 558 ESIENIRTVASLTREDMFQKKF---NHELqmpYNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLIKQSEVDYVDVF 634
Cdd:cd18548   183 ENLTGIRVIRAFNREDYEEERFdkaNDDL---TDTSLKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLV 259
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2119559688 635 kAFSA----ILFGGMAIGNASAFAPdaaKAEQSAKEI 667
Cdd:cd18548   260 -AFINylmqILMSLMMLSMVFVMLP---RASASAKRI 292
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
694-793 7.76e-16

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: 76.07  E-value: 7.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPtrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQW--LRSQ 771
Cdd:cd03229     1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRR 77
                          90       100
                  ....*....|....*....|...
gi 2119559688 772 IGIVSQEPVLFDR-TIAENIAYG 793
Cdd:cd03229    78 IGMVFQDFALFPHlTVLENIALG 100
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
75-285 1.03e-15

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 81.00  E-value: 1.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  75 KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRF--YDPEEGQIL--------------------------------- 119
Cdd:TIGR03269  14 EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvgepcpvcggtlepee 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 120 IDGVNLKDINLKWWRENIGIVSQEP-VLFGT-TIEENIRYGHLDV---TKEDIEQAA---KMANAHDFIMDLPQkyetlv 191
Cdd:TIGR03269  94 VDFWNLSDKLRRRIRKRIAIMLQRTfALYGDdTVLDNVLEALEEIgyeGKEAVGRAVdliEMVQLSHRITHIAR------ 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 192 gergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKA--SHGRTTIVIAHRLSTI-KTADMIAGF 268
Cdd:TIGR03269 168 -----DLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIeDLSDKAIWL 242
                         250
                  ....*....|....*..
gi 2119559688 269 KDGVVAEQGTHNELMSK 285
Cdd:TIGR03269 243 ENGEIKEEGTPDEVVAV 259
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
694-793 1.10e-15

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: 77.78  E-value: 1.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRPdttILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIG 773
Cdd:COG1120     2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIA 78
                          90       100
                  ....*....|....*....|.
gi 2119559688 774 IVSQEPVL-FDRTIAENIAYG 793
Cdd:COG1120    79 YVPQEPPApFGLTVRELVALG 99
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
66-284 1.17e-15

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 77.91  E-value: 1.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  66 FRYPS----RPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVS 141
Cdd:PRK15112   14 FRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIF 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 142 QEPvlfGTTIEENIRYGH-LDV-----TKEDIEQAAKmanahdfimdlpQKYETL--VGERGAQ-------LSGGQKQRI 206
Cdd:PRK15112   94 QDP---STSLNPRQRISQiLDFplrlnTDLEPEQREK------------QIIETLrqVGLLPDHasyyphmLAPGQKQRL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 207 AIARALVRNPKILLLDEATSALD-TESEGIVQDALE-KASHGRTTIVIAHRLSTIK-TADMIAGFKDGVVAEQGTHNELM 283
Cdd:PRK15112  159 GLARALILRPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKhISDQVLVMHQGEVVERGSTADVL 238

                  .
gi 2119559688 284 S 284
Cdd:PRK15112  239 A 239
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
75-271 1.19e-15

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 80.64  E-value: 1.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  75 KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYdPE---EGQILIDGVNLKDINLK-WWRENIGIVSQEPVLF-GT 149
Cdd:TIGR02633  15 KALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRdTERAGIVIIHQELTLVpEL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 150 TIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSAL- 228
Cdd:TIGR02633  94 SVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLt 173
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2119559688 229 DTESEGIVQDALEKASHGRTTIVIAHRLSTIKT-ADMIAGFKDG 271
Cdd:TIGR02633 174 EKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDG 217
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
75-258 1.23e-15

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: 76.13  E-value: 1.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  75 KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLL-QRFYDPE-EGQILIDGvNLKDINLkwwRENIGIVSQEPVLFGT-TI 151
Cdd:cd03232    21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILING-RPLDKNF---QRSTGYVEQQDVHSPNlTV 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 152 EENIRYghldvtkedieqAAKManahdfimdlpqkyetlvgeRGaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTE 231
Cdd:cd03232    97 REALRF------------SALL--------------------RG--LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQ 142
                         170       180
                  ....*....|....*....|....*...
gi 2119559688 232 SEGIVQDALEK-ASHGRTTIVIAHRLST 258
Cdd:cd03232   143 AAYNIVRFLKKlADSGQAILCTIHQPSA 170
ABC_6TM_exporter_like cd18550
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
388-628 1.40e-15

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes 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. 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 the chemical 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. However, 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: 349994 [Multi-domain]  Cd Length: 294  Bit Score: 78.29  E-value: 1.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 388 FAVIFSEILGVF------AILDEGEQERKI---IQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQ 458
Cdd:cd18550     6 LLILLSALLGLLpplllrEIIDDALPQGDLgllVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAHLQRM 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 459 EIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMM 538
Cdd:cd18550    86 SLAFFT--RTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGRRR 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 539 QGAAGKNKEALESAGKIAIE--SIENIRTVASLTREDMFQKKFNHELQMPYNIALkKAHLIGIGFSLS-QAVMFFAYAAS 615
Cdd:cd18550   164 RKLTREQQEKLAELNSIMQEtlSVSGALLVKLFGREDDEAARFARRSRELRDLGV-RQALAGRWFFAAlGLFTAIGPALV 242
                         250
                  ....*....|...
gi 2119559688 616 FWLGAYLIKQSEV 628
Cdd:cd18550   243 YWVGGLLVIGGGL 255
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
75-278 1.44e-15

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 77.36  E-value: 1.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  75 KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYD----PEEGQILI------DGVNLKDINLKwwRENIGIVSQEP 144
Cdd:PRK09984   18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGSHIELLgrtvqrEGRLARDIRKS--RANTGYIFQQF 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 145 VLFGT-TIEENIRYGHLDVT--------------KEDIEQA-AKMANAHdfimdlpqkyetLVGERGAQLSGGQKQRIAI 208
Cdd:PRK09984   96 NLVNRlSVLENVLIGALGSTpfwrtcfswftreqKQRALQAlTRVGMVH------------FAHQRVSTLSGGQQQRVAI 163
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 209 ARALVRNPKILLLDEATSALDTESEGIVQDALEKASH--GRTTIVIAHRLS-TIKTADMIAGFKDGVVAEQGT 278
Cdd:PRK09984  164 ARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDGS 236
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
67-278 1.55e-15

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 77.04  E-value: 1.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  67 RYPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlkdinlkwwrenigIVSqePVL 146
Cdd:COG1134    32 RRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG----------------RVS--ALL 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 147 -FGT------TIEENIRYG--HLDVTKEDIEqaAKMANAHDF--I---MDLPQKYetlvgergaqLSGGQKQRIAIARAL 212
Cdd:COG1134    94 eLGAgfhpelTGRENIYLNgrLLGLSRKEID--EKFDEIVEFaeLgdfIDQPVKT----------YSSGMRARLAFAVAT 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 213 VRNPKILLLDEATSALDTE----SEGIVQdalEKASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGT 278
Cdd:COG1134   162 AVDPDILLVDEVLAVGDAAfqkkCLARIR---ELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
ABC_6TM_TAP1 cd18589
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ...
401-617 1.65e-15

Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); 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: 350033 [Multi-domain]  Cd Length: 289  Bit Score: 77.90  E-value: 1.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 401 ILDEGEQERKIIQYVLMFVgVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRLATD 480
Cdd:cd18589    26 IMNKDAPEAFTAAITVMSL-LTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEIAFFD--SNQTGDIVSRVTTD 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 481 ASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESI 560
Cdd:cd18589   103 TEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETF 182
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 561 ENIRTVASLTREDMFQKKFNHELQMPYNIALKKAhligigfslsqavmfFAYAASFW 617
Cdd:cd18589   183 SAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEA---------------AAYAVSMW 224
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
694-811 1.75e-15

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: 80.33  E-value: 1.75e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPA---DGIVSLDGHNLKDLNLQWLRS 770
Cdd:COG1123     5 LEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGR 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2119559688 771 QIGIVSQEP--VLFDRTIAENIAYGDNSREVTMDEIIDAARKA 811
Cdd:COG1123    84 RIGMVFQDPmtQLNPVTVGDQIAEALENLGLSRAEARARVLEL 126
ABC_6TM_Tm288_like cd18547
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...
410-653 2.56e-15

Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD 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: 349991 [Multi-domain]  Cd Length: 298  Bit Score: 77.44  E-value: 2.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 410 KIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDHnnSVGALTTRLATDASQVQGAAG 489
Cdd:cd18547    43 GLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLRKDLFEKLQRLPLSYFDTH--SHGDIMSRVTNDVDNISQALS 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 490 IKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEAL-ESAGKIAiESIENIRTVAS 568
Cdd:cd18547   121 QSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALgELNGYIE-EMISGQKVVKA 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 569 LTREDMFQKKF---NHELqmpYNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLikqsevdyvdvfkafsaILFGGM 645
Cdd:cd18547   200 FNREEEAIEEFdeiNEEL---YKASFKAQFYSGLLMPIMNFINNLGYVLVAVVGGLL-----------------VINGAL 259

                  ....*...
gi 2119559688 646 AIGNASAF 653
Cdd:cd18547   260 TVGVIQAF 267
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
708-792 2.59e-15

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: 76.00  E-value: 2.59e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN---LQWLRSQIGIVSQEPVLFDR 784
Cdd:cd03261    12 GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRRRMGMLFQSGALFDS 91

                  ....*....
gi 2119559688 785 -TIAENIAY 792
Cdd:cd03261    92 lTVFENVAF 100
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
691-817 2.73e-15

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 76.95  E-value: 2.73e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 691 TANLSFANIIFRYPTRpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRS 770
Cdd:PRK13632    5 SVMIKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 771 QIGIVSQEPvlfDR-----TIAENIAYGDNSREVT---MDEII-DAARKANIHNFI 817
Cdd:PRK13632   84 KIGIIFQNP---DNqfigaTVEDDIAFGLENKKVPpkkMKDIIdDLAKKVGMEDYL 136
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
694-792 3.09e-15

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 75.47  E-value: 3.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPtrPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN---LQWLRS 770
Cdd:COG2884     2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLRR 79
                          90       100
                  ....*....|....*....|...
gi 2119559688 771 QIGIVSQE-PVLFDRTIAENIAY 792
Cdd:COG2884    80 RIGVVFQDfRLLPDRTVYENVAL 102
ABC_6TM_ABCB8_like cd18574
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ...
426-607 3.20e-15

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, 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. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.


Pssm-ID: 350018 [Multi-domain]  Cd Length: 295  Bit Score: 77.20  E-value: 3.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 426 LIAYFVQG-------YMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDHNNsvGALTTRLATDASQVQGAAGIKLGSSLMA 498
Cdd:cd18574    49 LGLYLLQSlltfayiSLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRT--GELVNRLTADVQEFKSSFKQCVSQGLRS 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 499 FCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKK 578
Cdd:cd18574   127 VTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELEL 206
                         170       180
                  ....*....|....*....|....*....
gi 2119559688 579 FNHELQmpynIALKKAHLIGIGFSLSQAV 607
Cdd:cd18574   207 YEEEVE----KAAKLNEKLGLGIGIFQGL 231
ABC_6TM_PCAT1_LagD_like cd18570
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...
387-623 4.07e-15

Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. 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. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.


Pssm-ID: 350014 [Multi-domain]  Cd Length: 294  Bit Score: 76.72  E-value: 4.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 387 AFAVIFSEILGVFAIL---------DE---GEQERKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKA 454
Cdd:cd18570     5 ILILLLSLLITLLGIAgsfffqiliDDiipSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 455 MLRQEIAFFDdhNNSVGALTTRLaTDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALE 534
Cdd:cd18570    85 LLKLPLSFFE--TRKTGEIISRF-NDANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIPLYILIILLF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 535 MQMMQgaaGKNKEALESAGK---IAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFA 611
Cdd:cd18570   162 NKPFK---KKNREVMESNAElnsYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKSFKLGKLSNLQSSIKGLISLIG 238
                         250
                  ....*....|..
gi 2119559688 612 YAASFWLGAYLI 623
Cdd:cd18570   239 SLLILWIGSYLV 250
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
707-822 1.62e-14

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 77.19  E-value: 1.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 707 PDTTILKG-LDLEVPQGQTVALVGSSGCGKSTTVQLTERFYdPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRT 785
Cdd:PRK11174  360 PDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGT 438
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2119559688 786 IAENIAYGDNsrEVTMDEIIDAARKANIHNFIASLPD 822
Cdd:PRK11174  439 LRDNVLLGNP--DASDEQLQQALENAWVSEFLPLLPQ 473
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
80-278 1.65e-14

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: 78.13  E-value: 1.65e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDI--NLKWWRENIGIVSQEPVLFG--TTIEENI 155
Cdd:TIGR01257  949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGG---KDIetNLDAVRQSLGMCPQHNILFHhlTVAEHIL 1025
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  156 RYGHLDVTKEDIEQAAKMANAHDfiMDLPQKYEtlvgERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGI 235
Cdd:TIGR01257 1026 FYAQLKGRSWEEAQLEMEAMLED--TGLHHKRN----EEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRS 1099
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 2119559688  236 VQDALEKASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGT 278
Cdd:TIGR01257 1100 IWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT 1143
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
694-779 1.66e-14

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: 73.69  E-value: 1.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRPDT-TILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN---LQWLR 769
Cdd:cd03257     2 LEVKNLSVSFPTGGGSvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIRR 81
                          90
                  ....*....|
gi 2119559688 770 SQIGIVSQEP 779
Cdd:cd03257    82 KEIQMVFQDP 91
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
693-822 1.85e-14

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 77.07  E-value: 1.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 693 NLSFAniifrYptRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQI 772
Cdd:PRK10790  345 NVSFA-----Y--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGV 417
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2119559688 773 GIVSQEPVLFDRTIAENIAYGdnsREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:PRK10790  418 AMVQQDPVVLADTFLANVTLG---RDISEEQVWQALETVQLAELARSLPD 464
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
698-792 1.91e-14

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: 72.05  E-value: 1.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 698 NIIFRYPtrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwLRSQIGIVSQ 777
Cdd:cd03230     5 NLSKRYG---KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIGYLPE 80
                          90
                  ....*....|....*.
gi 2119559688 778 EPVLFDR-TIAENIAY 792
Cdd:cd03230    81 EPSLYENlTVRENLKL 96
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
71-253 2.12e-14

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 72.60  E-value: 2.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  71 RPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDINLKWWRENIGIVSQ----EPVL 146
Cdd:PRK13539   12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG---GDIDDPDVAEACHYLGHrnamKPAL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 147 fgtTIEENIRY--GHLDVTKEDIEQAAKMANAHDfIMDLPQKYetlvgergaqLSGGQKQRIAIARALVRNPKILLLDEA 224
Cdd:PRK13539   89 ---TVAENLEFwaAFLGGEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEP 154
                         170       180       190
                  ....*....|....*....|....*....|
gi 2119559688 225 TSALDTESEGIVQDALekASH-GRTTIVIA 253
Cdd:PRK13539  155 TAALDAAAVALFAELI--RAHlAQGGIVIA 182
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
696-792 2.40e-14

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: 72.83  E-value: 2.40e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 696 FANIIFRYPtrPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN---LQWLRSQI 772
Cdd:cd03292     3 FINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRRKI 80
                          90       100
                  ....*....|....*....|.
gi 2119559688 773 GIVSQE-PVLFDRTIAENIAY 792
Cdd:cd03292    81 GVVFQDfRLLPDRNVYENVAF 101
ABC_6TM_exporter_like cd18564
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
415-623 3.23e-14

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes 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. 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 the chemical 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. However, 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: 350008 [Multi-domain]  Cd Length: 307  Bit Score: 74.47  E-value: 3.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 415 VLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDHnnSVGALTTRLATDASQVQGA---AGIK 491
Cdd:cd18564    57 AAALVGIALLRGLASYAGTYLTALVGQRVVLDLRRDLFAHLQRLSLSFHDRR--RTGDLLSRLTGDVGAIQDLlvsGVLP 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 492 LGSSLmafCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAgknKEALESAGKIAI---ESIENIRTVAS 568
Cdd:cd18564   135 LLTNL---LTLVGMLGVMFWLDWQLALIALAVAPLLLLAARRFSRRIKEAS---REQRRREGALASvaqESLSAIRVVQA 208
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 569 LTREDMFQKKFNHELQMPYNIALkKAHLIGIGFS-LSQAVMFFAYAASFWLGAYLI 623
Cdd:cd18564   209 FGREEHEERRFARENRKSLRAGL-RAARLQALLSpVVDVLVAVGTALVLWFGAWLV 263
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
12-223 4.45e-14

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 75.78  E-value: 4.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  12 LGNAMPHLQTLATARGAAYYLYQLiTMDPPIDSYSTeGKKLDNFQgNVQIRGVHFRYPSRPEAkiLYGVNLQIKRGQTVA 91
Cdd:PRK10522  279 LLSAVGALPTLLSAQVAFNKLNKL-ALAPYKAEFPR-PQAFPDWQ-TLELRNVTFAYQDNGFS--VGPINLTIKRGELLF 353
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  92 LVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENIGIVSQEPVLFGTTIE-ENIRYGHLDVTK--EDIE 168
Cdd:PRK10522  354 LIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLGpEGKPANPALVEKwlERLK 433
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 169 QAAKMANAHDFIMDLpqkyetlvgergaQLSGGQKQRIAIARALVRNPKILLLDE 223
Cdd:PRK10522  434 MAHKLELEDGRISNL-------------KLSKGQKKRLALLLALAEERDILLLDE 475
cbiO PRK13642
energy-coupling factor transporter ATPase;
694-811 5.07e-14

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 73.20  E-value: 5.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIG 773
Cdd:PRK13642    5 LEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2119559688 774 IVSQEP--VLFDRTIAENIAYGDNSREVTMDEIIDAARKA 811
Cdd:PRK13642   85 MVFQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEA 124
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
712-811 5.16e-14

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 72.89  E-value: 5.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYD-----PADGIVSLDGHNL--KDLNLQWLRSQIGIVSQEPVLFDR 784
Cdd:PRK14243   26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
                          90       100       110
                  ....*....|....*....|....*....|
gi 2119559688 785 TIAENIAYGD--NSREVTMDEIIDAA-RKA 811
Cdd:PRK14243  106 SIYDNIAYGAriNGYKGDMDELVERSlRQA 135
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
60-223 8.54e-14

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 74.83  E-value: 8.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHFRYPSRPEAK--ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINLKWWRENI 137
Cdd:COG4615   329 ELRGVTYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLF 408
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 GIVSQEPVLFGTTIeeniryghldvtkeDIEQAAKMANAHDFI--MDLPQKyetlVG-ERGA----QLSGGQKQRIAIAR 210
Cdd:COG4615   409 SAVFSDFHLFDRLL--------------GLDGEADPARARELLerLELDHK----VSvEDGRfsttDLSQGQRKRLALLV 470
                         170
                  ....*....|...
gi 2119559688 211 ALVRNPKILLLDE 223
Cdd:COG4615   471 ALLEDRPILVFDE 483
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
65-259 1.14e-13

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: 71.21  E-value: 1.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  65 HFRYPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlkdinLKWWRENIGIVSQEP 144
Cdd:cd03267    25 SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-------LVPWKRRKKFLRRIG 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 145 VLFGTTIE-----------------ENIRYGHLdvtKEDIEQAAKMANAHDfIMDLPQKyetlvgergaQLSGGQKQRIA 207
Cdd:cd03267    98 VVFGQKTQlwwdlpvidsfyllaaiYDLPPARF---KKRLDELSELLDLEE-LLDTPVR----------QLSLGQRMRAE 163
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 208 IARALVRNPKILLLDEATSALDTESEGIVQDAL--EKASHGRTTIVIAHRLSTI 259
Cdd:cd03267   164 IAAALLHEPEILFLDEPTIGLDVVAQENIRNFLkeYNRERGTTVLLTSHYMKDI 217
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
79-284 1.14e-13

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 74.36  E-value: 1.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  79 GVNLQIKRGQTVALVGSSGCGKS-TIVQLLQRFYDPE----EGQILIDGVNL---KDINLKWWREN-IGIVSQEPVLFGT 149
Cdd:PRK15134   27 DVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLlhaSEQTLRGVRGNkIAMIFQEPMVSLN 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 150 ---TIEENIrYG----HLDVTKE-------------DIEQAAKMANahdfimDLPQkyetlvgergaQLSGGQKQRIAIA 209
Cdd:PRK15134  107 plhTLEKQL-YEvlslHRGMRREaargeilncldrvGIRQAAKRLT------DYPH-----------QLSGGERQRVMIA 168
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 210 RALVRNPKILLLDEATSALDTESEGIVQDALE--KASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNELMS 284
Cdd:PRK15134  169 MALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQNRAATLFS 246
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
698-811 1.19e-13

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 72.08  E-value: 1.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 698 NIIFRYptRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQ 777
Cdd:PRK13647    9 DLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQ 86
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2119559688 778 EP--VLFDRTIAENIAYGDNSREVTMDEIIDAARKA 811
Cdd:PRK13647   87 DPddQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEA 122
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
59-284 1.43e-13

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: 74.07  E-value: 1.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPS--RPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQI-------LIDGVNLKDIN 129
Cdd:TIGR03269 280 IKVRNVSKRYISvdRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDG 359
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 130 LKWWRENIGIVSQEPVLFG-TTIEENIRYG-HLDVTKEdieqAAKMANAHDFIMD--LPQKYETLVGERGAQLSGGQKQR 205
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYPhRTVLDNLTEAiGLELPDE----LARMKAVITLKMVgfDEEKAEEILDKYPDELSEGERHR 435
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 206 IAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASH--GRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNEL 282
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVlDVCDRAALMRDGKIVKIGDPEEI 515

                  ..
gi 2119559688 283 MS 284
Cdd:TIGR03269 516 VE 517
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
75-229 1.49e-13

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 71.08  E-value: 1.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  75 KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDINL----KWWRENIGIVSQEPVLFGT- 149
Cdd:PRK10895   17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD---EDISLlplhARARRGIGYLPQEASIFRRl 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 150 TIEENIrYGHLDVtKEDIEQAAKMANAHDFIMDLpqKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 229
Cdd:PRK10895   94 SVYDNL-MAVLQI-RDDLSAEQREDRANELMEEF--HIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
59-254 1.71e-13

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 72.15  E-value: 1.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPsrpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDiNLKWWRENIG 138
Cdd:PRK13537    8 IDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVG 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQ----EPVLfgtTIEENI----RYGHLDVTkediEQAAKMANAHDFiMDLPQKYETLVGErgaqLSGGQKQRIAIAR 210
Cdd:PRK13537   84 VVPQfdnlDPDF---TVRENLlvfgRYFGLSAA----AARALVPPLLEF-AKLENKADAKVGE----LSGGMKRRLTLAR 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2119559688 211 ALVRNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAH 254
Cdd:PRK13537  152 ALVNDPDVLVLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTH 196
ABC_6TM_TAP2 cd18590
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ...
433-624 2.58e-13

Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); 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: 350034 [Multi-domain]  Cd Length: 289  Bit Score: 71.22  E-value: 2.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 433 GYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDhnNSVGALTTRLATDASQVqgAAGIKLGSSLMAFCSVVTGIVIGFVF 512
Cdd:cd18590    57 GGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEK--TKTGDLTSRLSTDTTLM--SRSVALNANVLLRSLVKTLGMLGFML 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 513 --SWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIA 590
Cdd:cd18590   133 slSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLK 212
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2119559688 591 LKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLIK 624
Cdd:cd18590   213 DRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQ 246
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
52-255 2.72e-13

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 69.99  E-value: 2.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  52 LDNFqgNVQIRGVHFRypsrpeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFY--DPEEGQILIDgvnlkdiN 129
Cdd:COG2401    31 LEAF--GVELRVVERY--------VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVP-------D 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 130 LKWWRENIGIvsqepvlfgttieENIryGHLDVTKEDIE--QAAKMANAHDFImdlpQKYetlvgergAQLSGGQKQRIA 207
Cdd:COG2401    94 NQFGREASLI-------------DAI--GRKGDFKDAVEllNAVGLSDAVLWL----RRF--------KELSTGQKFRFR 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2119559688 208 IARALVRNPKILLLDEATSALDTESEGIVQDALEKAS--HGRTTIVIAHR 255
Cdd:COG2401   147 LALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLArrAGITLVVATHH 196
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
698-811 3.35e-13

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 70.45  E-value: 3.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 698 NIIFRYPTRpdtTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYD-----PADGIVSLDGHNL--KDLNLQWLRS 770
Cdd:PRK14258   12 NLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNElesevRVEGRVEFFNQNIyeRRVNLNRLRR 88
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2119559688 771 QIGIVSQEPVLFDRTIAENIAYGDN----SREVTMDEIIDAARKA 811
Cdd:PRK14258   89 QVSMVHPKPNLFPMSVYDNVAYGVKivgwRPKLEIDDIVESALKD 133
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
694-822 3.42e-13

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 69.69  E-value: 3.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPT-RPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLT---ERfydPADGIVSLDGHNLKDLN---LQ 766
Cdd:COG1136     5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILgglDR---PTSGEVLIDGQDISSLSereLA 81
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 767 WLRSQ-IGIVSQEPVLFDR-TIAENIA----YGDNSREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:COG1136    82 RLRRRhIGFVFQFFNLLPElTALENVAlpllLAGVSRKERRERARELLERVGLGDRLDHRPS 143
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
84-332 3.46e-13

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: 70.13  E-value: 3.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  84 IKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNlkdinlkwwrenigiVSQEPVLFGTTIEENIRYGHLDVT 163
Cdd:cd03237    22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT---------------VSYKPQYIKADYEGTVRDLLSSIT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 164 KEdieqaakMANAHDFIMDL--PQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALE 241
Cdd:cd03237    87 KD-------FYTHPYFKTEIakPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 242 K--ASHGRTTIVIAHrlsTIKTADMIAgfkDGVVAEQGthnelmsKQGIYQQLVTLQSMKSADDNEIED----FNRD-DT 314
Cdd:cd03237   160 RfaENNEKTAFVVEH---DIIMIDYLA---DRLIVFEG-------EPSVNGVANPPQSLRSGMNRFLKNlditFRRDpET 226
                         250
                  ....*....|....*...
gi 2119559688 315 KRPSLRHQKSTIDMTPKK 332
Cdd:cd03237   227 GRPRINKLGSVKDREQKE 244
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
86-268 3.69e-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: 67.78  E-value: 3.69e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   86 RGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIdgvnlkdINLKWWRENIGIvsqepvlfgttieeniryghldvtke 165
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------IDGEDILEEVLD-------------------------- 47
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  166 dieqaakmanahdfimdlpQKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALE---- 241
Cdd:smart00382  48 -------------------QLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrll 108
                          170       180       190
                   ....*....|....*....|....*....|
gi 2119559688  242 ---KASHGRTTIVIAHRLSTIKTADMIAGF 268
Cdd:smart00382 109 lllKSEKNLTVILTTNDEKDLGPALLRRRF 138
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
70-254 4.45e-13

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 68.68  E-value: 4.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  70 SRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDI------NLKWWRENIGIvsqE 143
Cdd:PRK13538   10 ERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGI---K 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 144 PVLfgtTIEENIRY---GHLDVTKEDIEQAAKMANAHDFiMDLPqkyetlvgerGAQLSGGQKQRIAIARALVRNPKILL 220
Cdd:PRK13538   87 TEL---TALENLRFyqrLHGPGDDEALWEALAQVGLAGF-EDVP----------VRQLSAGQQRRVALARLWLTRAPLWI 152
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2119559688 221 LDEATSALDTESEGIVQDALEK-ASHGRTTIVIAH 254
Cdd:PRK13538  153 LDEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
692-793 5.04e-13

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 71.26  E-value: 5.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 692 ANLSFANIIFRYPtrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGhnlKDLNlqWLRSQ 771
Cdd:COG3839     2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG---RDVT--DLPPK 73
                          90       100
                  ....*....|....*....|....*.
gi 2119559688 772 ---IGIVSQEPVLFDR-TIAENIAYG 793
Cdd:COG3839    74 drnIAMVFQSYALYPHmTVYENIAFP 99
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
702-792 5.58e-13

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 70.88  E-value: 5.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 702 RYPTRP-DTTILKGLDLEVPQGQTVALVGSSGCGKST---TVQLTERfydPADGIVSLDGHNLKDLN---LQWLRSQIGI 774
Cdd:COG1135    10 TFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTALSereLRAARRKIGM 86
                          90
                  ....*....|....*....
gi 2119559688 775 VSQEPVLFD-RTIAENIAY 792
Cdd:COG1135    87 IFQHFNLLSsRTVAENVAL 105
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
77-278 5.96e-13

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 69.91  E-value: 5.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  77 LYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKdinlKWWREN-IGIVSQE-------PVLfg 148
Cdd:PRK15056   23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNlVAYVPQSeevdwsfPVL-- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 149 ttIEENI---RYGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEAT 225
Cdd:PRK15056   97 --VEDVVmmgRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPF 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 226 SALDTESEGIVQDAL-EKASHGRTTIVIAHRLSTIKTadmiagFKDGVVAEQGT 278
Cdd:PRK15056  171 TGVDVKTEARIISLLrELRDEGKTMLVSTHNLGSVTE------FCDYTVMVKGT 218
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
79-271 6.70e-13

Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 67.84  E-value: 6.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  79 GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDINLKWWRENI--GIV------SQEPVLFGTT 150
Cdd:cd03215    18 DVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDG---KPVTRRSPRDAIraGIAyvpedrKREGLVLDLS 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 151 IEENIryghldvtkedieqaakmanahdfimdlpqkyeTLvgerGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 230
Cdd:cd03215    95 VAENI---------------------------------AL----SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2119559688 231 ES-EGIVQDALEKASHGRTTIVIahrlST-----IKTADMIAGFKDG 271
Cdd:cd03215   138 GAkAEIYRLIRELADAGKAVLLI----SSeldelLGLCDRILVMYEG 180
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
694-793 1.51e-12

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 69.79  E-value: 1.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPtrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQL---TERfydPADGIVSLDGHNLkDLNLQWLRS 770
Cdd:COG1118     3 IEVRNISKRFG---SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDL-FTNLPPRER 75
                          90       100
                  ....*....|....*....|....
gi 2119559688 771 QIGIVSQEPVLF-DRTIAENIAYG 793
Cdd:COG1118    76 RVGFVFQHYALFpHMTVAENIAFG 99
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
714-779 1.74e-12

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 69.38  E-value: 1.74e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 714 GLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN---LQWLRSQIGIVSQEP 779
Cdd:COG4608    36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDP 104
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
71-229 2.32e-12

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 70.65  E-value: 2.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  71 RPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG----------VNLKDINLKWWRE----N 136
Cdd:PRK10261   26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRHvrgaD 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVL-------FGTTIEENIRYgHLDVTKED-IEQAAKMANAhdfiMDLPQKyETLVGERGAQLSGGQKQRIAI 208
Cdd:PRK10261  106 MAMIFQEPMTslnpvftVGEQIAESIRL-HQGASREEaMVEAKRMLDQ----VRIPEA-QTILSRYPHQLSGGMRQRVMI 179
                         170       180
                  ....*....|....*....|.
gi 2119559688 209 ARALVRNPKILLLDEATSALD 229
Cdd:PRK10261  180 AMALSCRPAVLIADEPTTALD 200
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
76-259 2.38e-12

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 70.91  E-value: 2.38e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   76 ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDP---EEGQILIDGVNLKdinlKWWRENIGIVSQEPVLFGT-TI 151
Cdd:TIGR00956  778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLD----SSFQRSIGYVQQQDLHLPTsTV 853
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  152 EENIRY-GHLDVTKEdIEQAAKMANAhDFIMDL--PQKY-ETLVGERGAQLSGGQKQRIAIARALVRNPKILL-LDEATS 226
Cdd:TIGR00956  854 RESLRFsAYLRQPKS-VSKSEKMEYV-EEVIKLleMESYaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTS 931
                          170       180       190
                   ....*....|....*....|....*....|....
gi 2119559688  227 ALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTI 259
Cdd:TIGR00956  932 GLDSQTAWSICKLMRKlADHGQAILCTIHQPSAI 965
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
698-777 3.39e-12

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: 65.53  E-value: 3.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 698 NIIFRYPTRpdtTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQ 777
Cdd:cd03214     4 NLSVGYGGR---TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
694-779 3.57e-12

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: 67.14  E-value: 3.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRP-DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQI 772
Cdd:COG1124     2 LEVRNLSVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81

                  ....*..
gi 2119559688 773 GIVSQEP 779
Cdd:COG1124    82 QMVFQDP 88
ABC_6TM_exporter_like cd18563
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
398-581 4.06e-12

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes 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. 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 the chemical 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. However, 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: 350007 [Multi-domain]  Cd Length: 296  Bit Score: 67.92  E-value: 4.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 398 VFAILDEGEQERKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDHnnSVGALTTRL 477
Cdd:cd18563    29 VLIQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRDLYEHLQRLSLSFFDKR--QTGSLMSRV 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 478 ATDASQVQ-----GAAGIkLGSSLMAfcsVVTGIVIgFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESA 552
Cdd:cd18563   107 TSDTDRLQdflsdGLPDF-LTNILMI---IGIGVVL-FSLNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRL 181
                         170       180
                  ....*....|....*....|....*....
gi 2119559688 553 GKIAIESIENIRTVASLTREDMFQKKFNH 581
Cdd:cd18563   182 NSVLNDTLPGIRVVKAFGQEKREIKRFDE 210
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
60-292 4.78e-12

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 66.87  E-value: 4.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHFRYPSRpeaKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDINL--------- 130
Cdd:PRK11701    8 SVRGLTKLYGPR---KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyalseaerr 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 131 KWWRENIGIVSQEP-------VLFGTTIEENI------RYGHLDVTK----EDIEQAAkmanahDFIMDLPQKYetlvge 193
Cdd:PRK11701   85 RLLRTEWGFVHQHPrdglrmqVSAGGNIGERLmavgarHYGDIRATAgdwlERVEIDA------ARIDDLPTTF------ 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 194 rgaqlSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTIK-TADMIAGFKD 270
Cdd:PRK11701  153 -----SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGlvRELGLAVVIVTHDLAVARlLAHRLLVMKQ 227
                         250       260
                  ....*....|....*....|...
gi 2119559688 271 GVVAEQG-THNELMSKQGIYQQL 292
Cdd:PRK11701  228 GRVVESGlTDQVLDDPQHPYTQL 250
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
75-229 4.88e-12

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 66.68  E-value: 4.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  75 KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILidgvnlKDINLKwwrenIGIVSQEPVLFGT---TI 151
Cdd:PRK09544   18 RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------RNGKLR-----IGYVPQKLYLDTTlplTV 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 152 EENIRYgHLDVTKEDIEQAAKMANAHDFIMDLPQKyetlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSALD 229
Cdd:PRK09544   87 NRFLRL-RPGTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
69-229 7.90e-12

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: 65.36  E-value: 7.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  69 PSRPEAKILYGVNLQIKRGQTVALVGSSGCGKST----IVQLLQRFYDPEeGQILIDGVNLKDINLKWWRENIgIVSQEP 144
Cdd:cd03233    15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSVE-GDIHYNGIPYKEFAEKYPGEII-YVSEED 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 145 VLFGT-TIEENIRYghldvtkedieqAAKMaNAHDFImdlpqkyetlvgeRGaqLSGGQKQRIAIARALVRNPKILLLDE 223
Cdd:cd03233    93 VHFPTlTVRETLDF------------ALRC-KGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCWDN 144

                  ....*.
gi 2119559688 224 ATSALD 229
Cdd:cd03233   145 STRGLD 150
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
696-793 1.00e-11

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: 65.82  E-value: 1.00e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 696 FANIIFRYPtrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwlRSQIGIV 775
Cdd:cd03296     5 VRNVSKRFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFV 79
                          90
                  ....*....|....*....
gi 2119559688 776 SQEPVLFDR-TIAENIAYG 793
Cdd:cd03296    80 FQHYALFRHmTVFDNVAFG 98
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
70-271 1.23e-11

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 67.83  E-value: 1.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  70 SRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDINLKWWRE----NIGIVSQE-P 144
Cdd:PRK10982    7 SFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQG---KEIDFKSSKEalenGISMVHQElN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 145 VLFGTTIEENIRYGHLDVTKEDIEQaAKMANAHDFIMDL------PQkyetlvgERGAQLSGGQKQRIAIARALVRNPKI 218
Cdd:PRK10982   84 LVLQRSVMDNMWLGRYPTKGMFVDQ-DKMYRDTKAIFDEldididPR-------AKVATLSVSQMQMIEIAKAFSYNAKI 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 219 LLLDEATSALdTESE-----GIVQDALEKashGRTTIVIAHRLSTI-KTADMIAGFKDG 271
Cdd:PRK10982  156 VIMDEPTSSL-TEKEvnhlfTIIRKLKER---GCGIVYISHKMEEIfQLCDEITILRDG 210
ABC_6TM_YwjA_like cd18549
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...
415-637 1.61e-11

Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis 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: 349993 [Multi-domain]  Cd Length: 295  Bit Score: 65.93  E-value: 1.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 415 VLMFVGVGVISLIAYFVQ--GYMFGRSGEYltlRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRLATDASQVQGAAGIKL 492
Cdd:cd18549    46 AILLALYILRTLLNYFVTywGHVMGARIET---DMRRDLFEHLQKLSFSFFD--NNKTGQLMSRITNDLFDISELAHHGP 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 493 GSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEalesagKIA-----IE-SIENIRTV 566
Cdd:cd18549   121 EDLFISIITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVRE------KIGeinaqLEdSLSGIRVV 194
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 567 ASLTREDMFQKKFNHElqmpyNIALKKA-----HLIGIGFSLSQAVMFFAYAASFWLGAYLIKQSEVDYVDVFkAF 637
Cdd:cd18549   195 KAFANEEYEIEKFDEG-----NDRFLESkkkayKAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLV-AF 264
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
698-804 1.61e-11

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 65.87  E-value: 1.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 698 NIIFRYPTrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN--LQWLRSQIGIV 775
Cdd:PRK13639    6 DLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKksLLEVRKTVGIV 83
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2119559688 776 SQEP--VLFDRTIAENIAYGDNSREVTMDEI 804
Cdd:PRK13639   84 FQNPddQLFAPTVEEDVAFGPLNLGLSKEEV 114
PLN03211 PLN03211
ABC transporter G-25; Provisional
73-258 1.69e-11

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 67.98  E-value: 1.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  73 EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQ-RFYDPE-EGQILIDGVNLKDINLKwwreNIGIVSQEPVLF-GT 149
Cdd:PLN03211   80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQGNNfTGTILANNRKPTKQILK----RTGFVTQDDILYpHL 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 150 TIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLP-QKYE-TLVGE---RGaqLSGGQKQRIAIARALVRNPKILLLDEA 224
Cdd:PLN03211  156 TVRETLVFCSLLRLPKSLTKQEKILVAESVISELGlTKCEnTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEP 233
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2119559688 225 TSALD-TESEGIVQDALEKASHGRTTIVIAHRLST 258
Cdd:PLN03211  234 TSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSS 268
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
705-822 2.14e-11

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 64.04  E-value: 2.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 705 TRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDP---ADGIVSLDGHNLKDLNLQwlRSQIGIVSQEPVL 781
Cdd:COG4136    10 TLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRRIGILFQDDLL 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2119559688 782 FDR-TIAENIAYG---DNSREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:COG4136    88 FPHlSVGENLAFAlppTIGRAQRRARVEQALEEAGLAGFADRDPA 132
ABC_6TM_exporter_like cd18565
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
357-623 2.32e-11

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes 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. 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 the chemical 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. However, 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: 350009 [Multi-domain]  Cd Length: 313  Bit Score: 65.67  E-value: 2.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 357 LGRILKLnkseAPFIVMG-CFASLVNGgaMPAFAVIFSEILGvfaILDEGEQerkIIQYVLMFVGVGVISLIAYFVQGYM 435
Cdd:cd18565    10 LNRLFDL----APPLLIGvAIDAVFNG--EASFLPLVPASLG---PADPRGQ---LWLLGGLTVAAFLLESLFQYLSGVL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 436 FGRSGEYLTLRLRSMSFKAMLRQEIAFFDDHnnSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWK 515
Cdd:cd18565    78 WRRFAQRVQHDLRTDTYDHVQRLDMAFFEDR--QTGDLMSVLNNDVNQLERFLDDGANSIIRVVVTVLGIGAILFYLNWQ 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 516 ITLLVIAFLPFVMIGGALEMQMMQgaaGKNKEALESAGKIA--IE-SIENIRTVASLTREDmFQKKFNHELQMPYNIALK 592
Cdd:cd18565   156 LALVALLPVPLIIAGTYWFQRRIE---PRYRAVREAVGDLNarLEnNLSGIAVIKAFTAED-FERERVADASEEYRDANW 231
                         250       260       270
                  ....*....|....*....|....*....|..
gi 2119559688 593 KAHLIGIGFS-LSQAVMFFAYAASFWLGAYLI 623
Cdd:cd18565   232 RAIRLRAAFFpVIRLVAGAGFVATFVVGGYWV 263
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
702-779 2.60e-11

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: 65.46  E-value: 2.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 702 RYPTRPDT-TILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDP---ADGIVSLDGHNLKDLN---LQWLR-SQIG 773
Cdd:COG0444    10 YFPTRRGVvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSekeLRKIRgREIQ 89

                  ....*.
gi 2119559688 774 IVSQEP 779
Cdd:COG0444    90 MIFQDP 95
cbiO PRK13637
energy-coupling factor transporter ATPase;
693-811 2.61e-11

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 65.07  E-value: 2.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 693 NLSFaniIFRYPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNL--KDLNLQWLRS 770
Cdd:PRK13637    7 NLTH---IYMEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDIRK 83
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2119559688 771 QIGIVSQEP--VLFDRTIAENIAYGDNSREVTMDEIIDAARKA 811
Cdd:PRK13637   84 KVGLVFQYPeyQLFEETIEKDIAFGPINLGLSEEEIENRVKRA 126
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
708-804 2.82e-11

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: 64.18  E-value: 2.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLkdLNLQWLRSQIGIVSQEPVLFDR-TI 786
Cdd:cd03300    12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI--TNLPPHKRPVNTVFQNYALFPHlTV 89
                          90
                  ....*....|....*...
gi 2119559688 787 AENIAYGDNSREVTMDEI 804
Cdd:cd03300    90 FENIAFGLRLKKLPKAEI 107
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
694-791 3.04e-11

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: 63.66  E-value: 3.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRPDTT-ILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWL---- 768
Cdd:cd03255     1 IELKNLSKTYGGGGEKVqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
                          90       100
                  ....*....|....*....|....
gi 2119559688 769 RSQIGIVSQEP-VLFDRTIAENIA 791
Cdd:cd03255    81 RRHIGFVFQSFnLLPDLTALENVE 104
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
708-811 3.07e-11

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 65.90  E-value: 3.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwlRSQIGIVSQEPVLFDR-TI 786
Cdd:PRK11432   18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFPHmSL 95
                          90       100
                  ....*....|....*....|....*
gi 2119559688 787 AENIAYGDNSREVTMDEIIDAARKA 811
Cdd:PRK11432   96 GENVGYGLKMLGVPKEERKQRVKEA 120
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
75-285 3.44e-11

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 65.31  E-value: 3.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  75 KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPeEGQILIDGVNLKDINL---------KWWRENIGIVSQEP- 144
Cdd:COG4170    21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKD-NWHVTADRFRWNGIDLlklsprerrKIIGREIAMIFQEPs 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 145 ------VLFGTTIEENI---RY-GHL-DVTKEDIEQAAKMANA-----HDFIMD-LPQkyetlvgergaQLSGGQKQRIA 207
Cdd:COG4170   100 scldpsAKIGDQLIEAIpswTFkGKWwQRFKWRKKRAIELLHRvgikdHKDIMNsYPH-----------ELTEGECQKVM 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 208 IARALVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNELMS 284
Cdd:COG4170   169 IAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARlnQLQGTSILLISHDLESIsQWADTITVLYCGQTVESGPTEQILK 248

                  .
gi 2119559688 285 K 285
Cdd:COG4170   249 S 249
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
79-278 3.52e-11

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 64.24  E-value: 3.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  79 GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLK-----DINLKwwreniGIVS--QEPVLFGT-T 150
Cdd:PRK11300   23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglpghQIARM------GVVRtfQHVRLFREmT 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 151 IEENI---RYGHLDVT---------------KEDIEQAAKMANAhdfiMDLpqkyeTLVGERGA-QLSGGQKQRIAIARA 211
Cdd:PRK11300   97 VIENLlvaQHQQLKTGlfsgllktpafrraeSEALDRAATWLER----VGL-----LEHANRQAgNLAYGQQRRLEIARC 167
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 212 LVRNPKILLLDEATSALD-TESEGIVQ--DALEKaSHGRTTIVIAHRLStiktadMIAGFKDGV-VAEQGT 278
Cdd:PRK11300  168 MVTQPEILMLDEPAAGLNpKETKELDEliAELRN-EHNVTVLLIEHDMK------LVMGISDRIyVVNQGT 231
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
59-282 3.60e-11

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 64.34  E-value: 3.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFrYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDP----EEGQILIDGVNLKDINLKwwR 134
Cdd:PRK10418    5 IELRNIAL-QAAQP---LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPCALR--G 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 135 ENIGIVSQEP-------------------VLFGTTIEENIRYGHLDVTKEDIEQAAKManaHDFimdlpqkyetlvgerg 195
Cdd:PRK10418   79 RKIATIMQNPrsafnplhtmhtharetclALGKPADDATLTAALEAVGLENAARVLKL---YPF---------------- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 196 aQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTI-KTADMIAGFKDGV 272
Cdd:PRK10418  140 -EMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVaRLADDVAVMSHGR 218
                         250
                  ....*....|
gi 2119559688 273 VAEQGTHNEL 282
Cdd:PRK10418  219 IVEQGDVETL 228
ABC_6TM_Rv0194_D1_like cd18543
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ...
409-641 4.14e-11

Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD 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 and a various type of lipids. 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. However, 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: 349987 [Multi-domain]  Cd Length: 291  Bit Score: 64.81  E-value: 4.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 409 RKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDHnnSVGALTTRLATDASQVQGAa 488
Cdd:cd18543    36 SALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAHLQRLDGAFHDRW--QSGQLLSRATSDLSLVQRF- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 489 gikLGSSLMAFCSVVT---GIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAgknKEALESAGKIAI---ESIEN 562
Cdd:cd18543   113 ---LAFGPFLLGNLLTlvvGLVVMLVLSPPLALVALASLPPLVLVARRFRRRYFPAS---RRAQDQAGDLATvveESVTG 186
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 563 IRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLIKQSEVDyVDVFKAFSAIL 641
Cdd:cd18543   187 IRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVLALGGWLVANGSLT-LGTLVAFSAYL 264
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
37-260 5.50e-11

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: 66.31  E-value: 5.50e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  37 TMDPPIDSYSTEGKKLDNFQGNVQIR----GVHFRYPS--RPEAKILYG-VNLQIKRGQTVALVGSSGCGKSTIVQLLQ- 108
Cdd:TIGR00954 421 PRVEEIESGREGGRNSNLVPGRGIVEyqdnGIKFENIPlvTPNGDVLIEsLSFEVPSGNNLLICGPNGCGKSSLFRILGe 500
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 109 -------RFYDPEEGQILIdgvnlkdinlkwwrenigiVSQEP----------VLFGTTIEENIRYGHLDvtkEDIEQaa 171
Cdd:TIGR00954 501 lwpvyggRLTKPAKGKLFY-------------------VPQRPymtlgtlrdqIIYPDSSEDMKRRGLSD---KDLEQ-- 556
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 172 kmanahdfIMDLPQKYETLVGERGAQ--------LSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKA 243
Cdd:TIGR00954 557 --------ILDNVQLTHILEREGGWSavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF 628
                         250
                  ....*....|....*..
gi 2119559688 244 shGRTTIVIAHRLSTIK 260
Cdd:TIGR00954 629 --GITLFSVSHRKSLWK 643
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
64-263 7.15e-11

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 62.27  E-value: 7.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  64 VHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDiNLKWWRENIGIVSQE 143
Cdd:PRK13540    7 LDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHR 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 144 ----PVLfgtTIEENIRYG-HLDVTKEDIEQAAKMANAHDFImDLPqkyetlvgerGAQLSGGQKQRIAIARALVRNPKI 218
Cdd:PRK13540   83 sginPYL---TLRENCLYDiHFSPGAVGITELCRLFSLEHLI-DYP----------CGLLSSGQKRQVALLRLWMSKAKL 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2119559688 219 LLLDEATSALDTES-EGIVQDALEKASHGRTTIVIAHRLSTIKTAD 263
Cdd:PRK13540  149 WLLDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
700-779 7.61e-11

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: 65.48  E-value: 7.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 700 IFRyPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTT----VQLTerfydPADGIVSLDGHNLKDLN---LQWLRSQI 772
Cdd:COG4172   291 LFR-RTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDLDGLSrraLRPLRRRM 364

                  ....*..
gi 2119559688 773 GIVSQEP 779
Cdd:COG4172   365 QVVFQDP 371
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
694-778 7.87e-11

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: 63.18  E-value: 7.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRyptRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGI-VSLDGHNLKDLNLQWLRSQI 772
Cdd:COG1119     4 LELRNVTVR---RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGERRGGEDVWELRKRI 80

                  ....*.
gi 2119559688 773 GIVSQE 778
Cdd:COG1119    81 GLVSPA 86
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
58-321 9.13e-11

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 65.04  E-value: 9.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  58 NVQIRGVHFRYPsrpEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILID---GVNL------KDI 128
Cdd:PRK10938    3 SLQISQGTFRLS---DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQfshITRLsfeqlqKLV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 129 NLKWWRENIGIVSQEPVLFGTTIEENIRYGHLDvtKEDIEQAAKMANahdfIMDLpqkyetlVGERGAQLSGGQKQRIAI 208
Cdd:PRK10938   80 SDEWQRNNTDMLSPGEDDTGRTTAEIIQDEVKD--PARCEQLAQQFG----ITAL-------LDRRFKYLSTGETRKTLL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 209 ARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIV-IAHRLSTIKT-ADMIAGFKDGVVAEQGTHNELMSkQ 286
Cdd:PRK10938  147 CQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVlVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQ-Q 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2119559688 287 GIYQQLV---TLQSMK--SADDNEIEDFNRDDTKRPSLRH 321
Cdd:PRK10938  226 ALVAQLAhseQLEGVQlpEPDEPSARHALPANEPRIVLNN 265
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
698-804 9.33e-11

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: 62.27  E-value: 9.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 698 NIIFRYPtrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwlRSQIGIVSQ 777
Cdd:cd03301     5 NVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIAMVFQ 79
                          90       100
                  ....*....|....*....|....*...
gi 2119559688 778 EPVLFDR-TIAENIAYGDNSREVTMDEI 804
Cdd:cd03301    80 NYALYPHmTVYDNIAFGLKLRKVPKDEI 107
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
79-225 1.08e-10

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 65.04  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  79 GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG--VNLKDINlKWWRENIGIVS----QEPVLFGTTIE 152
Cdd:COG1129   270 DVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPR-DAIRAGIAYVPedrkGEGLVLDLSIR 348
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 153 ENI---------RYGHLDVTKEDieqaakmANAHDFIMDL---PQKYETLVGergaQLSGGQKQRIAIARALVRNPKILL 220
Cdd:COG1129   349 ENItlasldrlsRGGLLDRRRER-------ALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLI 417

                  ....*
gi 2119559688 221 LDEAT 225
Cdd:COG1129   418 LDEPT 422
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
711-821 1.12e-10

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: 63.00  E-value: 1.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 711 ILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIAENI 790
Cdd:cd03288    36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSGSIRFNL 115
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2119559688 791 aygDNSREVTMDEIIDAARKANIHNFIASLP 821
Cdd:cd03288   116 ---DPECKCTDDRLWEALEIAQLKNMVKSLP 143
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
694-816 1.28e-10

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 63.11  E-value: 1.28e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRPDTTiLKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIG 773
Cdd:PRK13635    6 IRVEHISFRYPDAATYA-LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVG 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 774 IVSQEPvlfDR-----TIAENIAYGDNSREVTMDEII----DAARKANIHNF 816
Cdd:PRK13635   85 MVFQNP---DNqfvgaTVQDDVAFGLENIGVPREEMVervdQALRQVGMEDF 133
ABC_6TM_YknV_like cd18545
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...
411-639 1.79e-10

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD 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 and a various type of lipids. 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. However, 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: 349989 [Multi-domain]  Cd Length: 293  Bit Score: 62.87  E-value: 1.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 411 IIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRLATDASQVQGAAGI 490
Cdd:cd18545    39 LLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSHLQKLSFSFFD--SRPVGKILSRVINDVNSLSDLLSN 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 491 KLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFLPfVMIGGALEMQMMQGAAGKNKEAlesagKIAI------ESIENIR 564
Cdd:cd18545   117 GLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLP-LLVLVVFLLRRRARKAWQRVRK-----KISNlnaylhESISGIR 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 565 TVASLTREDMFQKKFNhELqmpyNIALKKAHL--IGIGFSLSQAVMF---FAYAASFWLGAYLIKQSEVDyVDVFKAFSA 639
Cdd:cd18545   191 VIQSFAREDENEEIFD-EL----NRENRKANMraVRLNALFWPLVELisaLGTALVYWYGGKLVLGGAIT-VGVLVAFIG 264
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
708-793 3.15e-10

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: 60.62  E-value: 3.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNL--KDLNLQWLRSQIGIVSQEPVLF-DR 784
Cdd:cd03262    12 DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQKVGMVFQQFNLFpHL 91

                  ....*....
gi 2119559688 785 TIAENIAYG 793
Cdd:cd03262    92 TVLENITLA 100
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
698-794 3.62e-10

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: 60.35  E-value: 3.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 698 NIIFRYptRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGhnlKDLNLQWLRSQIGIVSQ 777
Cdd:cd03226     4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKERRKSIGYVMQ 78
                          90
                  ....*....|....*....
gi 2119559688 778 EP--VLFDRTIAENIAYGD 794
Cdd:cd03226    79 DVdyQLFTDSVREELLLGL 97
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
77-284 3.92e-10

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 61.10  E-value: 3.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  77 LYGVNLQIKRGQTVALVGSSGCGKSTivqLLQRFYD--PEEGQILIDGVNLKDINL-KWWRENIGIVSQEPVLFGTTIee 153
Cdd:PRK03695   12 LGPLSAEVRAGEILHLVGPNGAGKST---LLARMAGllPGSGSIQFAGQPLEAWSAaELARHRAYLSQQQTPPFAMPV-- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 154 nirYGHLDVTKEDIEQAAKMANAHDFIMDLPQ---KYETLVGergaQLSGGQKQRIAIARALVR-----NP--KILLLDE 223
Cdd:PRK03695   87 ---FQYLTLHQPDKTRTEAVASALNEVAEALGlddKLGRSVN----QLSGGEWQRVRLAAVVLQvwpdiNPagQLLLLDE 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 224 ATSALDTESEGIVqDAL--EKASHGRTTIVIAHRLS-TIKTADMIAGFKDGVVAEQGTHNELMS 284
Cdd:PRK03695  160 PMNSLDVAQQAAL-DRLlsELCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLT 222
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
708-793 4.35e-10

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 61.18  E-value: 4.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVL-FDRTI 786
Cdd:PRK11231   14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITV 93

                  ....*..
gi 2119559688 787 AENIAYG 793
Cdd:PRK11231   94 RELVAYG 100
hmuV PRK13547
heme ABC transporter ATP-binding protein;
70-290 4.58e-10

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 61.38  E-value: 4.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  70 SRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQ-RFYDPEE-------GQILIDGVNLKDIN---LKWWRENIG 138
Cdd:PRK13547   10 ARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGAprgarvtGDVTLNGEPLAAIDaprLARLRAVLP 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 139 IVSQ--------EPVLFGttieeniRYGHLDV-------TKEDIEQAAKMANAhdfimdlpqkyETLVGERGAQLSGGQK 203
Cdd:PRK13547   90 QAAQpafafsarEIVLLG-------RYPHARRagalthrDGEIAWQALALAGA-----------TALVGRDVTTLSGGEL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 204 QRIAIARAL---------VRNPKILLLDEATSALDTESEGIVQDALEKASH----GRTTIVIAHRLSTiKTADMIAGFKD 270
Cdd:PRK13547  152 ARVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwnlGVLAIVHDPNLAA-RHADRIAMLAD 230
                         250       260
                  ....*....|....*....|
gi 2119559688 271 GVVAEQGTHNELMSKQGIYQ 290
Cdd:PRK13547  231 GAIVAHGAPADVLTPAHIAR 250
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
708-804 5.47e-10

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 61.89  E-value: 5.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwlRSQIGIVSQEPVLFDR-TI 786
Cdd:PRK09452   26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFPHmTV 103
                          90
                  ....*....|....*...
gi 2119559688 787 AENIAYGDNSREVTMDEI 804
Cdd:PRK09452  104 FENVAFGLRMQKTPAAEI 121
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
80-229 5.87e-10

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 63.22  E-value: 5.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG--VNLKDINLkwwRENIGIVSQEPVLFGT-TIEENIR 156
Cdd:NF033858  285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDAGDIAT---RRRVGYMSQAFSLYGElTVRQNLE 361
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 157 -YGHL-DVTKEDIEQA-AKMAnaHDFimDLpqkyETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 229
Cdd:NF033858  362 lHARLfHLPAAEIAARvAEML--ERF--DL----ADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
712-813 9.15e-10

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: 59.66  E-value: 9.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwlRSQIGIVSQEPVLF-DRTIAENI 790
Cdd:cd03299    15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
                          90       100
                  ....*....|....*....|....*..
gi 2119559688 791 AYG----DNSREVTMDEIIDAARKANI 813
Cdd:cd03299    93 AYGlkkrKVDKKEIERKVLEIAEMLGI 119
ABC_6TM_Rv0194_D2_like cd18546
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ...
415-623 1.00e-09

Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD 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 and a various type of lipids. 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. However, 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: 349990 [Multi-domain]  Cd Length: 292  Bit Score: 60.58  E-value: 1.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 415 VLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRLATDASQVQGAAGIKLGS 494
Cdd:cd18546    42 AAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAHLQRLSLDFHE--RETSGRIMTRMTSDIDALSELLQTGLVQ 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 495 SLMAFCSVVTGIVIGFVFSWKITLLVIAFLPfVMIGGALEMQMMQGAAgkNKEALESAGKIA---IESIENIRTVASLTR 571
Cdd:cd18546   120 LVVSLLTLVGIAVVLLVLDPRLALVALAALP-PLALATRWFRRRSSRA--YRRARERIAAVNadlQETLAGIRVVQAFRR 196
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 572 EDMFQKKFNHElqmpyNIALKKAH-----LIGIGFSLSQAVMFFAYAASFWLGAYLI 623
Cdd:cd18546   197 ERRNAERFAEL-----SDDYRDARlraqrLVAIYFPGVELLGNLATAAVLLVGAWRV 248
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
83-266 1.01e-09

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 62.11  E-value: 1.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  83 QIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQIlidgvnlkDINLKwwrenigiVSQEP----VLFGTTIEENIRyg 158
Cdd:COG1245   362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--------DEDLK--------ISYKPqyisPDYDGTVEEFLR-- 423
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 159 hlDVTKEDIEqaAKMANaHDFI--MDLPQKYETLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIV 236
Cdd:COG1245   424 --SANTDDFG--SSYYK-TEIIkpLGLEKLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAV 494
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2119559688 237 QDALEK--ASHGRTTIVIAHRLSTIktaDMIA 266
Cdd:COG1245   495 AKAIRRfaENRGKTAMVVDHDIYLI---DYIS 523
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
58-284 1.11e-09

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 60.91  E-value: 1.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  58 NVQIRGVHF---RYPSRPEAKILYGVNlqikRGQTVALVGSSGCGKS----TIVQLLQRFYDPEEGQILIDGVNLKDINL 130
Cdd:PRK11022    5 NVDKLSVHFgdeSAPFRAVDRISYSVK----QGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 131 KWWRENIG----IVSQEPVlfgTTIEENIRYGHLDVTKEDIEQAAKMANAHDFIMDLPqkyeTLVG-----ER----GAQ 197
Cdd:PRK11022   81 KERRNLVGaevaMIFQDPM---TSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLL----NQVGipdpaSRldvyPHQ 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 198 LSGGQKQRIAIARALVRNPKILLLDEATSALD-TESEGIVQDALE-KASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVA 274
Cdd:PRK11022  154 LSGGMSQRVMIAMAIACRPKLLIADEPTTALDvTIQAQIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAGQVV 233
                         250
                  ....*....|
gi 2119559688 275 EQGTHNELMS 284
Cdd:PRK11022  234 ETGKAHDIFR 243
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
48-288 1.16e-09

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 61.83  E-value: 1.16e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  48 EGKKLdnFQGNVQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQIlidgvnlkd 127
Cdd:PRK15064  311 QDKKL--HRNALEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV--------- 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 128 inlKWwREN--IGIVSQEPVL-FGTTI---------------EENIR--YGHLDVTKEDIEQAAKManahdfimdlpqky 187
Cdd:PRK15064  377 ---KW-SENanIGYYAQDHAYdFENDLtlfdwmsqwrqegddEQAVRgtLGRLLFSQDDIKKSVKV-------------- 438
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 188 etlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEK-------ASHGRTTI-VIAHRLSTI 259
Cdd:PRK15064  439 ----------LSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKyegtlifVSHDREFVsSLATRIIEI 508
                         250       260
                  ....*....|....*....|....*....
gi 2119559688 260 KTadmiagfkDGVVAEQGTHNELMSKQGI 288
Cdd:PRK15064  509 TP--------DGVVDFSGTYEEYLRSQGI 529
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
60-232 1.29e-09

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 61.49  E-value: 1.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHFRYPsrPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQrfydpeegqilidGVNlKDINLKWWRE---N 136
Cdd:TIGR03719   6 TMNRVSKVVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVD-KDFNGEARPQpgiK 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLFGT-TIEENIRYG---HLDVTKEDIEQAAKMA-----------------------NAHDF------IMD- 182
Cdd:TIGR03719  70 VGYLPQEPQLDPTkTVRENVEEGvaeIKDALDRFNEISAKYAepdadfdklaaeqaelqeiidaaDAWDLdsqleiAMDa 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 183 --LPQKyETLVgergAQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 232
Cdd:TIGR03719 150 lrCPPW-DADV----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
83-266 1.38e-09

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 61.36  E-value: 1.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  83 QIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQIlidgvnlkDINLKwwrenigiVSQEPvlfgTTIEENIryghlDV 162
Cdd:PRK13409  361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV--------DPELK--------ISYKP----QYIKPDY-----DG 415
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 163 TKED-IEQAAKMANA----HDFI--MDLPQKYETLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGI 235
Cdd:PRK13409  416 TVEDlLRSITDDLGSsyykSEIIkpLQLERLLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 491
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2119559688 236 VQDALEK--ASHGRTTIVIAHRLSTIktaDMIA 266
Cdd:PRK13409  492 VAKAIRRiaEEREATALVVDHDIYMI---DYIS 521
cbiO PRK13650
energy-coupling factor transporter ATPase;
698-811 1.59e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 59.75  E-value: 1.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 698 NIIFRYPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQ 777
Cdd:PRK13650    9 NLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQ 88
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 2119559688 778 EP--VLFDRTIAENIAYGDNSREVTMDEIIDAARKA 811
Cdd:PRK13650   89 NPdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEA 124
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
709-779 2.60e-09

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: 60.47  E-value: 2.60e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688 709 TTILKGLDLEVPQGQTVALVGSSGCGKSTT----VQLTERFYDPADGIVSLDGHNLKDLNLQWLR----SQIGIVSQEP 779
Cdd:COG4172    23 VEAVKGVSFDIAAGETLALVGESGSGKSVTalsiLRLLPDPAAHPSGSILFDGQDLLGLSERELRrirgNRIAMIFQEP 101
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
715-807 4.83e-09

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: 57.30  E-value: 4.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 715 LDLEVPqGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKD----LNLQWLRSQIGIVSQEPVLFDR-TIAEN 789
Cdd:cd03297    17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFPHlNVREN 95
                          90       100
                  ....*....|....*....|...
gi 2119559688 790 IAYG-----DNSREVTMDEIIDA 807
Cdd:cd03297    96 LAFGlkrkrNREDRISVDELLDL 118
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
712-808 5.69e-09

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 57.86  E-value: 5.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYD-----PADGIVSLDGHNLKDLNLQW--LRSQIGIVSQEPVLFDR 784
Cdd:PRK14239   21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNIYSPRTDTvdLRKEIGMVFQQPNPFPM 100
                          90       100
                  ....*....|....*....|....
gi 2119559688 785 TIAENIAYGDNSREVTMDEIIDAA 808
Cdd:PRK14239  101 SIYENVVYGLRLKGIKDKQVLDEA 124
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
708-806 6.31e-09

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: 57.06  E-value: 6.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNL-QWLRSQIGIVSQEPVLFDR-T 785
Cdd:cd03224    12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPhERARAGIGYVPEGRRIFPElT 91
                          90       100
                  ....*....|....*....|....*.
gi 2119559688 786 IAENI-----AYGDNSREVTMDEIID 806
Cdd:cd03224    92 VEENLllgayARRRAKRKARLERVYE 117
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
78-268 7.87e-09

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: 57.38  E-value: 7.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  78 YGVN------LQIKR-GQTVALVGSSGCGKSTIVQLLQ--------RFYDPEEGQILID---GVNLKDINLKWWRENIGI 139
Cdd:cd03236    10 YGPNsfklhrLPVPReGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 140 ------VSQEPVLFGTTIEENIRYGHLDVTKEDIEQAakmanahdfiMDLpqkyETLVGERGAQLSGGQKQRIAIARALV 213
Cdd:cd03236    90 ivkpqyVDLIPKAVKGKVGELLKKKDERGKLDELVDQ----------LEL----RHVLDRNIDQLSGGELQRVAIAAALA 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2119559688 214 RNPKILLLDEATSALDTESEGIVQDAL-EKASHGRTTIVIAHRLSTIktaDMIAGF 268
Cdd:cd03236   156 RDADFYFFDEPSSYLDIKQRLNAARLIrELAEDDNYVLVVEHDLAVL---DYLSDY 208
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
694-764 8.54e-09

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 57.39  E-value: 8.54e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 694 LSFANIIFRYPT------RPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN 764
Cdd:PRK10419    4 LNVSGLSHHYAHgglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
ABC_6TM_exporter_like cd18778
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
405-645 1.10e-08

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes 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. 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 the chemical 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. However, 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: 350051 [Multi-domain]  Cd Length: 293  Bit Score: 57.16  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 405 GEQERKIIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDDHnnSVGALTTRLATDASQV 484
Cdd:cd18778    33 SKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYDKLQRLSLRYFDDR--QTGDLMSRVINDVANV 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 485 QG--AAGIKLGSSlmafcSVVTGIVIG---FVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIES 559
Cdd:cd18778   111 ERliADGIPQGIT-----NVLTLVGVAiilFSINPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDN 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 560 IENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLsqaVMFFA---YAASFWLGAYLIKQSEVDYVDVFkA 636
Cdd:cd18778   186 LSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPL---MEFLTslgTVLVLGFGGRLVLAGELTIGDLV-A 261

                  ....*....
gi 2119559688 637 FsaILFGGM 645
Cdd:cd18778   262 F--LLYLGL 268
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
694-793 1.46e-08

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 55.55  E-value: 1.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRPDTT--ILKGLDLEVPQGQTVALVGSSGCGKSTTVQ--LTErfYDPADGIVSLDGHnlkdlnlqwlr 769
Cdd:cd03250     1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSalLGE--LEKLSGSVSVPGS----------- 67
                          90       100
                  ....*....|....*....|....
gi 2119559688 770 sqIGIVSQEPVLFDRTIAENIAYG 793
Cdd:cd03250    68 --IAYVSQEPWIQNGTIRENILFG 89
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
708-793 1.53e-08

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 56.39  E-value: 1.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYD-----PADGIVSLDGHNL--KDLNLQWLRSQIGIVSQEPV 780
Cdd:PRK14267   16 SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPN 95
                          90
                  ....*....|....
gi 2119559688 781 LFDR-TIAENIAYG 793
Cdd:PRK14267   96 PFPHlTIYDNVAIG 109
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
696-791 1.57e-08

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 57.12  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 696 FANIIFRYPT-RPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN---LQWLRSQ 771
Cdd:PRK11153    4 LKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSekeLRKARRQ 83
                          90       100
                  ....*....|....*....|.
gi 2119559688 772 IGIVSQE-PVLFDRTIAENIA 791
Cdd:PRK11153   84 IGMIFQHfNLLSSRTVFDNVA 104
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
710-793 1.67e-08

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 56.53  E-value: 1.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 710 TILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVL-FDRTIAE 788
Cdd:PRK10253   21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQE 100

                  ....*
gi 2119559688 789 NIAYG 793
Cdd:PRK10253  101 LVARG 105
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
150-282 1.97e-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: 58.10  E-value: 1.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 150 TIEenIRYGH------LDVTKEDieqaakmanAHDFIMDLP---QKYETLV---------GERGAQLSGGQKQRIAIARA 211
Cdd:TIGR00630 775 TLE--VKYKGkniadvLDMTVEE---------AYEFFEAVPsisRKLQTLCdvglgyirlGQPATTLSGGEAQRIKLAKE 843
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 212 LVR---NPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTIKTADMI------AGFKDGVVAEQGTHNE 281
Cdd:TIGR00630 844 LSKrstGRTLYILDEPTTGLHFDDIKKLLEVLQRlVDKGNTVVVIEHNLDVIKTADYIidlgpeGGDGGGTVVASGTPEE 923

                  .
gi 2119559688 282 L 282
Cdd:TIGR00630 924 V 924
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
708-792 2.18e-08

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 55.49  E-value: 2.18e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVLFDRTIA 787
Cdd:PRK10247   19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFGDTVY 98

                  ....*
gi 2119559688 788 ENIAY 792
Cdd:PRK10247   99 DNLIF 103
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
81-272 2.20e-08

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 56.66  E-value: 2.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  81 NLQIKRGQTVALVGSSGCGKS----TIVQLLQRfydpeEGQI----LIDG---VNLKDINLKWWR-ENIGIVSQEPVlfg 148
Cdd:PRK09473   36 NFSLRAGETLGIVGESGSGKSqtafALMGLLAA-----NGRIggsaTFNGreiLNLPEKELNKLRaEQISMIFQDPM--- 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 149 TTIEENIRYG---------HLDVTK-EDIEQ------AAKMANAHDFIMDLPQKYetlvgergaqlSGGQKQRIAIARAL 212
Cdd:PRK09473  108 TSLNPYMRVGeqlmevlmlHKGMSKaEAFEEsvrmldAVKMPEARKRMKMYPHEF-----------SGGMRQRVMIAMAL 176
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 213 VRNPKILLLDEATSALDTESEGIVQDALE--KASHGRTTIVIAHRLStiktadMIAGFKDGV 272
Cdd:PRK09473  177 LCRPKLLIADEPTTALDVTVQAQIMTLLNelKREFNTAIIMITHDLG------VVAGICDKV 232
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
44-231 2.43e-08

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 57.65  E-value: 2.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  44 SYSTEGKKL-DNFQGNVQirgvhfrypsrpeakilygvnlqikRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIdG 122
Cdd:PRK11147  326 NYQIDGKQLvKDFSAQVQ-------------------------RGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-G 379
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 123 VNLKDINLKWWRENIgivsqEPvlfGTTIEENIRYGHLDVTKEDIEQAAkMANAHDFIMDlPQKYETLVgergAQLSGGQ 202
Cdd:PRK11147  380 TKLEVAYFDQHRAEL-----DP---EKTVMDNLAEGKQEVMVNGRPRHV-LGYLQDFLFH-PKRAMTPV----KALSGGE 445
                         170       180
                  ....*....|....*....|....*....
gi 2119559688 203 KQRIAIARALVRNPKILLLDEATSALDTE 231
Cdd:PRK11147  446 RNRLLLARLFLKPSNLLILDEPTNDLDVE 474
ABC_6TM_PrtD_LapB_HlyB_like cd18566
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ...
414-623 2.48e-08

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: 56.44  E-value: 2.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 414 YVLMfVGVGVISL---IAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRLAtDASQVQGAAGi 490
Cdd:cd18566    42 QVLV-IGVVIAILlesLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFE--REPSGAHLERLN-SLEQIREFLT- 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 491 klGSSLMAFCS---VVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIENIRTVA 567
Cdd:cd18566   117 --GQALLALLDlpfVLIFLGLIWYLGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIK 194
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 568 SLTREDMFQKKFNhELQMPYNIA-LKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLI 623
Cdd:cd18566   195 AMAMEPQMLRRYE-RLQANAAYAgFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLV 250
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
716-806 3.03e-08

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: 56.65  E-value: 3.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 716 DLEVPQGQTVALVGSSGCGKSTTVQL---TERfydPADGIVSLDGHNLKD-LNLQWL---RSQIGIVSQEPVLFD-RTIA 787
Cdd:COG4148    19 DFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEVLQDsARGIFLpphRRRIGYVFQEARLFPhLSVR 95
                          90       100
                  ....*....|....*....|....
gi 2119559688 788 ENIAYG-----DNSREVTMDEIID 806
Cdd:COG4148    96 GNLLYGrkrapRAERRISFDEVVE 119
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
701-822 3.08e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 56.01  E-value: 3.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 701 FRYPTrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNL--KDLNLQWLRSQIGIVSQE 778
Cdd:PRK13636   13 YNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRESVGMVFQD 90
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2119559688 779 P--VLFDRTIAENIAYGDNSREVTMDEIIDAARKANIHNFIASLPD 822
Cdd:PRK13636   91 PdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKD 136
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
60-232 3.25e-08

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 57.05  E-value: 3.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHFRYPsrPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQrfydpeegqilidGVNlKDINLKWWRE---N 136
Cdd:PRK11819    8 TMNRVSKVVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA-------------GVD-KEFEGEARPApgiK 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 137 IGIVSQEPVLFGT-TIEENIRYGHLDVTK-----EDI------------EQAAKMA---------NAHDF------IMD- 182
Cdd:PRK11819   72 VGYLPQEPQLDPEkTVRENVEEGVAEVKAaldrfNEIyaayaepdadfdALAAEQGelqeiidaaDAWDLdsqleiAMDa 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 183 --LPQKyETLVGergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTES 232
Cdd:PRK11819  152 lrCPPW-DAKVT----KLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
702-741 3.27e-08

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 55.45  E-value: 3.27e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2119559688 702 RYPTRpdtTILKGLDLEVPQGQTVALVGSSGCGKSTTVQL 741
Cdd:PRK11247   21 RYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRL 57
cbiO PRK13649
energy-coupling factor transporter ATPase;
712-810 3.63e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 55.52  E-value: 3.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNL----KDLNLQWLRSQIGIVSQ--EPVLFDRT 785
Cdd:PRK13649   23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstsKNKDIKQIRKKVGLVFQfpESQLFEET 102
                          90       100
                  ....*....|....*....|....*
gi 2119559688 786 IAENIAYGDNSREVTMDEIIDAARK 810
Cdd:PRK13649  103 VLKDVAFGPQNFGVSQEEAEALARE 127
ABC_6TM_PrtD_LapB_HlyB_like cd18782
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
414-627 3.76e-08

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of 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: 350055 [Multi-domain]  Cd Length: 294  Bit Score: 55.68  E-value: 3.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 414 YVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRLatdaSQVQGAAGIKLG 493
Cdd:cd18782    44 IGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTIIDHLLRLPLGFFD--KRPVGELSTRI----SELDTIRGFLTG 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 494 SSLMAFCSVVTG---IVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQgaaGKNKEALESAGKIA---IESIENIRTVA 567
Cdd:cd18782   118 TALTTLLDVLFSviyIAVLFSYSPLLTLVVLATVPLQLLLTFLFGPILR---RQIRRRAEASAKTQsylVESLTGIQTVK 194
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 568 SLTREDMFQKKFNHELqmpynialkkAHLIGIGFSLSQAVMFFAYAASF----------WLGAYLIKQSE 627
Cdd:cd18782   195 AQNAELKARWRWQNRY----------ARSLGEGFKLTVLGTTSGSLSQFlnklssllvlWVGAYLVLRGE 254
cbiO PRK13646
energy-coupling factor transporter ATPase;
712-808 3.97e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 55.56  E-value: 3.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDG----HNLKDLNLQWLRSQIGIVSQ--EPVLFDRT 785
Cdd:PRK13646   23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIRPVRKRIGMVFQfpESQLFEDT 102
                          90       100
                  ....*....|....*....|...
gi 2119559688 786 IAENIAYGDNSREVTMDEIIDAA 808
Cdd:PRK13646  103 VEREIIFGPKNFKMNLDEVKNYA 125
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
698-804 4.09e-08

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 56.61  E-value: 4.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 698 NIIFRYPTRPdttILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGhNLKdlnlqwlrsqIGIVSQ 777
Cdd:COG0488     3 NLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR----------IGYLPQ 68
                          90       100
                  ....*....|....*....|....*...
gi 2119559688 778 EPVLFD-RTIAENIAYGDNSREVTMDEI 804
Cdd:COG0488    69 EPPLDDdLTVLDTVLDGDAELRALEAEL 96
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
706-808 5.14e-08

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 54.78  E-value: 5.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 706 RPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVL-FDR 784
Cdd:PRK13548   12 LGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPF 91
                          90       100
                  ....*....|....*....|....*..
gi 2119559688 785 TIAENIAYG---DNSREVTMDEIIDAA 808
Cdd:PRK13548   92 TVEEVVAMGrapHGLSRAEDDALVAAA 118
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
712-811 5.28e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 55.41  E-value: 5.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNL----KDLNLQWLRSQIGIVSQ--EPVLFDRT 785
Cdd:PRK13634   23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkKNKKLKPLRKKVGIVFQfpEHQLFEET 102
                          90       100
                  ....*....|....*....|....*.
gi 2119559688 786 IAENIAYGDNSREVTMDEIIDAARKA 811
Cdd:PRK13634  103 VEKDICFGPMNFGVSEEDAKQKAREM 128
cbiO PRK13640
energy-coupling factor transporter ATPase;
694-821 5.54e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 55.19  E-value: 5.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRPDTtILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDP---ADGIVSLDGHNLKDLNLQWLRS 770
Cdd:PRK13640    6 VEFKHVSFTYPDSKKP-ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIRE 84
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 771 QIGIVSQEP--VLFDRTIAENIAYGDNSREVTMDEIIDAARKA----NIHNFIASLP 821
Cdd:PRK13640   85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVladvGMLDYIDSEP 141
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
712-791 5.57e-08

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 54.11  E-value: 5.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHN---LKDLNLQWLRSQIGIVSQE-PVLFDRTIA 787
Cdd:PRK10908   18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrLKNREVPFLRRQIGMIFQDhHLLMDRTVY 97

                  ....
gi 2119559688 788 ENIA 791
Cdd:PRK10908   98 DNVA 101
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
712-757 6.31e-08

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: 54.39  E-value: 6.31e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDG 757
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG 46
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
702-792 6.32e-08

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: 54.05  E-value: 6.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 702 RYPTRPdTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDlNLQWLRSQIGIVSQEPVL 781
Cdd:cd03263     9 TYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDAL 86
                          90
                  ....*....|..
gi 2119559688 782 FDR-TIAENIAY 792
Cdd:cd03263    87 FDElTVREHLRF 98
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
82-232 6.64e-08

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 56.11  E-value: 6.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  82 LQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDgvnlKDInlkwwrenigIVS---QEP--VLFGTT---IEE 153
Cdd:PRK11147   24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE----QDL----------IVArlqQDPprNVEGTVydfVAE 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 154 NI--------RYGHL------DVTKEDIEQAAKM------ANAHDF---IMDLPQKYETLVGERGAQLSGGQKQRIAIAR 210
Cdd:PRK11147   90 GIeeqaeylkRYHDIshlvetDPSEKNLNELAKLqeqldhHNLWQLenrINEVLAQLGLDPDAALSSLSGGWLRKAALGR 169
                         170       180
                  ....*....|....*....|..
gi 2119559688 211 ALVRNPKILLLDEATSALDTES 232
Cdd:PRK11147  170 ALVSNPDVLLLDEPTNHLDIET 191
ycf16 CHL00131
sulfate ABC transporter protein; Validated
73-246 7.35e-08

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 54.26  E-value: 7.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  73 EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLL--QRFYDPEEGQILIDGVNLKDINLKwWRENIGI--VSQEPV-LF 147
Cdd:CHL00131   19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPE-ERAHLGIflAFQYPIeIP 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 148 GTTIEENIRyghLDVTKEDIEQAAKMANAHDFIMDLPQKYEtLVGERGAQL--------SGGQKQRIAIARALVRNPKIL 219
Cdd:CHL00131   98 GVSNADFLR---LAYNSKRKFQGLPELDPLEFLEIINEKLK-LVGMDPSFLsrnvnegfSGGEKKRNEILQMALLDSELA 173
                         170       180
                  ....*....|....*....|....*..
gi 2119559688 220 LLDEATSALDTesegivqDALEKASHG 246
Cdd:CHL00131  174 ILDETDSGLDI-------DALKIIAEG 193
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
76-259 7.71e-08

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 56.27  E-value: 7.71e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   76 ILYGVNLQIKRGQTVALVGSSGCGKSTIVQLL----QRFYDPEEGQILIDGVNLKDInLKWWRENIGIVSQEPVLFGT-T 150
Cdd:TIGR00956   76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEI-KKHYRGDVVYNAETDVHFPHlT 154
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  151 IEE-----------NIRYghLDVTKEdiEQAAKMANAHDFIMDLPQKYETLVGE---RGaqLSGGQKQRIAIARALVRNP 216
Cdd:TIGR00956  155 VGEtldfaarcktpQNRP--DGVSRE--EYAKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGA 228
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2119559688  217 KILLLDEATSALDTESegivqdALEKASHGRTTIVIAHRLSTI 259
Cdd:TIGR00956  229 KIQCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLV 265
cbiO PRK13641
energy-coupling factor transporter ATPase;
694-810 7.76e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 54.84  E-value: 7.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPtrPDTTI-LKGLD---LEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGH----NLKDLNL 765
Cdd:PRK13641    3 IKFENVDYIYS--PGTPMeKKGLDnisFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpETGNKNL 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2119559688 766 QWLRSQIGIVSQ--EPVLFDRTIAENIAYGDNSREVTMDEIIDAARK 810
Cdd:PRK13641   81 KKLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALK 127
PLN03140 PLN03140
ABC transporter G family member; Provisional
75-257 1.14e-07

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 55.62  E-value: 1.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   75 KILYGVNLQIKRGQTVALVGSSGCGKSTIVQLL--QRFYDPEEGQILIDGVNLKD---INLKWWRENIGIVSQEpvlfgT 149
Cdd:PLN03140   894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGFPKKQetfARISGYCEQNDIHSPQ-----V 968
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  150 TIEENIRYGHL-----DVTKED-------IEQAAKMANAHDFIMDLPqkyetlvGERGaqLSGGQKQRIAIARALVRNPK 217
Cdd:PLN03140   969 TVRESLIYSAFlrlpkEVSKEEkmmfvdeVMELVELDNLKDAIVGLP-------GVTG--LSTEQRKRLTIAVELVANPS 1039
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2119559688  218 ILLLDEATSALDTESEGIVQDALEKA-SHGRTTIVIAHRLS 257
Cdd:PLN03140  1040 IIFMDEPTSGLDARAAAIVMRTVRNTvDTGRTVVCTIHQPS 1080
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
73-262 1.20e-07

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 52.95  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  73 EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKDIN---LKWWRENIGIVSQepvlfgT 149
Cdd:PRK13541   12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAkpyCTYIGHNLGLKLE------M 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 150 TIEENIRYGHLDVTKEDIEQAAkmanAHDFimdlpqKYETLVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALD 229
Cdd:PRK13541   86 TVFENLKFWSEIYNSAETLYAA----IHYF------KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
                         170       180       190
                  ....*....|....*....|....*....|....
gi 2119559688 230 TESEGIVQDALE-KASHGRTTIVIAHRLSTIKTA 262
Cdd:PRK13541  156 KENRDLLNNLIVmKANSGGIVLLSSHLESSIKSA 189
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
77-265 1.34e-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: 52.33  E-value: 1.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  77 LYGVNLQIKRGQTVALVGSSGCGKSTIVQllqrfydpeegqilidgvnlkdinlkwwrenigivsqepvlfgTTIEENIR 156
Cdd:cd03238    11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN-------------------------------------------EGLYASGK 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 157 YGHLDVTKEDIEQAAKMANAHDFIMDLPQKYETLvGERGAQLSGGQKQRIAIARALVRNPK--ILLLDEATSALDTESEG 234
Cdd:cd03238    48 ARLISFLPKFSRNKLIFIDQLQFLIDVGLGYLTL-GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2119559688 235 IVQDALEK-ASHGRTTIVIAHRLSTIKTADMI 265
Cdd:cd03238   127 QLLEVIKGlIDLGNTVILIEHNLDVLSSADWI 158
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
60-229 1.37e-07

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: 54.83  E-value: 1.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  60 QIRGVHFRYPSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPE-EGQILIDGvnlKDINLKWWRENI- 137
Cdd:TIGR02633 259 EARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFING---KPVDIRNPAQAIr 335
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 -------------GIVSQEPVLFGTTIEENIRY---GHLDVTKED--IEQAAKMANAHDFIMDLPQkyetlvgergAQLS 199
Cdd:TIGR02633 336 agiamvpedrkrhGIVPILGVGKNITLSVLKSFcfkMRIDAAAELqiIGSAIQRLKVKTASPFLPI----------GRLS 405
                         170       180       190
                  ....*....|....*....|....*....|
gi 2119559688 200 GGQKQRIAIARALVRNPKILLLDEATSALD 229
Cdd:TIGR02633 406 GGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
80-281 1.40e-07

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 54.92  E-value: 1.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDINLKWWRENI--GIV------SQEPVLFGTTI 151
Cdd:PRK11288  272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG---KPIDIRSPRDAIraGIMlcpedrKAEGIIPVHSV 348
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 152 EENI---------RYGHLdvtkedIEQAAKMANAHDFIMDLPQKY---ETLVGergaQLSGGQKQRIAIARALVRNPKIL 219
Cdd:PRK11288  349 ADNInisarrhhlRAGCL------INNRWEAENADRFIRSLNIKTpsrEQLIM----NLSGGNQQKAILGRWLSEDMKVI 418
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 220 LLDEATSALD--TESEgIVQDALEKASHGRTTIVIAHRL-STIKTADMIAGFKDGVVAEQGTHNE 281
Cdd:PRK11288  419 LLDEPTRGIDvgAKHE-IYNVIYELAAQGVAVLFVSSDLpEVLGVADRIVVMREGRIAGELAREQ 482
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
77-278 1.45e-07

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: 53.39  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  77 LYGVNLQIKRGQTVALVGSSGCGKSTIVQ-----LLQRFYDPEEGQILidgvNLKDInlkWWRENIG---IVSQEPVlfG 148
Cdd:cd03271    11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINdtlypALARRLHLKKEQPG----NHDRI---EGLEHIDkviVIDQSPI--G 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 149 TTIEEN------------------------------IRYGH------LDVTKEDieqaakmanAHDFIMDLPQ---KYET 189
Cdd:cd03271    82 RTPRSNpatytgvfdeirelfcevckgkrynretleVRYKGksiadvLDMTVEE---------ALEFFENIPKiarKLQT 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 190 LV---------GERGAQLSGGQKQRIAIARALVR---NPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRL 256
Cdd:cd03271   153 LCdvglgyiklGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRlVDKGNTVVVIEHNL 232
                         250       260
                  ....*....|....*....|....*...
gi 2119559688 257 STIKTADMI------AGFKDGVVAEQGT 278
Cdd:cd03271   233 DVIKCADWIidlgpeGGDGGGQVVASGT 260
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
69-229 1.72e-07

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 54.55  E-value: 1.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  69 PSRPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPE-EGQILIDGvnlKDINLKWWRENI---------- 137
Cdd:PRK13549  270 PVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDG---KPVKIRNPQQAIaqgiamvped 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 138 ----GIVSQEPVLFGTTIEENIRYGHLDVtkedIEQAAKMANAHDFIMDLPQKYETLVgERGAQLSGGQKQRIAIARALV 213
Cdd:PRK13549  347 rkrdGIVPVMGVGKNITLAALDRFTGGSR----IDDAAELKTILESIQRLKVKTASPE-LAIARLSGGNQQKAVLAKCLL 421
                         170
                  ....*....|....*.
gi 2119559688 214 RNPKILLLDEATSALD 229
Cdd:PRK13549  422 LNPKILILDEPTRGID 437
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
79-259 1.88e-07

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 53.94  E-value: 1.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  79 GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLkdinlkwWRE------NIGIVsqepvlFG---- 148
Cdd:COG4586    40 DISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVP-------FKRrkefarRIGVV------FGqrsq 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 149 -----TTIEEniryghLDVTKE--DIEQAAKMANAHDF--IMDLPQKYETLVgeRgaQLSGGQKQRIAIARALVRNPKIL 219
Cdd:COG4586   107 lwwdlPAIDS------FRLLKAiyRIPDAEYKKRLDELveLLDLGELLDTPV--R--QLSLGQRMRCELAAALLHRPKIL 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2119559688 220 LLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTI 259
Cdd:COG4586   177 FLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDI 218
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
78-266 2.13e-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: 54.41  E-value: 2.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  78 YGVN---L----QIKRGQTVALVGSSGCGKSTIVQLLQrfydpeeGQIlidgvnlkdinlkwwRENIGIVSQEPvlfgtT 150
Cdd:COG1245    83 YGENgfrLyglpVPKKGKVTGILGPNGIGKSTALKILS-------GEL---------------KPNLGDYDEEP-----S 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 151 IEENIRY-------GHL-DVTKEDIEQAAKmanahdfimdlPQ------KY------ETL--VGERGA------------ 196
Cdd:COG1245   136 WDEVLKRfrgtelqDYFkKLANGEIKVAHK-----------PQyvdlipKVfkgtvrELLekVDERGKldelaeklglen 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 197 -------QLSGGQKQRIAIARALVRNPKILLLDEATSALD----TESEGIVQDALEKashGRTTIVIAHRLSTIktaDMI 265
Cdd:COG1245   205 ildrdisELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLIRELAEE---GKYVLVVEHDLAIL---DYL 278

                  .
gi 2119559688 266 A 266
Cdd:COG1245   279 A 279
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
694-764 2.14e-07

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: 53.27  E-value: 2.14e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 694 LSFANIIFRYPT------RPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN 764
Cdd:TIGR02769   3 LEVRDVTHTYRTgglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLD 79
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
710-793 2.18e-07

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 52.83  E-value: 2.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 710 TILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIV-----SLDGHnlKDLNLQ-----WLRSQIGIVSQEP 779
Cdd:PRK11264   17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTA--RSLSQQkglirQLRQHVGFVFQNF 94
                          90
                  ....*....|....*
gi 2119559688 780 VLF-DRTIAENIAYG 793
Cdd:PRK11264   95 NLFpHRTVLENIIEG 109
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
712-809 2.24e-07

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 54.25  E-value: 2.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN-LQWLRSQIGIVSQEPVLF-DRTIAEN 789
Cdd:COG1129    20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAGIAIIHQELNLVpNLSVAEN 99
                          90       100
                  ....*....|....*....|
gi 2119559688 790 IAYGdnsREVTMDEIIDAAR 809
Cdd:COG1129   100 IFLG---REPRRGGLIDWRA 116
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
708-793 2.38e-07

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 52.61  E-value: 2.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTER---FYDPA--DGIVSLDGHNLKDLNLQWLRSQIGIVSQEP-VL 781
Cdd:PRK14247   15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlieLYPEArvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPnPI 94
                          90
                  ....*....|..
gi 2119559688 782 FDRTIAENIAYG 793
Cdd:PRK14247   95 PNLSIFENVALG 106
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
694-804 2.46e-07

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 53.09  E-value: 2.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPtrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNL--KDLNLQWLRSQ 771
Cdd:PRK13638    2 LATSDLWFRYQ---DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdySKRGLLALRQQ 78
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2119559688 772 IGIVSQEP--VLFDRTIAENIAYGDNSREVTMDEI 804
Cdd:PRK13638   79 VATVFQDPeqQIFYTDIDSDIAFSLRNLGVPEAEI 113
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
715-806 2.59e-07

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 53.69  E-value: 2.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 715 LDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNlQWLRSqIGIVSQEPVLFDR-TIAENIAYG 793
Cdd:PRK11607   38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-PYQRP-INMMFQSYALFPHmTVEQNIAFG 115
                          90
                  ....*....|...
gi 2119559688 794 DNSREVTMDEIID 806
Cdd:PRK11607  116 LKQDKLPKAEIAS 128
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
78-266 2.66e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 54.04  E-value: 2.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  78 YGVN---L----QIKRGQTVALVGSSGCGKSTIVQLLQrfydpeeGQIlidgvnlkdinlkwwRENIGIVSQEP----VL 146
Cdd:PRK13409   83 YGVNgfkLyglpIPKEGKVTGILGPNGIGKTTAVKILS-------GEL---------------IPNLGDYEEEPswdeVL 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 147 --F-GTTIE---ENIRYGHLDVTK--EDIEQAAKM--ANAHDFIM--DLPQKYETLVGERG---------AQLSGGQKQR 205
Cdd:PRK13409  141 krFrGTELQnyfKKLYNGEIKVVHkpQYVDLIPKVfkGKVRELLKkvDERGKLDEVVERLGlenildrdiSELSGGELQR 220
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 206 IAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIVIAHRLSTIktaDMIA 266
Cdd:PRK13409  221 VAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAVL---DYLA 278
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
79-229 2.89e-07

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 53.88  E-value: 2.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  79 GVNLQIKRGQTVALVGSSGCGKSTIVQLL--QRfyDPEEGQILIDGVNLKDINLKWWREN-IGIVSQEPVLFGT----TI 151
Cdd:COG3845   276 DVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPRERRRLgVAYIPEDRLGRGLvpdmSV 353
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 152 EENI-----------RYGHLDvTKEDIEQAAKMANAHDfImdLPQKYETLVGergaQLSGGQKQRIAIARALVRNPKILL 220
Cdd:COG3845   354 AENLilgryrrppfsRGGFLD-RKAIRAFAEELIEEFD-V--RTPGPDTPAR----SLSGGNQQKVILARELSRDPKLLI 425

                  ....*....
gi 2119559688 221 LDEATSALD 229
Cdd:COG3845   426 AAQPTRGLD 434
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
711-793 2.94e-07

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 53.90  E-value: 2.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 711 ILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwLRSQIGI--VSQEPVLF-DRTIA 787
Cdd:PRK15439   26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIylVPQEPLLFpNLSVK 104

                  ....*.
gi 2119559688 788 ENIAYG 793
Cdd:PRK15439  105 ENILFG 110
ABC_6TM_CyaB_HlyB_like cd18588
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ...
415-623 3.03e-07

Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. 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 I 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. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).


Pssm-ID: 350032 [Multi-domain]  Cd Length: 294  Bit Score: 52.89  E-value: 3.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 415 VLM--FVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRlatdasqVQGAAGIK- 491
Cdd:cd18588    43 VLAigLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLRLPLSYFE--SRQVGDTVAR-------VRELESIRq 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 492 --LGSSLMA---FCSVVTGIVIGFVFSWKITLLVIAFLPF-----VMIGGALEMQMMQ--GAAGKNKEALesagkiaIES 559
Cdd:cd18588   114 flTGSALTLvldLVFSVVFLAVMFYYSPTLTLIVLASLPLyallsLLVTPILRRRLEEkfQRGAENQSFL-------VET 186
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 560 IENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLI 623
Cdd:cd18588   187 VTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKLTTLAILWFGAYLV 250
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
710-777 3.28e-07

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 52.09  E-value: 3.28e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 710 TILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQW---LRSQ-IGIVSQ 777
Cdd:PRK10584   24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRAKhVGFVFQ 95
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
705-808 3.46e-07

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 53.31  E-value: 3.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 705 TRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEPVL--- 781
Cdd:PRK09536   12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsfe 91
                          90       100
                  ....*....|....*....|....*...
gi 2119559688 782 FD-RTIAENIAYGDNSREVTMDEIIDAA 808
Cdd:PRK09536   92 FDvRQVVEMGRTPHRSRFDTWTETDRAA 119
ABC_6TM_Pgp_ABCB1_D1_like cd18577
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...
1-32 4.42e-07

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: 52.48  E-value: 4.42e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2119559688   1 VFFSVMIGAFSLGNAMPHLQTLATARGAAYYL 32
Cdd:cd18577   269 VFFAVLIGAFSLGQIAPNLQAFAKARAAAAKI 300
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
694-792 4.64e-07

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: 51.13  E-value: 4.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPtrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNlqwlRSQIG 773
Cdd:cd03269     1 LEVENVTKRFG---RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIG 73
                          90       100
                  ....*....|....*....|
gi 2119559688 774 IVSQEPVLF-DRTIAENIAY 792
Cdd:cd03269    74 YLPEERGLYpKMKVIDQLVY 93
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
692-792 6.07e-07

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: 50.63  E-value: 6.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 692 ANLSFANIIF---RYPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQ-LTERFYDPAD-GIVSLDGHNLKdlnLQ 766
Cdd:cd03213     2 VTLSFRNLTVtvkSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNaLAGRRTGLGVsGEVLINGRPLD---KR 78
                          90       100
                  ....*....|....*....|....*..
gi 2119559688 767 WLRSQIGIVSQEPVLFDR-TIAENIAY 792
Cdd:cd03213    79 SFRKIIGYVPQDDILHPTlTVRETLMF 105
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
84-254 6.76e-07

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 52.86  E-value: 6.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  84 IKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlkDINLKWwrenigiVSQE-PVLFGTTIEENIryghlDV 162
Cdd:PRK10636   24 INPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG----NWQLAW-------VNQEtPALPQPALEYVI-----DG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 163 TKE--DIEQAAKMANAHD---FIMDLPQKYETL----VGERGAQL------------------SGGQKQRIAIARALVRN 215
Cdd:PRK10636   88 DREyrQLEAQLHDANERNdghAIATIHGKLDAIdawtIRSRAASLlhglgfsneqlerpvsdfSGGWRMRLNLAQALICR 167
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2119559688 216 PKILLLDEATSALDTesegivqDA---LEK--ASHGRTTIVIAH 254
Cdd:PRK10636  168 SDLLLLDEPTNHLDL-------DAviwLEKwlKSYQGTLILISH 204
cbiO PRK13643
energy-coupling factor transporter ATPase;
694-803 8.57e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 51.66  E-value: 8.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRY-PTRP-DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDG----HNLKDLNLQW 767
Cdd:PRK13643    2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsSTSKQKEIKP 81
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2119559688 768 LRSQIGIVSQEP--VLFDRTIAENIAYGDNSREVTMDE 803
Cdd:PRK13643   82 VRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEK 119
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
694-780 8.77e-07

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: 49.35  E-value: 8.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPtrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN-LQWLRSQI 772
Cdd:cd03216     1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGI 77

                  ....*...
gi 2119559688 773 GIVSQEPV 780
Cdd:cd03216    78 AMVYQLSV 85
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
698-822 9.49e-07

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: 51.39  E-value: 9.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 698 NIIFRYpTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDpADGIVSLDGHNLKDLNLQWLRSQIGIVSQ 777
Cdd:cd03289     7 DLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGVIPQ 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2119559688 778 EPVLFDRTIAENI-AYGDNSREvtmdEIIDAARKANIHNFIASLPD 822
Cdd:cd03289    85 KVFIFSGTFRKNLdPYGKWSDE----EIWKVAEEVGLKSVIEQFPG 126
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
685-793 1.38e-06

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 50.56  E-value: 1.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 685 EQLHTFTANLSFANIIFRYPTRpdtTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN 764
Cdd:PRK10575    3 EYTNHSDTTFALRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS 79
                          90       100       110
                  ....*....|....*....|....*....|
gi 2119559688 765 LQWLRSQIGIVSQE-PVLFDRTIAENIAYG 793
Cdd:PRK10575   80 SKAFARKVAYLPQQlPAAEGMTVRELVAIG 109
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
79-229 1.51e-06

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 51.54  E-value: 1.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  79 GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGvnlKDINLKWWRENI--GIV------SQEPVLFGTT 150
Cdd:PRK10762  270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG---HEVVTRSPQDGLanGIVyisedrKRDGLVLGMS 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 151 IEENIRYGHLDVTKED---IEQAAKMANAHDFIMDLPQK---YETLVGErgaqLSGGQKQRIAIARALVRNPKILLLDEA 224
Cdd:PRK10762  347 VKENMSLTALRYFSRAggsLKHADEQQAVSDFIRLFNIKtpsMEQAIGL----LSGGNQQKVAIARGLMTRPKVLILDEP 422

                  ....*
gi 2119559688 225 TSALD 229
Cdd:PRK10762  423 TRGVD 427
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
712-779 1.81e-06

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 50.73  E-value: 1.81e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN---LQWLRSQIGIVSQEP 779
Cdd:PRK11308   31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP 101
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
59-263 1.99e-06

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 51.17  E-value: 1.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGVHFRYPSRPeakILYGVNLQIKRGQTVALVGSSGCGKSTIVQL------------LQRFydpeeGQILIDGVNLK 126
Cdd:PRK10938  261 IVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLitgdhpqgysndLTLF-----GRRRGSGETIW 332
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 127 DInlkwwRENIGIVSQEPVL---FGTTIEENIRYGHLDVTkeDIEQAAKmanahDFIMDLPQKYETLVGERGAQ------ 197
Cdd:PRK10938  333 DI-----KKHIGYVSSSLHLdyrVSTSVRNVILSGFFDSI--GIYQAVS-----DRQQKLAQQWLDILGIDKRTadapfh 400
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 198 -LSGGQkQRIA-IARALVRNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIV------------IAHRLSTIKTA 262
Cdd:PRK10938  401 sLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfvshhaedapacITHRLEFVPDG 479

                  .
gi 2119559688 263 D 263
Cdd:PRK10938  480 D 480
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
410-807 2.00e-06

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: 51.87  E-value: 2.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  410 KIIQYVLMFVGVGVISLI-------------AYFVQGYMFGRS-------GEYL------TLRLRSMSFKAMLRQEIAFF 463
Cdd:TIGR00957  326 KAIHDLMMFIGPQILSLLirfvndpmapdwqGYFYTGLLFVCAclqtlilHQYFhicfvsGMRIKTAVMGAVYRKALVIT 405
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  464 DD--HNNSVGALTTRLATDASQVqgaagIKLGSSLMAFCSVVTGIVIGFVFSWK----ITLLVIAFLPF-VMIGGALEMQ 536
Cdd:TIGR00957  406 NSarKSSTVGEIVNLMSVDAQRF-----MDLATYINMIWSAPLQVILALYFLWLnlgpSVLAGVAVMVLmVPLNAVMAMK 480
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  537 M--MQGAAGKNKEaleSAGKIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAA 614
Cdd:TIGR00957  481 TktYQVAHMKSKD---NRIKLMNEILNGIKVLKLYAWELAFLDKVEGIRQEELKVLKKSAYLHAVGTFTWVCTPFLVALI 557
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  615 SFWLGAYLikqSEVDYVDVFKAF-SAILFG---------GMAIGNASafapdaaKAEQSAKEIFKLIDKK---PD-IDNE 680
Cdd:TIGR00957  558 TFAVYVTV---DENNILDAEKAFvSLALFNilrfplnilPMVISSIV-------QASVSLKRLRIFLSHEelePDsIERR 627
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  681 SEKGEQLHTFTANlsfaNIIFRYpTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGhnl 760
Cdd:TIGR00957  628 TIKPGEGNSITVH----NATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG--- 699
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*..
gi 2119559688  761 kdlnlqwlrsQIGIVSQEPVLFDRTIAENIAYGDNSREVTMDEIIDA 807
Cdd:TIGR00957  700 ----------SVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEA 736
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
708-780 2.05e-06

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 49.06  E-value: 2.05e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERF--YDPADGIVSLDGHNLKDLNLQwLRSQIGI--VSQEPV 780
Cdd:cd03217    12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGIflAFQYPP 87
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
73-316 2.40e-06

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 51.32  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  73 EAKILYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQI-LIDGVNLkdinlkwwreniGIVSQEPVLFGTTI 151
Cdd:PRK10636  324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKL------------GYFAQHQLEFLRAD 391
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 152 EENIRygHLD-VTKEDIEQAAKmanahDFIMDLPQKYETlVGERGAQLSGGQKQRIAIARALVRNPKILLLDEATSALDT 230
Cdd:PRK10636  392 ESPLQ--HLArLAPQELEQKLR-----DYLGGFGFQGDK-VTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDL 463
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 231 ESEGIVQDAL---EKAshgrtTIVIAHRLSTIK-TADMIAGFKDGVVAE-QGTHNElmskqgiYQQ-LVTLQSMKSADDN 304
Cdd:PRK10636  464 DMRQALTEALidfEGA-----LVVVSHDRHLLRsTTDDLYLVHDGKVEPfDGDLED-------YQQwLSDVQKQENQTDE 531
                         250
                  ....*....|....*...
gi 2119559688 305 EIEDFN------RDDTKR 316
Cdd:PRK10636  532 APKENNansaqaRKDQKR 549
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
197-269 3.03e-06

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


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 48.12  E-value: 3.03e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 197 QLSGGQKQRIAIARAL----VRNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTIKTADMIAGFK 269
Cdd:cd03227    77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEhLVKGAQVIVITHLPELAELADKLIHIK 154
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
694-804 3.22e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 49.36  E-value: 3.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRPDTTiLKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIG 773
Cdd:PRK13648    8 IVFKNVSFQYQSDASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
                          90       100       110
                  ....*....|....*....|....*....|...
gi 2119559688 774 IVSQEP--VLFDRTIAENIAYGDNSREVTMDEI 804
Cdd:PRK13648   87 IVFQNPdnQFVGSIVKYDVAFGLENHAVPYDEM 119
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
698-807 3.49e-06

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: 48.91  E-value: 3.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 698 NIIFRYPtrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHN-LKDlnLQWLRSQIGIVS 776
Cdd:cd03265     5 NLVKKYG---DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDvVRE--PREVRRRIGIVF 79
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2119559688 777 QEPVLFDR-TIAENIA-----YGDNSREVT--MDEIIDA 807
Cdd:cd03265    80 QDLSVDDElTGWENLYiharlYGVPGAERRerIDELLDF 118
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
75-258 3.64e-06

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 50.32  E-value: 3.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  75 KILY-GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILI-DGVNLkdinlkwwreniGIVSQ--EPVLFGTT 150
Cdd:TIGR03719 335 KLLIdDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKL------------AYVDQsrDALDPNKT 402
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 151 IEENIRYG--HLDVTKEDIEQAAKMAnAHDFIMDLPQKyetLVGergaQLSGGQKQRIAIARALVRNPKILLLDEATSAL 228
Cdd:TIGR03719 403 VWEEISGGldIIKLGKREIPSRAYVG-RFNFKGSDQQK---KVG----QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDL 474
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2119559688 229 DTESEGIVQDALEKasHGRTTIVIAH------RLST 258
Cdd:TIGR03719 475 DVETLRALEEALLN--FAGCAVVISHdrwfldRIAT 508
ABC_6TM_exporter_like cd18540
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...
411-653 4.09e-06

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes 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. 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 the chemical 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. However, 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: 349984 [Multi-domain]  Cd Length: 295  Bit Score: 49.40  E-value: 4.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 411 IIQYVLMFVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTTRLATDASQVqgaAGI 490
Cdd:cd18540    41 LTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFEHLQTLSFSYFD--KTPVGWIMARVTSDTQRL---GEI 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 491 kLGSSLM----AFCSVVTGIVIGFVFSWKITLLVIAFLPF-VMIGGALEMQMMQGaagkNKEALESAGKI--AI-ESIEN 562
Cdd:cd18540   116 -ISWGLVdlvwGITYMIGILIVMLILNWKLALIVLAVVPVlAVVSIYFQKKILKA----YRKVRKINSRItgAFnEGITG 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 563 IRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLsqaVMFFAYAAS---FWLGAYLikqsevdyvdvfkafsa 639
Cdd:cd18540   191 AKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPI---VLFLGSIATalvLWYGGIL----------------- 250
                         250
                  ....*....|....
gi 2119559688 640 ILFGGMAIGNASAF 653
Cdd:cd18540   251 VLAGAITIGTLVAF 264
cbiO PRK13644
energy-coupling factor transporter ATPase;
698-793 4.99e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 49.22  E-value: 4.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 698 NIIFRYPTrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN-LQWLRSQIGIVS 776
Cdd:PRK13644    6 NVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLVGIVF 83
                          90
                  ....*....|....*....
gi 2119559688 777 QEP--VLFDRTIAENIAYG 793
Cdd:PRK13644   84 QNPetQFVGRTVEEDLAFG 102
ABC_6TM_PrtD_LapB_HlyB_like cd18783
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...
414-623 5.76e-06

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of 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: 350056 [Multi-domain]  Cd Length: 294  Bit Score: 49.05  E-value: 5.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 414 YVLmfvGVGVISLIAY-----FVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFDdhNNSVGALTtrlatdaSQVQGAA 488
Cdd:cd18783    42 YVL---TIGVVIALLFegilgYLRRYLLLVATTRIDARLALRTFDRLLSLPIDFFE--RTPAGVLT-------KHMQQIE 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 489 GIK---LGSSLMAFCSVVTGIV---IGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAAGKNKEALESAGKIAIESIEN 562
Cdd:cd18783   110 RIRqflTGQLFGTLLDATSLLVflpVLFFYSPTLALVVLAFSALIALIILAFLPPFRRRLQALYRAEGERQAFLVETVHG 189
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2119559688 563 IRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLI 623
Cdd:cd18783   190 IRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMTVGVIWVGAYLV 250
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
692-737 5.95e-06

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 49.46  E-value: 5.95e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2119559688 692 ANLSFANIIFRYPTrpDTTILKGLDLEVPQGQTVALVGSSGCGKST 737
Cdd:PRK11650    2 AGLKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKST 45
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
697-811 6.79e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 48.55  E-value: 6.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 697 ANIIFRYPTRPDTT---ILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQW-LRSQI 772
Cdd:PRK13633    8 KNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIRNKA 87
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2119559688 773 GIVSQEPvlfDRTIA-----ENIAYGDNSREVTMDEI---IDAARKA 811
Cdd:PRK13633   88 GMVFQNP---DNQIVativeEDVAFGPENLGIPPEEIrerVDESLKK 131
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
712-790 7.08e-06

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: 48.20  E-value: 7.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwLRSQIGIVS--QEPVLFDR-TIAE 788
Cdd:cd03219    16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFPElTVLE 94

                  ..
gi 2119559688 789 NI 790
Cdd:cd03219    95 NV 96
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
705-792 7.38e-06

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 48.61  E-value: 7.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 705 TRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWL---RSQIGIVSQEPVL 781
Cdd:PRK11831   16 TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMSMLFQSGAL 95
                          90
                  ....*....|..
gi 2119559688 782 F-DRTIAENIAY 792
Cdd:PRK11831   96 FtDMNVFDNVAY 107
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
708-792 7.91e-06

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 48.12  E-value: 7.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNL---KD---LNLQWLRSQIGIVSQEPVL 781
Cdd:PRK14246   22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDifqIDAIKLRKEVGMVFQQPNP 101
                          90
                  ....*....|..
gi 2119559688 782 FDR-TIAENIAY 792
Cdd:PRK14246  102 FPHlSIYDNIAY 113
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
694-786 8.79e-06

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 49.20  E-value: 8.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRpdTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIG 773
Cdd:PRK10522  323 LELRNVTFAYQDN--GFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS 400
                          90
                  ....*....|...
gi 2119559688 774 IVSQEPVLFDRTI 786
Cdd:PRK10522  401 AVFTDFHLFDQLL 413
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
712-792 9.02e-06

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: 47.75  E-value: 9.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDlNLQWLRSQIGIVSQEPVLFDR-TIAENI 790
Cdd:cd03266    21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDRlTARENL 99

                  ..
gi 2119559688 791 AY 792
Cdd:cd03266   100 EY 101
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
84-259 9.07e-06

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: 46.80  E-value: 9.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  84 IKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNlkdINLKwwrenigivsqepvlfgttieeniryghldvt 163
Cdd:cd03222    22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGIT---PVYK-------------------------------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 164 kedieqaakmanahdfimdlPQKYEtlvgergaqLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKA 243
Cdd:cd03222    67 --------------------PQYID---------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
                         170
                  ....*....|....*...
gi 2119559688 244 S-HG-RTTIVIAHRLSTI 259
Cdd:cd03222   118 SeEGkKTALVVEHDLAVL 135
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
77-261 1.02e-05

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 49.12  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  77 LYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG-VNLKDINLKWWRENIGIVSQE--PVLFGTTIEE 153
Cdd:PRK13545   40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGsAALIAISSGLNGQLTGIENIElkGLMMGLTKEK 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 154 niryghldvTKEDIEQAAKMANAHDFIMDLPQKYetlvgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALD-TES 232
Cdd:PRK13545  120 ---------IKEIIPEIIEFADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGDqTFT 179
                         170       180
                  ....*....|....*....|....*....
gi 2119559688 233 EGIVQDALEKASHGRTTIVIAHRLSTIKT 261
Cdd:PRK13545  180 KKCLDKMNEFKEQGKTIFFISHSLSQVKS 208
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
694-757 1.11e-05

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: 47.53  E-value: 1.11e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2119559688 694 LSFANIIFRYPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDG 757
Cdd:cd03220    20 LKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG 83
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
713-791 1.21e-05

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 48.16  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 713 KGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN-LQWL--RSQIGIVSQEPV--LFDR-TI 786
Cdd:PRK15079   38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKdDEWRavRSDIQMIFQDPLasLNPRmTI 117

                  ....*
gi 2119559688 787 AENIA 791
Cdd:PRK15079  118 GEIIA 122
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
712-822 1.45e-05

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 48.11  E-value: 1.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRS----QIGIVSQEPVLFDR-TI 786
Cdd:PRK10070   44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMPHmTV 123
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2119559688 787 AENIAYGDNSREVTMDE----IIDAARKANIHNFIASLPD 822
Cdd:PRK10070  124 LDNTAFGMELAGINAEErrekALDALRQVGLENYAHSYPD 163
PLN03073 PLN03073
ABC transporter F family; Provisional
66-237 1.48e-05

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 48.70  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  66 FRYPSRPeakILY-GVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILidgvnlkdinlKWWRENIGIVSQEp 144
Cdd:PLN03073  516 FGYPGGP---LLFkNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----------RSAKVRMAVFSQH- 580
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 145 vlfgttieenirygHLDVTkeDIEQAAKMANAHDFIMDLPQKYETLVGERGAQ----------LSGGQKQRIAIARALVR 214
Cdd:PLN03073  581 --------------HVDGL--DLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTgnlalqpmytLSGGQKSRVAFAKITFK 644
                         170       180
                  ....*....|....*....|....
gi 2119559688 215 NPKILLLDEATSALDTES-EGIVQ 237
Cdd:PLN03073  645 KPHILLLDEPSNHLDLDAvEALIQ 668
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
709-793 1.83e-05

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 47.77  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 709 TTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwlRSQIGIVSQEPVLFDR-TIA 787
Cdd:PRK10851   15 TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFRHmTVF 92

                  ....*.
gi 2119559688 788 ENIAYG 793
Cdd:PRK10851   93 DNIAFG 98
cbiO PRK13645
energy-coupling factor transporter ATPase;
689-793 2.05e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 47.31  E-value: 2.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 689 TFTANLSFANIIFRYPTRP--DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGH----NLKD 762
Cdd:PRK13645    2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYaipaNLKK 81
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2119559688 763 LN-LQWLRSQIGIVSQEP--VLFDRTIAENIAYG 793
Cdd:PRK13645   82 IKeVKRLRKEIGLVFQFPeyQLFQETIEKDIAFG 115
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
84-310 2.09e-05

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: 48.47  E-value: 2.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688   84 IKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG----VNLKDINlkwwrENIGIVSQ----EPVLFGTtiEENI 155
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGksilTNISDVH-----QNMGYCPQfdaiDDLLTGR--EHLY 2034
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  156 RYGHL-DVTKEDIEqaaKMANAHDFIMDLPQKYETLVGergaQLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEG 234
Cdd:TIGR01257 2035 LYARLrGVPAEEIE---KVANWSIQSLGLSLYADRLAG----TYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688  235 IVQDALEK-ASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGTHNELMSKQGiYQQLVTLQsMKSADDNEIEDFN 310
Cdd:TIGR01257 2108 MLWNTIVSiIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG-DGYIVTMK-IKSPKDDLLPDLN 2183
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
695-785 2.10e-05

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: 46.37  E-value: 2.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 695 SFANIIFRYPTRPdttILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDlnlqwLRSQIGI 774
Cdd:cd03235     1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK-----ERKRIGY 72
                          90
                  ....*....|.
gi 2119559688 775 VSQEPvLFDRT 785
Cdd:cd03235    73 VPQRR-SIDRD 82
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
694-779 2.21e-05

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 47.93  E-value: 2.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRpdTTILKGLDLEVPQ----------GQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGH---NL 760
Cdd:PRK10261  314 LQVRNLVTRFPLR--SGLLNRVTREVHAvekvsfdlwpGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTL 391
                          90
                  ....*....|....*....
gi 2119559688 761 KDLNLQWLRSQIGIVSQEP 779
Cdd:PRK10261  392 SPGKLQALRRDIQFIFQDP 410
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
712-810 2.50e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 47.00  E-value: 2.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSL---DGHNLK----------DLNLQW----------- 767
Cdd:PRK13651   23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKktkekekvleKLVIQKtrfkkikkike 102
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2119559688 768 LRSQIGIVSQ--EPVLFDRTIAENIAYGDNSREVTMDEIIDAARK 810
Cdd:PRK13651  103 IRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAK 147
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
703-793 2.83e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 46.72  E-value: 2.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 703 YPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQIGIVSQEP--V 780
Cdd:PRK13652   11 YSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQ 90
                          90
                  ....*....|...
gi 2119559688 781 LFDRTIAENIAYG 793
Cdd:PRK13652   91 IFSPTVEQDIAFG 103
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
80-289 2.87e-05

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 47.42  E-value: 2.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDGVNLKD------IN-----LKWWRENIGIVSQEPVLFG 148
Cdd:PRK10982  267 VSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNhnaneaINhgfalVTEERRSTGIYAYLDIGFN 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 149 TTIEENIRYghldVTKEDIEQAAKMANAHDFIMDLPQ----KYETLVGergaQLSGGQKQRIAIARALVRNPKILLLDEA 224
Cdd:PRK10982  347 SLISNIRNY----KNKVGLLDNSRMKSDTQWVIDSMRvktpGHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEP 418
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 225 TSALDTESE-GIVQDALEKASHGRTTIVIAHRL-STIKTADMIAGFKDGVVA-----EQGTHNELMSKQGIY 289
Cdd:PRK10982  419 TRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMpELLGITDRILVMSNGLVAgivdtKTTTQNEILRLASLH 490
ABC_6TM_HetC_like cd18568
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ...
388-641 3.39e-05

Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. 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. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.


Pssm-ID: 350012 [Multi-domain]  Cd Length: 294  Bit Score: 46.40  E-value: 3.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 388 FAVIFSEILGVFA------ILDE--GEQERKIIQYVLM-FVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQ 458
Cdd:cd18568     9 LASLLLQLLGLALplftqiILDRvlVHKNISLLNLILIgLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYKHLLSL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 459 EIAFFDDHNnsVGALTTRLA-TDASQ---VQGAAGIklgssLMAFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALE 534
Cdd:cd18568    89 PLSFFASRK--VGDIITRFQeNQKIRrflTRSALTT-----ILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 535 MQMMQGAagkNKEALESAGKIA---IESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFA 611
Cdd:cd18568   162 SPKLKRN---SREIFQANAEQQsflVEALTGIATIKALAAERPIRWRWENKFAKALNTRFRGQKLSIVLQLISSLINHLG 238
                         250       260       270
                  ....*....|....*....|....*....|
gi 2119559688 612 YAASFWLGAYLIKQSEVDyVDVFKAFSAIL 641
Cdd:cd18568   239 TIAVLWYGAYLVISGQLT-IGQLVAFNMLF 267
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
707-807 3.97e-05

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: 45.78  E-value: 3.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 707 PDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLRSQ----IGIVSQEPVLF 782
Cdd:cd03290    12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
                          90       100
                  ....*....|....*....|....*
gi 2119559688 783 DRTIAENIAYGDNSREVTMDEIIDA 807
Cdd:cd03290    92 NATVEENITFGSPFNKQRYKAVTDA 116
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
707-800 4.11e-05

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 46.98  E-value: 4.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 707 PDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQ-LTERfYDPADGIVSLdGHNLKdlnlqwlrsqIGIVSQEPVLFD-- 783
Cdd:COG0488   326 GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKlLAGE-LEPDSGTVKL-GETVK----------IGYFDQHQEELDpd 393
                          90
                  ....*....|....*...
gi 2119559688 784 RTIAENIA-YGDNSREVT 800
Cdd:COG0488   394 KTVLDELRdGAPGGTEQE 411
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
714-790 4.47e-05

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 45.75  E-value: 4.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 714 GLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWLrSQIGIVS--QEPVLF-DRTIAENI 790
Cdd:PRK11300   23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVRtfQHVRLFrEMTVIENL 101
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
176-285 6.00e-05

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 47.13  E-value: 6.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  176 AHDFIMDLP---QKYETL---------VGERGAQLSGGQKQRIAIARAL---VRNPKILLLDEATSALDTES-EGIVQDA 239
Cdd:PRK00635   776 AEKFFLDEPsihEKIHALcslgldylpLGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDiKALIYVL 855
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2119559688  240 LEKASHGRTTIVIAHRLSTIKTADMI------AGFKDGVVAEQGTHNELMSK 285
Cdd:PRK00635   856 QSLTHQGHTVVIIEHNMHVVKVADYVlelgpeGGNLGGYLLASCSPEELIHL 907
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
692-793 6.41e-05

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 46.18  E-value: 6.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 692 ANLSFANIifrYPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwlRSQ 771
Cdd:PRK11000    2 ASVTLRNV---TKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERG 76
                          90       100
                  ....*....|....*....|...
gi 2119559688 772 IGIVSQEPVLFDR-TIAENIAYG 793
Cdd:PRK11000   77 VGMVFQSYALYPHlSVAENMSFG 99
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
694-811 7.66e-05

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 45.08  E-value: 7.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYPTRPdttILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNlqwlrSQIG 773
Cdd:PRK11248    2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG-----AERG 73
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2119559688 774 IVSQ-EPVLFDRTIAENIAYGDNSREVTMDEIIDAARKA 811
Cdd:PRK11248   74 VVFQnEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQM 112
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
705-820 9.31e-05

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 45.95  E-value: 9.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 705 TRPD-TTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNlkdlnlqwlrsQIGIVSQEPVLFD 783
Cdd:COG4178   371 RTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA-----------RVLFLPQRPYLPL 439
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2119559688 784 RTIAENIAYGDNSREVTMDEIIDAARKANIHNFIASL 820
Cdd:COG4178   440 GTLREALLYPATAEAFSDAELREALEAVGLGHLAERL 476
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
712-793 1.03e-04

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 45.55  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQwLRSQ--IGIVSQEPVLFDR-TIAE 788
Cdd:PRK09700   21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQlgIGIIYQELSVIDElTVLE 99

                  ....*
gi 2119559688 789 NIAYG 793
Cdd:PRK09700  100 NLYIG 104
PLN03232 PLN03232
ABC transporter C family member; Provisional
390-807 1.13e-04

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 46.12  E-value: 1.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  390 VIFSEILgvfAILDEGEQerKIIQYV---LMFVGV--GVISLIAYFVQgymFGRSGeyltLRLRSMSFKAMLRQEIAFFD 464
Cdd:PLN03232   322 VILSHLL---QSMQEGDP--AWVGYVyafLIFFGVtfGVLCESQYFQN---VGRVG----FRLRSTLVAAIFHKSLRLTH 389
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  465 D--HNNSVGALTTRLATDASQVQGAAGIKLGSSLMAFCSVVTGIVI----GfVFSWKITLLVIAFLPFVMIggalemqMM 538
Cdd:PLN03232   390 EarKNFASGKVTNMITTDANALQQIAEQLHGLWSAPFRIIVSMVLLyqqlG-VASLFGSLILFLLIPLQTL-------IV 461
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  539 QGAAGKNKEALESAGK---IAIESIENIRTVASLTREDMFQKKF----NHELQMpyniaLKKAHLIG-----IGFSLSQA 606
Cdd:PLN03232   462 RKMRKLTKEGLQWTDKrvgIINEILASMDTVKCYAWEKSFESRIqgirNEELSW-----FRKAQLLSafnsfILNSIPVV 536
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  607 VMFFAYAASFWLGAYLIKQSEVDYVDVFKAFSAILfggMAIGNASAFAPDAAKAEQSAKEIF----KLIDKKPdidnese 682
Cdd:PLN03232   537 VTLVSFGVFVLLGGDLTPARAFTSLSLFAVLRSPL---NMLPNLLSQVVNANVSLQRIEELLlseeRILAQNP------- 606
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  683 kgeQLHTFTANLSFANIIFRYPTRPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADgIVSLDghnlkd 762
Cdd:PLN03232   607 ---PLQPGAPAISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE-TSSVV------ 676
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 2119559688  763 lnlqwLRSQIGIVSQEPVLFDRTIAENIAYGDNSREVTMDEIIDA 807
Cdd:PLN03232   677 -----IRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDV 716
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
59-278 1.38e-04

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 45.11  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  59 VQIRGV--HFrypsrPEAKILYGVNLQIKRGQTVALVGSSGCGKSTIVqLLQRFYDPEEGQilidgvnlKDINLKWW--- 133
Cdd:NF000106   14 VEVRGLvkHF-----GEVKAVDGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGR--------RPWRF*TWcan 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 134 ----RENIGIvsQEPVLFGT----TIEENIRY--GHLDVTKEDIEQAAKmanahdfimDLPQKYE--TLVGERGAQLSGG 201
Cdd:NF000106   80 rralRRTIG*--HRPVR*GRresfSGRENLYMigR*LDLSRKDARARAD---------ELLERFSltEAAGRAAAKYSGG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 202 QKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKASHGRTTIV-----------IAHRLSTIKTADMIAgfkD 270
Cdd:NF000106  149 MRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLlttqymeeaeqLAHELTVIDRGRVIA---D 225

                  ....*...
gi 2119559688 271 GVVAEQGT 278
Cdd:NF000106  226 GKVDELKT 233
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
709-791 1.42e-04

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 44.04  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 709 TTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDL---NLQWLRSQ-IGIVSQ-EPVLFD 783
Cdd:PRK11629   22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaAKAELRNQkLGFIYQfHHLLPD 101

                  ....*...
gi 2119559688 784 RTIAENIA 791
Cdd:PRK11629  102 FTALENVA 109
PLN03073 PLN03073
ABC transporter F family; Provisional
197-254 1.50e-04

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 45.24  E-value: 1.50e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 197 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEKAShgRTTIVIAH 254
Cdd:PLN03073  344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSH 399
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
197-288 1.50e-04

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 45.16  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 197 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTIKTA-DMIAGFKDGVVA 274
Cdd:PRK09700  409 ELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLT 488
                          90
                  ....*....|....
gi 2119559688 275 EQGTHNELMSKQGI 288
Cdd:PRK09700  489 QILTNRDDMSEEEI 502
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
711-790 1.90e-04

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 44.19  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 711 ILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDL-------------NLQWLRSQIGIVSQ 777
Cdd:PRK10619   20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTMVFQ 99
                          90
                  ....*....|....
gi 2119559688 778 EPVLFDR-TIAENI 790
Cdd:PRK10619  100 HFNLWSHmTVLENV 113
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
694-756 2.80e-04

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: 41.67  E-value: 2.80e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 694 LSFANIIFRYPTRPdttILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLD 756
Cdd:cd03221     1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG 60
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
693-797 2.91e-04

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: 43.03  E-value: 2.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 693 NLSFANIiFRYPTRPDTT--ILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPAD---GIVSLDGHNLKdlNLQW 767
Cdd:cd03234     3 VLPWWDV-GLKAKNWNKYarILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRK--PDQF 79
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2119559688 768 LRSqIGIVSQEPVLFDR-TIAENIAYGDNSR 797
Cdd:cd03234    80 QKC-VAYVRQDDILLPGlTVRETLTYTAILR 109
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
710-779 2.94e-04

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 44.31  E-value: 2.94e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2119559688 710 TILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYdPADGIVSLDGHNLKDLNLQWL---RSQIGIVSQEP 779
Cdd:PRK15134  300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDP 371
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
92-254 3.62e-04

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 44.11  E-value: 3.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  92 LVGSSGCGKSTIVQLLQRFYDPEEGQILIDgVNlkdinlkwwrENIGIVSQEP-----------VLFGTT-----IEENI 155
Cdd:PRK15064   32 LIGANGCGKSTFMKILGGDLEPSAGNVSLD-PN----------ERLGKLRQDQfafeeftvldtVIMGHTelwevKQERD 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 156 R-YGHLDVTKEDIEQAAKM-------------ANAHDFIM----DLPQKYETLvgergAQLSGGQKQRIAIARALVRNPK 217
Cdd:PRK15064  101 RiYALPEMSEEDGMKVADLevkfaemdgytaeARAGELLLgvgiPEEQHYGLM-----SEVAPGWKLRVLLAQALFSNPD 175
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2119559688 218 ILLLDEATSALDTESEGIVQDAL-EKAShgrTTIVIAH 254
Cdd:PRK15064  176 ILLLDEPTNNLDINTIRWLEDVLnERNS---TMIIISH 210
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
198-278 3.94e-04

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 44.25  E-value: 3.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 198 LSGGQKQRIAIARALVR--NPKIL-LLDEATSAL---DtesegiVQ---DALEK-ASHGRTTIVIAHRLSTIKTADMI-- 265
Cdd:COG0178   827 LSGGEAQRVKLASELSKrsTGKTLyILDEPTTGLhfhD------IRkllEVLHRlVDKGNTVVVIEHNLDVIKTADWIid 900
                          90
                  ....*....|....*...
gi 2119559688 266 ----AGFKDG-VVAEqGT 278
Cdd:COG0178   901 lgpeGGDGGGeIVAE-GT 917
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
77-316 4.46e-04

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 42.88  E-value: 4.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  77 LYGVNLQIKRGQTVALVGSSGCGKSTIVQLLQRFYDPEEGQILIDG-VNLKDInlkwwreNIGIVSQepvLFGTtieENI 155
Cdd:PRK13546   40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGeVSVIAI-------SAGLSGQ---LTGI---ENI 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 156 RYGHLDV------TKEDIEQAAKMANAHDFIMDLPQKYetlvgergaqlSGGQKQRIAIARALVRNPKILLLDEATSALD 229
Cdd:PRK13546  107 EFKMLCMgfkrkeIKAMTPKIIEFSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGD 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 230 -TESEGIVQDALEKASHGRTTIVIAHRLSTIKT-ADMIAGFKDGVVAEQGTHNELMSKqgiYQQLvtLQSMKSADDNEIE 307
Cdd:PRK13546  176 qTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK---YEAF--LNDFKKKSKAEQK 250
                         250
                  ....*....|
gi 2119559688 308 DFNRD-DTKR 316
Cdd:PRK13546  251 EFRNKlDESR 260
ABC_6TM_CvaB_RaxB_like cd18567
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ...
418-623 5.21e-04

Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.


Pssm-ID: 350011 [Multi-domain]  Cd Length: 294  Bit Score: 42.83  E-value: 5.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 418 FVGVGVISLIAYFVQGYMFGRSGEYLTLRLRSMSFKAMLRQEIAFFddHNNSVGALTTRLATdASQVQGAAGIKLGSSLM 497
Cdd:cd18567    48 FGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFRHLLRLPLSYF--EKRHLGDIVSRFGS-LDEIQQTLTTGFVEALL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 498 AFCSVVTGIVIGFVFSWKITLLVIAFLPFVMIGGALEMQMMQGAagkNKEALESAGK---IAIESIENIRTVASLTREDM 574
Cdd:cd18567   125 DGLMAILTLVMMFLYSPKLALIVLAAVALYALLRLALYPPLRRA---TEEQIVASAKeqsHFLETIRGIQTIKLFGREAE 201
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2119559688 575 FQKKFNHELQMPYNIALKKAHLiGIGFSLSQAVMF-FAYAASFWLGAYLI 623
Cdd:cd18567   202 REARWLNLLVDAINADIRLQRL-QILFSAANGLLFgLENILVIYLGALLV 250
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
715-792 5.26e-04

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: 43.85  E-value: 5.26e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688  715 LDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLkDLNLQWLRSQIGIVSQEPVLFDR-TIAENIAY 792
Cdd:TIGR01257  949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILF 1026
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
701-779 5.98e-04

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 42.47  E-value: 5.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 701 FRYPT----RPDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQWlRSQ-IGIV 775
Cdd:PRK15112   14 FRYRTgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY-RSQrIRMI 92

                  ....
gi 2119559688 776 SQEP 779
Cdd:PRK15112   93 FQDP 96
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
691-764 6.92e-04

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 43.17  E-value: 6.92e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2119559688 691 TANLSFANIIFRYPTRPDTT-ILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLN 764
Cdd:PRK10535    2 TALLELKDIRRSYPSGEEQVeVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLD 76
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
712-800 7.26e-04

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 43.07  E-value: 7.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 712 LKGLDLEVPQGQTVALVGSSGCGKSTTVQ-LTerfydpadGIVSLDGHNL----KDLNLQWLR-SQ---IGIVSQEPVLF 782
Cdd:PRK10762   20 LSGAALNVYPGRVMALVGENGAGKSTMMKvLT--------GIYTRDAGSIlylgKEVTFNGPKsSQeagIGIIHQELNLI 91
                          90
                  ....*....|....*....
gi 2119559688 783 DR-TIAENIAYGdnsREVT 800
Cdd:PRK10762   92 PQlTIAENIFLG---REFV 107
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
708-801 9.34e-04

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: 42.50  E-value: 9.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPA--DGIVSLDGHNLKDLNLQWL-RSQIGIVSQEPVLF-D 783
Cdd:TIGR02633  13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpE 92
                          90
                  ....*....|....*...
gi 2119559688 784 RTIAENIAYGDnsrEVTM 801
Cdd:TIGR02633  93 LSVAENIFLGN---EITL 107
ABC_6TM_T1SS_like cd18555
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ...
387-623 1.02e-03

Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. 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 I 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). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.


Pssm-ID: 349999 [Multi-domain]  Cd Length: 294  Bit Score: 42.11  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 387 AFAVIFSEILGVFAIL---------DEGEQERKIIQYVLMFVGVGVISLIAY---FVQGYMFGRSGEYLTLRLRSMSFKA 454
Cdd:cd18555     5 ISILLLSLLLQLLTLLipiltqyviDNVIVPGNLNLLNVLGIGILILFLLYGlfsFLRGYIIIKLQTKLDKSLMSDFFEH 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 455 MLRQEIAFFDdhNNSVGALTTRlATDASQVQGAAGIKLGSSLMAFCSVVTGIVIGFVFSWKITLLVIAFlpfVMIGGALE 534
Cdd:cd18555    85 LLKLPYSFFE--NRSSGDLLFR-ANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLL---GLLIVLLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 535 MQMMQGAAGKNKEALESAGK---IAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFA 611
Cdd:cd18555   159 LLTRKKIKKLNQEEIVAQTKvqsYLTETLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFIA 238
                         250
                  ....*....|..
gi 2119559688 612 YAASFWLGAYLI 623
Cdd:cd18555   239 PLLILWIGAYLV 250
PRK01889 PRK01889
GTPase RsgA; Reviewed
84-107 1.08e-03

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 42.23  E-value: 1.08e-03
                          10        20
                  ....*....|....*....|....*
gi 2119559688  84 IKRGQTVALVGSSGCGKSTIV-QLL 107
Cdd:PRK01889  192 LSGGKTVALLGSSGVGKSTLVnALL 216
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
707-810 1.13e-03

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 42.32  E-value: 1.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 707 PDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGhnlKDLNL----QWLRSQIGIVSQEPVLF 782
Cdd:COG3845    16 GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG---KPVRIrsprDAIALGIGMVHQHFMLV 92
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2119559688 783 DR-TIAENIAYGdnsREVTMDEIID--AARK 810
Cdd:COG3845    93 PNlTVAENIVLG---LEPTKGGRLDrkAARA 120
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
709-737 1.14e-03

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 41.10  E-value: 1.14e-03
                          10        20
                  ....*....|....*....|....*....
gi 2119559688 709 TTILKGLDLEVPQGQTVALVGSSGCGKST 737
Cdd:COG2401    43 RYVLRDLNLEIEPGEIVLIVGASGSGKST 71
uvrA PRK00349
excinuclease ABC subunit UvrA;
160-265 1.71e-03

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 41.98  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 160 LDVTkedIEQAAkmanahDFIMDLPQ---KYETLV---------GERGAQLSGGQKQRIAIARALVRNP--KIL-LLDEA 224
Cdd:PRK00349  790 LDMT---VEEAL------EFFEAIPKiarKLQTLVdvglgyiklGQPATTLSGGEAQRVKLAKELSKRStgKTLyILDEP 860
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2119559688 225 TSALDTES--------EGIVQdalekasHGRTTIVIAHRLSTIKTADMI 265
Cdd:PRK00349  861 TTGLHFEDirkllevlHRLVD-------KGNTVVVIEHNLDVIKTADWI 902
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
80-284 1.72e-03

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 41.33  E-value: 1.72e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  80 VNLQIKRGQTVALVGSSGCGKSTIVQLLQRFyDPEEGQILIDGVNLKDINL---------KWWRENIGIVSQEP------ 144
Cdd:PRK15093   26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTADRMRFDDIDLlrlsprerrKLVGHNVSMIFQEPqscldp 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 145 -VLFGTTIEENI-----------RYGHLdvTKEDIEQAAKMA-NAHDFIM-DLPqkYEtlvgergaqLSGGQKQRIAIAR 210
Cdd:PRK15093  105 sERVGRQLMQNIpgwtykgrwwqRFGWR--KRRAIELLHRVGiKDHKDAMrSFP--YE---------LTEGECQKVMIAI 171
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2119559688 211 ALVRNPKILLLDEATSALDTESEGIVQDALEK--ASHGRTTIVIAHRLSTI-KTADMIAGFKDGVVAEQGTHNELMS 284
Cdd:PRK15093  172 ALANQPRLLIADEPTNAMEPTTQAQIFRLLTRlnQNNNTTILLISHDLQMLsQWADKINVLYCGQTVETAPSKELVT 248
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
708-763 1.77e-03

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 40.93  E-value: 1.77e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 708 DTTILKGLDLEVPQGQTVALVGSSGCGKST-TVQLTERF-YDPADGIVSLDGHNLKDL 763
Cdd:PRK09580   13 DKAILRGLNLEVRPGEVHAIMGPNGSGKSTlSATLAGREdYEVTGGTVEFKGKDLLEL 70
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
691-793 1.99e-03

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 41.44  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 691 TANLSFANIIFRYPtrpDTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLKDLNLQ-WLR 769
Cdd:PRK11288    2 SPYLSFDGIGKTFP---GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALA 78
                          90       100
                  ....*....|....*....|....*
gi 2119559688 770 SQIGIVSQEPVLF-DRTIAENIAYG 793
Cdd:PRK11288   79 AGVAIIYQELHLVpEMTVAENLYLG 103
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
709-807 2.02e-03

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 41.82  E-value: 2.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688  709 TTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGhnlkdlnlqwlrsQIGIVSQEPVLFDRTIAE 788
Cdd:TIGR01271  439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSPQTSWIMPGTIKD 505
                           90
                   ....*....|....*....
gi 2119559688  789 NIAYGDNSREVTMDEIIDA 807
Cdd:TIGR01271  506 NIIFGLSYDEYRYTSVIKA 524
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
707-738 2.36e-03

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 40.45  E-value: 2.36e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2119559688 707 PDTTILKGLDLEVPQGQTVALVGSSGCGKSTT 738
Cdd:PRK10418   14 AAQPLVHGVSLTLQRGRVLALVGGSGSGKSLT 45
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
694-737 2.44e-03

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: 39.44  E-value: 2.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2119559688 694 LSFANIIFRYPTrpDTTILKGLDLEVPQGQTVALVGSSGCGKST 737
Cdd:cd03223     1 IELENLSLATPD--GRVLLKDLSFEIKPGDRLLITGPSGTGKSS 42
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
178-277 2.49e-03

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: 40.32  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 178 DFIMDLPQKYETLvgERGAQ-LSGGQKQRIAIARALVRNPK--ILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIA 253
Cdd:cd03270   119 GFLVDVGLGYLTL--SRSAPtLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRlRDLGNTVLVVE 196
                          90       100       110
                  ....*....|....*....|....*....|
gi 2119559688 254 HRLSTIKTADMI------AGFKDGVVAEQG 277
Cdd:cd03270   197 HDEDTIRAADHVidigpgAGVHGGEIVAQG 226
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
694-817 2.84e-03

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: 39.94  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 694 LSFANIIFRYP-TRPDTTILKGLDLEVPQGQTVALVGSSGCGKST----TVQLTERFYDPaDGIVSLDGHNLKDLNLQWl 768
Cdd:cd03233     4 LSWRNISFTTGkGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKEFAEKY- 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2119559688 769 RSQIGIVSQEpvlfDRTIAeniaygdnsrEVTMDEIIDAARKANIHNFI 817
Cdd:cd03233    82 PGEIIYVSEE----DVHFP----------TLTVRETLDFALRCKGNEFV 116
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
680-803 3.52e-03

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213258 [Multi-domain]  Cd Length: 282  Bit Score: 40.23  E-value: 3.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 680 ESEKGEQLHTFTANLSFANIIFRYptrpdTTILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGhn 759
Cdd:cd03291    26 QENNDRKHSSDDNNLFFSNLCLVG-----APVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-- 98
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2119559688 760 lkdlnlqwlrsQIGIVSQEPVLFDRTIAENIAYGdnsreVTMDE 803
Cdd:cd03291    99 -----------RISFSSQFSWIMPGTIKENIIFG-----VSYDE 126
PRK01889 PRK01889
GTPase RsgA; Reviewed
721-739 3.67e-03

GTPase RsgA; Reviewed


Pssm-ID: 234988 [Multi-domain]  Cd Length: 356  Bit Score: 40.30  E-value: 3.67e-03
                          10
                  ....*....|....*....
gi 2119559688 721 QGQTVALVGSSGCGKSTTV 739
Cdd:PRK01889  194 GGKTVALLGSSGVGKSTLV 212
ABC_6TM_LapB_like cd18587
Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; ...
417-623 3.69e-03

Six-transmembrane helical domain of the ABC transporter subunit LapB and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), such as LapB. LapB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion, LapA is a RTX (repeats in toxin) protein found in Pseudomonas fluorescens and is required for biofilm formation in this organism. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. In this T1SS system, LapB is a cytoplasmic membrane-localized ATPase, LapC is a membrane fusion protein, and LapE is an outer membrane protein.


Pssm-ID: 350031  Cd Length: 293  Bit Score: 40.11  E-value: 3.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 417 MFVGVGVI---SLIAYFVQGYMFGRSGEYLTLRLRSMSF-KAM-LRqeiafFDDHNNSVGALttrlatdASQVQGAAGIK 491
Cdd:cd18587    44 LAIGVLIAllfDFILKLLRAYFIDVAGKRADVILSSRLFeRVLgLR-----LEARPASVGSF-------ANNLREFESVR 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2119559688 492 lgsSLMAFCSVVTGIVIGFVFswkITLLVIAFL-------PFV----MIGGALEMQ---------MMQGAAGKNKeales 551
Cdd:cd18587   112 ---DFFTSATLTALIDLPFVL---LFLAVIALIggplalvPLVaiplVLLYGLLLQkplrrlveeSMRESAQKNA----- 180
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2119559688 552 agkIAIESIENIRTVASLTREDMFQKKFNHELQMPYNIALKKAHLIGIGFSLSQAVMFFAYAASFWLGAYLI 623
Cdd:cd18587   181 ---LLVESLSGLETIKALGAEGRMQRRWEEAVAALARSSLKSRLLSSSATNFAQFVQQLVTVAIVIVGVYLI 249
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
198-229 4.09e-03

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 40.42  E-value: 4.09e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2119559688 198 LSGGQKQRIAIARALVRNPKILLLDEATSALD 229
Cdd:PRK15439  404 LSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
694-761 5.22e-03

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 39.16  E-value: 5.22e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2119559688 694 LSFANIIFRYPTRPdttILKGLDLEVPQGQTVALVGSSGCGKSTTVQLTERFYDPADGIVSLDGHNLK 761
Cdd:PRK13540    2 LDVIELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK 66
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
191-265 6.06e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 40.20  E-value: 6.06e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2119559688  191 VGERGAQLSGGQKQRIAIARALVRNPK---ILLLDEATSALDTESEGIVQDALEK-ASHGRTTIVIAHRLSTIKTADMI 265
Cdd:PRK00635  1693 LGQNLSSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTlVSLGHSVIYIDHDPALLKQADYL 1771
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
197-241 6.20e-03

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 40.10  E-value: 6.20e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2119559688 197 QLSGGQKQRIAIARALVRNPKILLLDEATSALDTESEGIVQDALE 241
Cdd:PRK11819  445 VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALL 489
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
721-769 6.21e-03

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: 38.12  E-value: 6.21e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2119559688  721 QGQTVALVGSSGCGKSTTVQLTERFYDPAD-GIVSLDGHNLKDLNLQWLR 769
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGgGVIYIDGEDILEEVLDQLL 50
ABC_6TM_Pgp_ABCB1 cd18558
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ...
1-32 6.64e-03

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: 39.57  E-value: 6.64e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2119559688   1 VFFSVMIGAFSLGNAMPHLQTLATARGAAYYL 32
Cdd:cd18558   281 VFFSVLIGAFSAGQQVPSIEAFANARGAAYHI 312
YjeQ_EngC cd01854
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ...
86-117 9.70e-03

Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.


Pssm-ID: 206747 [Multi-domain]  Cd Length: 211  Bit Score: 38.15  E-value: 9.70e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2119559688  86 RGQTVALVGSSGCGKSTIVQLLQrfydPEEGQ 117
Cdd:cd01854    84 KGKTSVLVGQSGVGKSTLLNALL----PELVL 111
 
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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