|
Name |
Accession |
Description |
Interval |
E-value |
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-239 |
2.55e-162 |
|
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: 448.47 E-value: 2.55e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGV 81
Cdd:cd03252 1 ITFEHVRFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKIL 161
Cdd:cd03252 81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1MT0_A 162 IFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEpESLYSYLYQLQ 239
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAE-NGLYAYLYQLQ 237
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
1-241 |
7.08e-160 |
|
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: 459.21 E-value: 7.08e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 1 DITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVG 80
Cdd:TIGR01846 455 AITFENIRFRYAPDSPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMG 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 81 VVLQDNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKI 160
Cdd:TIGR01846 535 VVLQENVLFSRSIRDNIALCNPGAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRI 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 161 LIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEpESLYSYLYQLQS 240
Cdd:TIGR01846 615 LIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLAL-QGLYARLWQQQS 693
|
.
1MT0_A 241 D 241
Cdd:TIGR01846 694 G 694
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
1-239 |
1.33e-134 |
|
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: 394.97 E-value: 1.33e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 1 DITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVG 80
Cdd:COG2274 473 DIELENVSFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 81 VVLQDNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKI 160
Cdd:COG2274 553 VVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPRI 632
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1MT0_A 161 LIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLsEPESLYSYLYQLQ 239
Cdd:COG2274 633 LILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELL-ARKGLYAELVQQQ 710
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
1-240 |
3.42e-130 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 379.51 E-value: 3.42e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 1 DITFRNIRFRYKPDSPViLDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVG 80
Cdd:COG1132 339 EIEFENVSFSYPGDRPV-LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 81 VVLQDNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKI 160
Cdd:COG1132 418 VVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPPI 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 161 LIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEpESLYSYLYQLQS 240
Cdd:COG1132 498 LILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLAR-GGLYARLYRLQF 576
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
2-239 |
3.45e-114 |
|
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: 326.42 E-value: 3.45e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRY--KPDSPvILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQV 79
Cdd:cd03249 1 IEFKNVSFRYpsRPDVP-ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 80 GVVLQDNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPK 159
Cdd:cd03249 80 GLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 160 ILIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEPEsLYSYLYQLQ 239
Cdd:cd03249 160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKG-VYAKLVKAQ 238
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-236 |
9.54e-112 |
|
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: 320.33 E-value: 9.54e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGV 81
Cdd:cd03251 1 VEFKNVTFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKIL 161
Cdd:cd03251 81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1MT0_A 162 IFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEpESLYSYLY 236
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQ-GGVYAKLH 234
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-239 |
5.05e-108 |
|
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: 311.09 E-value: 5.05e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPvILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGV 81
Cdd:cd03253 1 IEFENVTFAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKIL 161
Cdd:cd03253 80 VPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1MT0_A 162 IFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLsEPESLYSYLYQLQ 239
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELL-AKGGLYAEMWKAQ 236
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
1-227 |
2.83e-105 |
|
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: 315.16 E-value: 2.83e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 1 DITFRNIRFRYkPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVG 80
Cdd:COG4988 336 SIELEDVSFSY-PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 81 VVLQDNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKI 160
Cdd:COG4988 415 WVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPL 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1MT0_A 161 LIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSE 227
Cdd:COG4988 495 LLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-240 |
6.48e-103 |
|
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: 310.21 E-value: 6.48e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPvILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGV 81
Cdd:COG5265 358 VRFENVSFGYDPERP-ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKIL 161
Cdd:COG5265 437 VPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPIL 516
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1MT0_A 162 IFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLsEPESLYSYLYQLQS 240
Cdd:COG5265 517 IFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELL-AQGGLYAQMWARQQ 594
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
1-225 |
6.62e-100 |
|
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: 290.28 E-value: 6.62e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 1 DITFRNIRFRYKPDSPViLDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVG 80
Cdd:cd03254 2 EIEFENVNFSYDEKKPV-LKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 81 VVLQDNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKI 160
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
1MT0_A 161 LIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELL 225
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELL 225
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
1-239 |
1.72e-96 |
|
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: 293.14 E-value: 1.72e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 1 DITFRNIRFRY--KPDSPViLDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQ 78
Cdd:TIGR02204 337 EIEFEQVNFAYpaRPDQPA-LDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRAR 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 79 VGVVLQDNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNP 158
Cdd:TIGR02204 416 MALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIARAILKDA 495
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 159 KILIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEPEsLYSYLYQL 238
Cdd:TIGR02204 496 PILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIAKGG-LYARLARL 574
|
.
1MT0_A 239 Q 239
Cdd:TIGR02204 575 Q 575
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
1-238 |
1.76e-95 |
|
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: 290.13 E-value: 1.76e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 1 DITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVG 80
Cdd:COG4987 333 SLELEDVSFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 81 VVLQDNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKI 160
Cdd:COG4987 413 VVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPI 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1MT0_A 161 LIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEPESlYSYLYQL 238
Cdd:COG4987 493 LLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLAQNGR-YRQLYQR 569
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
1-239 |
1.83e-93 |
|
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: 285.07 E-value: 1.83e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 1 DITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLA---LADpnwLRR 77
Cdd:TIGR02203 330 DVEFRNVTFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAdytLAS---LRR 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 78 QVGVVLQDNVLLNRSIIDNISLANPG-MSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVN 156
Cdd:TIGR02203 407 QVALVSQDVVLFNDTIANNIAYGRTEqADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAIARALLK 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 157 NPKILIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEpESLYSYLY 236
Cdd:TIGR02203 487 DAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLAR-NGLYAQLH 565
|
...
1MT0_A 237 QLQ 239
Cdd:TIGR02203 566 NMQ 568
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-214 |
2.09e-89 |
|
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: 261.16 E-value: 2.09e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGV 81
Cdd:cd03228 1 IEFKNVSFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLNRSIIDNIslanpgmsvekviyaaklagahdfiselregyntivgeqgagLSGGQRQRIAIARALVNNPKIL 161
Cdd:cd03228 81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
1MT0_A 162 IFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGK 214
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
1-239 |
1.49e-86 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 267.66 E-value: 1.49e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 1 DITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDL---ALADpnwLRR 77
Cdd:PRK11176 341 DIEFRNVTFTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLrdyTLAS---LRN 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 78 QVGVVLQDNVLLNRSIIDNISLANPGM-SVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVN 156
Cdd:PRK11176 418 QVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLR 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 157 NPKILIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLsEPESLYSYLY 236
Cdd:PRK11176 498 DSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELL-AQNGVYAQLH 576
|
...
1MT0_A 237 QLQ 239
Cdd:PRK11176 577 KMQ 579
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
2-233 |
1.03e-84 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 266.20 E-value: 1.03e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRY--KPDSPViLDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQV 79
Cdd:TIGR00958 479 IEFQDVSFSYpnRPDVPV-LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQV 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 80 GVVLQDNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPK 159
Cdd:TIGR00958 558 ALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPR 637
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1MT0_A 160 ILIFDEATSALDYESEHVIMRNMHKicKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEPESLYS 233
Cdd:TIGR00958 638 VLILDEATSALDAECEQLLQESRSR--ASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
1-225 |
3.75e-84 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 261.43 E-value: 3.75e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 1 DITFRNIRFRYkPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVG 80
Cdd:PRK13657 334 AVEFDDVSFSY-DNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 81 VVLQDNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKI 160
Cdd:PRK13657 413 VVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPI 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
1MT0_A 161 LIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELL 225
Cdd:PRK13657 493 LILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELV 557
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
1-219 |
4.67e-84 |
|
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: 249.43 E-value: 4.67e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 1 DITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVG 80
Cdd:cd03245 2 RIEFRNVSFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 81 VVLQDNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKI 160
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
1MT0_A 161 LIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQG 219
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
1-228 |
7.89e-84 |
|
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: 262.97 E-value: 7.89e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 1 DITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVG 80
Cdd:TIGR03797 451 AIEVDRVTFRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLG 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 81 VVLQDNVLLNRSIIDNISLANPgMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKI 160
Cdd:TIGR03797 531 VVLQNGRLMSGSIFENIAGGAP-LTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRI 609
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1MT0_A 161 LIFDEATSALDYESEHVIMRNMHKIckGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEP 228
Cdd:TIGR03797 610 LLFDEATSALDNRTQAIVSESLERL--KVTRIVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMARE 675
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
2-215 |
7.85e-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: 244.30 E-value: 7.85e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRY--KPDSPViLDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQV 79
Cdd:cd03248 12 VKFQNVTFAYptRPDTLV-LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 80 GVVLQDNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPK 159
Cdd:cd03248 91 SLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQ 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
1MT0_A 160 ILIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKI 215
Cdd:cd03248 171 VLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
2-228 |
8.21e-77 |
|
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: 245.24 E-value: 8.21e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGV 81
Cdd:TIGR03796 478 VELRNITFGYSPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAM 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKIL 161
Cdd:TIGR03796 558 VDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSIL 637
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1MT0_A 162 IFDEATSALDYESEHVIMRNMHKicKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEP 228
Cdd:TIGR03796 638 ILDEATSALDPETEKIIDDNLRR--RGCTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVG 702
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-210 |
1.18e-74 |
|
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: 235.26 E-value: 1.18e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGV 81
Cdd:TIGR02857 322 LEFSGVSVAY-PGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKIL 161
Cdd:TIGR02857 401 VPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLL 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
1MT0_A 162 IFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVM 210
Cdd:TIGR02857 481 LLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
1-219 |
3.32e-71 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 216.98 E-value: 3.32e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 1 DITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVG 80
Cdd:cd03244 2 DIEFKNVSLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 81 VVLQDNVLLNRSIIDNIslaNP-GMSVEKVIYAA-KLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNP 158
Cdd:cd03244 82 IIPQDPVLFSGTIRSNL---DPfGEYSDEELWQAlERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
1MT0_A 159 KILIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQG 219
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFD 219
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
2-235 |
1.86e-70 |
|
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: 225.92 E-value: 1.86e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGV 81
Cdd:TIGR01192 335 VEFRHITFEF-ANSSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIAT 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKIL 161
Cdd:TIGR01192 414 VFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHDFILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPIL 493
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1MT0_A 162 IFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEPESLYSYL 235
Cdd:TIGR01192 494 VLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLIEKGSFQELIQKDGRFYKLL 567
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-227 |
6.83e-68 |
|
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: 218.46 E-value: 6.83e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGV 81
Cdd:COG4618 331 LSVENLTVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGY 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLNRSIIDNIS-LANPgmSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKI 160
Cdd:COG4618 411 LPQDVELFDGTIAENIArFGDA--DPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRL 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1MT0_A 161 LIFDEATSALDYESEHVIMRNMHKICK-GRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSE 227
Cdd:COG4618 489 VVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-231 |
2.72e-65 |
|
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: 202.18 E-value: 2.72e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGV 81
Cdd:COG1122 1 IELENLSFSY-PGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQ--DNVLLNRSIIDNI--SLANPGMS----VEKVIYAAKLAGahdfISELREgYNTivgeqgAGLSGGQRQRIAIARA 153
Cdd:COG1122 80 VFQnpDDQLFAPTVEEDVafGPENLGLPreeiRERVEEALELVG----LEHLAD-RPP------HELSGGQKQRVAIAGV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 154 LVNNPKILIFDEATSALDYESEHVIMRNMHKICK-GRTVIIIAHRLSTV-KNADRIIVMEKGKIVEQGKHKELLSEPESL 231
Cdd:COG1122 149 LAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKeGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDYELL 228
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
6-239 |
5.89e-64 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 208.41 E-value: 5.89e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 6 NIR-FRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGVVLQ 84
Cdd:PRK10789 317 NIRqFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 85 DNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKILIFD 164
Cdd:PRK10789 397 TPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1MT0_A 165 EATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEPeSLYSYLYQLQ 239
Cdd:PRK10789 477 DALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQS-GWYRDMYRYQ 550
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
1-237 |
1.75e-63 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 207.37 E-value: 1.75e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 1 DITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVG 80
Cdd:PRK11160 338 SLTLNNVSFTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAIS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 81 VVLQDNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFIsELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKI 160
Cdd:PRK11160 418 VVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQQVGLEKLL-EDDKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPL 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1MT0_A 161 LIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEpESLYSYLYQ 237
Cdd:PRK11160 497 LLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQ-QGRYYQLKQ 572
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
11-241 |
3.35e-63 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 207.00 E-value: 3.35e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 11 YKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFyIPENGQVLIDGHDLALADPNWLRRQVGVVLQDNVLLN 90
Cdd:PRK11174 358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGF-LPYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPH 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 91 RSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKILIFDEATSAL 170
Cdd:PRK11174 437 GTLRDNVLLGNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1MT0_A 171 DYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEPESLYSYLYQLQSD 241
Cdd:PRK11174 517 DAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQEE 587
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
1-239 |
1.10e-61 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 203.03 E-value: 1.10e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 1 DITFRNIRFRYKPDSPViLDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVG 80
Cdd:PRK10790 340 RIDIDNVSFAYRDDNLV-LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVA 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 81 VVLQDNVLLNRSIIDNISLANPgMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKI 160
Cdd:PRK10790 419 MVQQDPVVLADTFLANVTLGRD-ISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQI 497
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1MT0_A 161 LIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEpESLYSYLYQLQ 239
Cdd:PRK10790 498 LILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA-QGRYWQMYQLQ 575
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
1-227 |
2.50e-61 |
|
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: 204.20 E-value: 2.50e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 1 DITFRNIRFRYKPDSPvILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVG 80
Cdd:TIGR01193 473 DIVINDVSYSYGYGSN-ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 81 VVLQDNVLLNRSIIDNISL-ANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPK 159
Cdd:TIGR01193 552 YLPQEPYIFSGSILENLLLgAKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSK 631
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1MT0_A 160 ILIFDEATSALDYESEHVIMRNMHKIcKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSE 227
Cdd:TIGR01193 632 VLILDESTSNLDTITEKKIVNNLLNL-QDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-232 |
5.16e-61 |
|
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: 199.36 E-value: 5.16e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRY---KPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLA---LADPNWL 75
Cdd:COG1123 261 LEVRNLSKRYpvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTklsRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 76 RRQVGVVLQDNvllNRSIidnislaNPGMSVEKVI-YAAKLAG------AHDFISELREgyntIVG--EQGAG-----LS 141
Cdd:COG1123 341 RRRVQMVFQDP---YSSL-------NPRMTVGDIIaEPLRLHGllsraeRRERVAELLE----RVGlpPDLADrypheLS 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 142 GGQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQ 218
Cdd:COG1123 407 GGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDLAVVRYiADRVAVMYDGRIVED 486
|
250
....*....|....
1MT0_A 219 GKHKELLSEPESLY 232
Cdd:COG1123 487 GPTEEVFANPQHPY 500
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-231 |
1.33e-60 |
|
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: 191.49 E-value: 1.33e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNW-LRRQVG 80
Cdd:TIGR04520 1 IEVENVSFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWeIRKKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 81 VVLQ--DNVLLNRSIIDNI--SLANPGMS----VEKVIYAAKLAGAHDFISelREGYNtivgeqgagLSGGQRQRIAIAR 152
Cdd:TIGR04520 81 MVFQnpDNQFVGATVEDDVafGLENLGVPreemRKRVDEALKLVGMEDFRD--REPHL---------LSGGQKQRVAIAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 153 ALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEPES 230
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFSQVEL 229
|
.
1MT0_A 231 L 231
Cdd:TIGR04520 230 L 230
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-227 |
7.28e-59 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 194.49 E-value: 7.28e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGV 81
Cdd:TIGR01842 317 LSVENVTIVPPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGY 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKIL 161
Cdd:TIGR01842 397 LPQDVELFPGTVAENIARFGENADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPKLV 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1MT0_A 162 IFDEATSALDYESEHVIMRNMHKI-CKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSE 227
Cdd:TIGR01842 477 VLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
2-229 |
5.42e-58 |
|
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: 183.55 E-value: 5.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIR--FRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWL---R 76
Cdd:cd03258 2 IELKNVSkvFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 77 RQVGVVLQD-NVLLNRSIIDNISLANPGMSVEKVIYAAKlagahdfISELREgyntIVGEQG------AGLSGGQRQRIA 149
Cdd:cd03258 82 RRIGMIFQHfNLLSSRTVFENVALPLEIAGVPKAEIEER-------VLELLE----LVGLEDkadaypAQLSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 150 IARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLS 226
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEVFA 230
|
...
1MT0_A 227 EPE 229
Cdd:cd03258 231 NPQ 233
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-219 |
5.58e-58 |
|
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: 183.48 E-value: 5.58e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 6 NIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWL---RRQVGVV 82
Cdd:cd03257 8 SVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKEIQMV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 83 LQDNVLlnrsiidniSLaNPGMSVEKVIY-AAKLAGAHDFISELREgyntIVGEQGAG--------------LSGGQRQR 147
Cdd:cd03257 88 FQDPMS---------SL-NPRMTIGEQIAePLRIHGKLSKKEARKE----AVLLLLVGvglpeevlnrypheLSGGQRQR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1MT0_A 148 IAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQG 219
Cdd:cd03257 154 VAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
1-219 |
2.79e-57 |
|
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: 181.07 E-value: 2.79e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 1 DITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVG 80
Cdd:cd03369 6 EIEVENLSVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 81 VVLQDNVLLNRSIIDNISLANpgMSVEKVIYAAklagahdfiseLRegyntiVGEQGAGLSGGQRQRIAIARALVNNPKI 160
Cdd:cd03369 86 IIPQDPTLFSGTIRSNLDPFD--EYSDEEIYGA-----------LR------VSEGGLNLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
1MT0_A 161 LIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQG 219
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-214 |
5.09e-57 |
|
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: 180.36 E-value: 5.09e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 4 FRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGVVL 83
Cdd:cd03225 2 LKNLSFSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 84 Q--DNVLLNRSIIDNI--SLANPGMS----VEKVIYAAKLAGahdfISELREgYNTivgeqgAGLSGGQRQRIAIARALV 155
Cdd:cd03225 82 QnpDDQFFGPTVEEEVafGLENLGLPeeeiEERVEEALELVG----LEGLRD-RSP------FTLSGGQKQRVAIAGVLA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
1MT0_A 156 NNPKILIFDEATSALDYESEHVIMRNMHKICK-GRTVIIIAHRLSTVKN-ADRIIVMEKGK 214
Cdd:cd03225 151 MDPDILLLDEPTAGLDPAGRRELLELLKKLKAeGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-215 |
7.31e-57 |
|
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: 178.95 E-value: 7.31e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGV 81
Cdd:cd03246 1 LEVENVSFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLNRSIIDNIslanpgmsvekviyaaklagahdfiselregyntivgeqgagLSGGQRQRIAIARALVNNPKIL 161
Cdd:cd03246 81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
1MT0_A 162 IFDEATSALDYESEHVIMRN--MHKIcKGRTVIIIAHRLSTVKNADRIIVMEKGKI 215
Cdd:cd03246 119 VLDEPNSHLDVEGERALNQAiaALKA-AGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
1-198 |
4.34e-56 |
|
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: 187.18 E-value: 4.34e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 1 DITFRNIRFRYkPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVG 80
Cdd:TIGR02868 334 TLELRDLSAGY-PGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 81 VVLQDNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKI 160
Cdd:TIGR02868 413 VCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPI 492
|
170 180 190
....*....|....*....|....*....|....*...
1MT0_A 161 LIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRL 198
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
2-230 |
2.36e-53 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 174.88 E-value: 2.36e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNI--RFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWL---R 76
Cdd:COG1135 2 IELENLskTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 77 RQVGVVLQ-DNVLLNRSIIDNISLanP----GMSVEKViyAAKlagahdfISELREgyntIVGEQG------AGLSGGQR 145
Cdd:COG1135 82 RKIGMIFQhFNLLSSRTVAENVAL--PleiaGVPKAEI--RKR-------VAELLE----LVGLSDkadaypSQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 146 QRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHK 222
Cdd:COG1135 147 QRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGPVL 226
|
....*...
1MT0_A 223 ELLSEPES 230
Cdd:COG1135 227 DVFANPQS 234
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
2-223 |
2.40e-53 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 171.39 E-value: 2.40e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPN---WLRRQ 78
Cdd:COG2884 2 IRFENVSKRY-PGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 79 VGVVLQDNVLL-NRSIIDNISLA------NPGMSVEKVIYAAKLAG----AHDFISElregyntivgeqgagLSGGQRQR 147
Cdd:COG2884 81 IGVVFQDFRLLpDRTVYENVALPlrvtgkSRKEIRRRVREVLDLVGlsdkAKALPHE---------------LSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1MT0_A 148 IAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK-GRTVIIIAHRLSTVKNAD-RIIVMEKGKIVEQGKHKE 223
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRrGTTVLIATHDLELVDRMPkRVLELEDGRLVRDEARGV 223
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
2-230 |
3.30e-53 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 171.72 E-value: 3.30e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLAL--ADPNWLRRQV 79
Cdd:COG1126 2 IEIENLHKSF--GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDskKDINKLRRKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 80 GVVLQD-NVLLNRSIIDNISLAnP----GMSVEKviyAAKLAgahdfISELREgyntiVG--EQG----AGLSGGQRQRI 148
Cdd:COG1126 80 GMVFQQfNLFPHLTVLENVTLA-PikvkKMSKAE---AEERA-----MELLER-----VGlaDKAdaypAQLSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 149 AIARALVNNPKILIFDEATSALDYE--SEhV--IMRNMHKicKGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKE 223
Cdd:COG1126 146 AIARALAMEPKVMLFDEPTSALDPElvGE-VldVMRDLAK--EGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEE 222
|
....*..
1MT0_A 224 LLSEPES 230
Cdd:COG1126 223 FFENPQH 229
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-231 |
4.65e-53 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 178.56 E-value: 4.65e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRfYIPEN----GQVLIDGHDLALADPNWLRR 77
Cdd:COG1123 5 LEVRDLSVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPHGgrisGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 78 QVGVVLQD--NVLLNRSIIDNI--SLANPGMSVEKVIYAAKLAGAHDFISELREGYNtivgeqgAGLSGGQRQRIAIARA 153
Cdd:COG1123 84 RIGMVFQDpmTQLNPVTVGDQIaeALENLGLSRAEARARVLELLEAVGLERRLDRYP-------HQLSGGQRQRVAIAMA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 154 LVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLSEPES 230
Cdd:COG1123 157 LALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
.
1MT0_A 231 L 231
Cdd:COG1123 237 L 237
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-235 |
5.17e-53 |
|
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: 171.32 E-value: 5.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADP---NWLRRQ 78
Cdd:COG1127 6 IEVRNLTKSF--GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEkelYELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 79 VGVVLQDNVLL-NRSIIDNISLA---NPGMS-------VEKVIYAAKLAGAHD-FISElregyntivgeqgagLSGGQRQ 146
Cdd:COG1127 84 IGMLFQGGALFdSLTVFENVAFPlreHTDLSeaeirelVLEKLELVGLPGAADkMPSE---------------LSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 147 RIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKE 223
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEE 228
|
250
....*....|...
1MT0_A 224 LL-SEPESLYSYL 235
Cdd:COG1127 229 LLaSDDPWVRQFL 241
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-215 |
1.14e-52 |
|
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: 169.59 E-value: 1.14e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSP--VILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWL---- 75
Cdd:cd03255 1 IELKNLSKTYGGGGEkvQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 76 RRQVGVVLQDNVLLNR-SIIDNISLAnpgMSVEKVIYAAKLAGAHDFISE--LREGYNTIVGEqgagLSGGQRQRIAIAR 152
Cdd:cd03255 81 RRHIGFVFQSFNLLPDlTALENVELP---LLLAGVPKKERRERAEELLERvgLGDRLNHYPSE----LSGGQQQRVAIAR 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
1MT0_A 153 ALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKNADRIIVMEKGKI 215
Cdd:cd03255 154 ALANDPKIILADEPTGNLDSETGKEVMELLRELNKeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-219 |
3.81e-52 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 167.10 E-value: 3.81e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNwLRRQVGV 81
Cdd:cd03247 1 LSINNVSFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLISV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLNRSIIDNIslanpgmsvekviyaaklagahdfiselregyntivgeqGAGLSGGQRQRIAIARALVNNPKIL 161
Cdd:cd03247 80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
1MT0_A 162 IFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQG 219
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-233 |
8.64e-52 |
|
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: 168.44 E-value: 8.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 6 NIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGVVLQD 85
Cdd:COG1124 8 SVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRVQMVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 86 NVLlnrsiidniSLaNPGMSVEKVI----YAAKLAGAHDFISELREgyntIVG----------EQgagLSGGQRQRIAIA 151
Cdd:COG1124 88 PYA---------SL-HPRHTVDRILaeplRIHGLPDREERIAELLE----QVGlppsfldrypHQ---LSGGQRQRVAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 152 RALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLSEP 228
Cdd:COG1124 151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREerGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLAGP 230
|
....*
1MT0_A 229 ESLYS 233
Cdd:COG1124 231 KHPYT 235
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-218 |
1.00e-51 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 167.53 E-value: 1.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSP--VILDNINLSIKQGEVIGIVGRSGSGKSTLTKLI---QRfyiPENGQVLIDGHDLALADPN--- 73
Cdd:COG1136 5 LELRNLTKSYGTGEGevTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILgglDR---PTSGEVLIDGQDISSLSERela 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 74 WLRRQ-VGVVLQD-NVLLNRSIIDNISLA------NPGMSVEKVIYAAKLAG----AHDFISELregyntivgeqgaglS 141
Cdd:COG1136 82 RLRRRhIGFVFQFfNLLPELTALENVALPlllagvSRKERRERARELLERVGlgdrLDHRPSQL---------------S 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1MT0_A 142 GGQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKNADRIIVMEKGKIVEQ 218
Cdd:COG1136 147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRelGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-224 |
6.61e-51 |
|
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: 165.43 E-value: 6.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSpvILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFY-----IPENGQVLIDGHDLAL--ADPNW 74
Cdd:cd03260 1 IELRDLNVYYGDKH--ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDldVDVLE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 75 LRRQVGVVLQDNVLLNRSIIDNISlanpgmsvekviYAAKLAGAHDfiselREGYNTIVGE---------------QGAG 139
Cdd:cd03260 79 LRRRVGMVFQKPNPFPGSIYDNVA------------YGLRLHGIKL-----KEELDERVEEalrkaalwdevkdrlHALG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 140 LSGGQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQ 218
Cdd:cd03260 142 LSGGQQQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEF 221
|
....*.
1MT0_A 219 GKHKEL 224
Cdd:cd03260 222 GPTEQI 227
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-227 |
2.08e-50 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 164.47 E-value: 2.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDspVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLAlADPNWLRRQVGV 81
Cdd:COG1131 1 IEVRGLTKRYGDK--TALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA-RDPAEVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLnrsiidnislanPGMSVEKVI-YAAKLAG-----AHDFISE------LREGYNTIVGEqgagLSGGQRQRIA 149
Cdd:COG1131 78 VPQEPALY------------PDLTVRENLrFFARLYGlprkeARERIDEllelfgLTDAADRKVGT----LSGGMKQRLG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 150 IARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK-GRTVIIIAHRLSTV-KNADRIIVMEKGKIVEQGKHKELLSE 227
Cdd:COG1131 142 LALALLHDPELLILDEPTSGLDPEARRELWELLRELAAeGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-231 |
1.43e-49 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 163.24 E-value: 1.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGV 81
Cdd:PRK13632 8 IKVENVSFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQ--DNVLLNRSIIDNI--SLANPGMSVEK---VIY-AAKLAGAHDFISelREGYNtivgeqgagLSGGQRQRIAIARA 153
Cdd:PRK13632 88 IFQnpDNQFIGATVEDDIafGLENKKVPPKKmkdIIDdLAKKVGMEDYLD--KEPQN---------LSGGQKQRVAIASV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 154 LVNNPKILIFDEATSALDYESEHVIMRNMHKICKGR--TVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEPESL 231
Cdd:PRK13632 157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEIL 236
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-214 |
1.97e-49 |
|
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: 159.33 E-value: 1.97e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 3 TFRNIRFRYKpdSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGVV 82
Cdd:cd00267 1 EIENLSFRYG--GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 83 LQdnvllnrsiidnislanpgmsvekviyaaklagahdfiselregyntivgeqgagLSGGQRQRIAIARALVNNPKILI 162
Cdd:cd00267 79 PQ-------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
1MT0_A 163 FDEATSALDYESEHVIMRNMHKIC-KGRTVIIIAHRLSTVKNA-DRIIVMEKGK 214
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAeEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-168 |
2.27e-49 |
|
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: 158.97 E-value: 2.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGVVLQDNVLLNRSII-DNI 97
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVrENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1MT0_A 98 SLanpGMSVEKVIYAAKLAGAHDFISELREGY--NTIVGEQGAGLSGGQRQRIAIARALVNNPKILIFDEATS 168
Cdd:pfam00005 81 RL---GLLLKGLSKREKDARAEEALEKLGLGDlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
2-228 |
3.29e-49 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 164.59 E-value: 3.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPVI--LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWL---R 76
Cdd:PRK11153 2 IELKNISKVFPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 77 RQVGVVLQD-NVLLNRSIIDNISLanP----GMSVEKViyAAK------LAGahdfISELREGYNtivgeqgAGLSGGQR 145
Cdd:PRK11153 82 RQIGMIFQHfNLLSSRTVFDNVAL--PlelaGTPKAEI--KARvtelleLVG----LSDKADRYP-------AQLSGGQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 146 QRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHK 222
Cdd:PRK11153 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGTVS 226
|
....*.
1MT0_A 223 ELLSEP 228
Cdd:PRK11153 227 EVFSHP 232
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-216 |
6.23e-49 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 160.99 E-value: 6.23e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWL---RRQ 78
Cdd:COG3638 3 LELRNLSKRY-PGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALrrlRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 79 VGVVLQDNVLLNR-SIIDNI---SLANPGM--SVEKVIYAAKLAGAHDFISElregyntiVG-----EQGAG-LSGGQRQ 146
Cdd:COG3638 82 IGMIFQQFNLVPRlSVLTNVlagRLGRTSTwrSLLGLFPPEDRERALEALER--------VGladkaYQRADqLSGGQQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1MT0_A 147 RIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKN-ADRIIVMEKGKIV 216
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRyADRIIGLRDGRVV 226
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-215 |
1.25e-48 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 158.83 E-value: 1.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGV 81
Cdd:COG4619 1 LELEGLSFRV--GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLNRSIIDNI----SLANPGMSVEKviyaaklagAHDFISELreGYNTIVGEQGAG-LSGGQRQRIAIARALVN 156
Cdd:COG4619 79 VPQEPALWGGTVRDNLpfpfQLRERKFDRER---------ALELLERL--GLPPDILDKPVErLSGGERQRLALIRALLL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1MT0_A 157 NPKILIFDEATSALDYES----EHVIMRNMHKicKGRTVIIIAH------RLstvknADRIIVMEKGKI 215
Cdd:COG4619 148 QPDVLLLDEPTSALDPENtrrvEELLREYLAE--EGRAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
2-217 |
1.58e-48 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 160.26 E-value: 1.58e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRY--KPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPnwlrrQV 79
Cdd:COG1116 8 LELRGVSKRFptGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP-----DR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 80 GVVLQDNVLLN-RSIIDNISLanpGMSVEKVIYAAKLAGAHDFISElregyntiVGEQGAG------LSGGQRQRIAIAR 152
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVAL---GLELRGVPKAERRERARELLEL--------VGLAGFEdayphqLSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1MT0_A 153 ALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAH------RLstvknADRIIVMEK--GKIVE 217
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLWQetGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
2-227 |
2.27e-48 |
|
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: 159.82 E-value: 2.27e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGV 81
Cdd:COG1120 2 LEAENLSVGY--GGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVllnrsiidnislANPGMSVEKVI------YAAKLA--GAHDF-----------ISELRE-GYNTivgeqgagLS 141
Cdd:COG1120 80 VPQEPP------------APFGLTVRELValgrypHLGLFGrpSAEDReaveealertgLEHLADrPVDE--------LS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 142 GGQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLstvkN-----ADRIIVMEKGK 214
Cdd:COG1120 140 GGERQRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARerGRTVVMVLHDL----NlaaryADRLVLLKDGR 215
|
250
....*....|...
1MT0_A 215 IVEQGKHKELLSE 227
Cdd:COG1120 216 IVAQGPPEEVLTP 228
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
2-238 |
2.44e-48 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 159.25 E-value: 2.44e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKpdSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLAlADPNWLRRQVGV 81
Cdd:COG4555 2 IEVENLSKKYG--KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR-KEPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVL-LNRSIIDNISLANP--GMSVEKVIYAAKlagahDFIS--ELREGYNTIVGEqgagLSGGQRQRIAIARALVN 156
Cdd:COG4555 79 LPDERGLyDRLTVRENIRYFAElyGLFDEELKKRIE-----ELIEllGLEEFLDRRVGE----LSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 157 NPKILIFDEATSALDYESEHVIMRNMHKICK-GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLSE--PESLY 232
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREILRALKKeGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEigEENLE 229
|
....*.
1MT0_A 233 SYLYQL 238
Cdd:COG4555 230 DAFVAL 235
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-218 |
4.32e-48 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 158.02 E-value: 4.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSP--VILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGhdLALADPNwlrRQV 79
Cdd:cd03293 1 LEVRNVSKTYGGGGGavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG--EPVTGPG---PDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 80 GVVLQDNVLLN-RSIIDNISLanpGMSVEKVIYAAKLAGAHDFISElregyntiVGEQGAG------LSGGQRQRIAIAR 152
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVAL---GLELQGVPKAEARERAEELLEL--------VGLSGFEnayphqLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1MT0_A 153 ALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLS-TVKNADRIIVMEK--GKIVEQ 218
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRetGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-214 |
1.00e-47 |
|
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: 155.42 E-value: 1.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKpdSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNW--LRRQV 79
Cdd:cd03229 1 LELKNVSKRYG--QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 80 GVVLQDNVLLNR-SIIDNISLanpgmsvekviyaaklagahdfiselregyntivgeqgaGLSGGQRQRIAIARALVNNP 158
Cdd:cd03229 79 GMVFQDFALFPHlTVLENIAL---------------------------------------GLSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
1MT0_A 159 KILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKN-ADRIIVMEKGK 214
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKSLQAqlGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-217 |
2.76e-47 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 167.51 E-value: 2.76e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPV-ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLI-DGHDLALADPNWLRRQV 79
Cdd:PTZ00265 383 IQFKNVRFHYDTRKDVeIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 80 GVVLQDNVLLNRSIIDNIS-------------------------------------------LANPGMSVE--------- 107
Cdd:PTZ00265 463 GVVSQDPLLFSNSIKNNIKyslyslkdlealsnyynedgndsqenknkrnscrakcagdlndMSNTTDSNEliemrknyq 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 108 -----KVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNM 182
Cdd:PTZ00265 543 tikdsEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
250 260 270 280
....*....|....*....|....*....|....*....|.
1MT0_A 183 HKIcKG---RTVIIIAHRLSTVKNADRIIVM---EKGKIVE 217
Cdd:PTZ00265 623 NNL-KGnenRITIIIAHRLSTIRYANTIFVLsnrERGSTVD 662
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-224 |
2.99e-47 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 156.12 E-value: 2.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWL---RRQ 78
Cdd:cd03261 1 IELRGLTKSF--GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 79 VGVVLQDNVLLNR-SIIDNISLA-------NPGMSVEKVIYAAKLAGahdfiseLREGYNTIVGEqgagLSGGQRQRIAI 150
Cdd:cd03261 79 MGMLFQSGALFDSlTVFENVAFPlrehtrlSEEEIREIVLEKLEAVG-------LRGAEDLYPAE----LSGGMKKRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1MT0_A 151 ARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTV-KNADRIIVMEKGKIVEQGKHKEL 224
Cdd:cd03261 148 ARALALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKelGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-233 |
1.42e-46 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 165.50 E-value: 1.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGV 81
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITI 1364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLNRSIIDNIslaNP--GMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPK 159
Cdd:TIGR00957 1365 IPQDPVLFSGSLRMNL---DPfsQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTK 1441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1MT0_A 160 ILIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEPESLYS 233
Cdd:TIGR00957 1442 ILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYS 1515
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-219 |
1.45e-46 |
|
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: 152.59 E-value: 1.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 5 RNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGVVLQ 84
Cdd:cd03214 3 ENLSVGY--GGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 85 dnvllnrsiidnislanpgmsvekviyAAKLAGAHDFiseLREGYNTivgeqgagLSGGQRQRIAIARALVNNPKILIFD 164
Cdd:cd03214 81 ---------------------------ALELLGLAHL---ADRPFNE--------LSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
1MT0_A 165 EATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLS-TVKNADRIIVMEKGKIVEQG 219
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRLARerGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-228 |
2.48e-46 |
|
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: 156.37 E-value: 2.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 5 RNIRFRYKPDSPVI--LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFyIPEN----GQVLIDGHDLALADPNWLR-- 76
Cdd:COG0444 5 RNLKVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGL-LPPPgitsGEILFDGEDLLKLSEKELRki 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 77 --RQVGVVLQD--NVLlnrsiidnislaNPGMSVEKVIyaAKLAGAHDFISElREGYNTI------VGEQGAG------- 139
Cdd:COG0444 84 rgREIQMIFQDpmTSL------------NPVMTVGDQI--AEPLRIHGGLSK-AEARERAiellerVGLPDPErrldryp 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 140 --LSGGQRQRIAIARALVNNPKILIFDEATSALDyesehV-----IMRNMHKICK--GRTVIIIAHRLSTVKN-ADRIIV 209
Cdd:COG0444 149 heLSGGMRQRVMIARALALEPKLLIADEPTTALD-----VtiqaqILNLLKDLQRelGLAILFITHDLGVVAEiADRVAV 223
|
250
....*....|....*....
1MT0_A 210 MEKGKIVEQGKHKELLSEP 228
Cdd:COG0444 224 MYAGRIVEEGPVEELFENP 242
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-219 |
1.13e-45 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 151.52 E-value: 1.13e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDspVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNwlRRQVGV 81
Cdd:cd03259 1 LELKGLSKTYGSV--RALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLL-NRSIIDNIS--LANPGMS----VEKVIYAAKLAGahdfISELREGYNtivgeqgAGLSGGQRQRIAIARAL 154
Cdd:cd03259 77 VFQDYALFpHLTVAENIAfgLKLRGVPkaeiRARVRELLELVG----LEGLLNRYP-------HELSGGQQQRVALARAL 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1MT0_A 155 VNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLS-TVKNADRIIVMEKGKIVEQG 219
Cdd:cd03259 146 AREPSLLLLDEPLSALDAKLREELREELKELQRelGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-215 |
1.66e-45 |
|
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: 151.14 E-value: 1.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDspVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNW--LRRQV 79
Cdd:cd03262 1 IEIKNLHKSFGDF--HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNIneLRQKV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 80 GVVLQD-NVLLNRSIIDNISLAnPgMSVEKVIYAAKLAGAHDF-----ISELREGYNtivgeqgAGLSGGQRQRIAIARA 153
Cdd:cd03262 79 GMVFQQfNLFPHLTVLENITLA-P-IKVKGMSKAEAEERALELlekvgLADKADAYP-------AQLSGGQQQRVAIARA 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1MT0_A 154 LVNNPKILIFDEATSALDYE-SEHV--IMRNMHKicKGRTVIIIAHRLSTVKN-ADRIIVMEKGKI 215
Cdd:cd03262 150 LAMNPKVMLFDEPTSALDPElVGEVldVMKDLAE--EGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-228 |
2.90e-45 |
|
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: 151.30 E-value: 2.90e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPViLDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGV 81
Cdd:cd03295 1 IEFENVTKRYGGGKKA-VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLL-NRSIIDNISLAnpgMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKI 160
Cdd:cd03295 80 VIQQIGLFpHMTVEENIALV---PKLLKWPKEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1MT0_A 161 LIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRL-STVKNADRIIVMEKGKIVEQGKHKELLSEP 228
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-215 |
4.59e-45 |
|
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: 148.70 E-value: 4.59e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKpdSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLAlADPNWLRRQVGV 81
Cdd:cd03230 1 IEVRNLSKRYG--KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK-KEPEEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLnrsiidnislanPGMSVEKVIYaaklagahdfiselregyntivgeqgagLSGGQRQRIAIARALVNNPKIL 161
Cdd:cd03230 78 LPEEPSLY------------ENLTVRENLK----------------------------LSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
1MT0_A 162 IFDEATSALDYESEHVIMRNMHKICK-GRTVIIIAHRLSTVKN-ADRIIVMEKGKI 215
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKeGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-232 |
7.01e-45 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 153.33 E-value: 7.01e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 1 DITFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNwlRRQVG 80
Cdd:COG3842 5 ALELENVSKRY--GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 81 VVLQDNVLL-NRSIIDNI--SLANPGMS-------VEKVIYAAKLAG-AHDFISElregyntivgeqgagLSGGQRQRIA 149
Cdd:COG3842 81 MVFQDYALFpHLTVAENVafGLRMRGVPkaeirarVAELLELVGLEGlADRYPHQ---------------LSGGQQQRVA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 150 IARALVNNPKILIFDEATSALDYES-EHVI--MRNMHKIcKGRTVIIIAHRLS---TVknADRIIVMEKGKIVEQGKHKE 223
Cdd:COG3842 146 LARALAPEPRVLLLDEPLSALDAKLrEEMReeLRRLQRE-LGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEE 222
|
....*....
1MT0_A 224 LLSEPESLY 232
Cdd:COG3842 223 IYERPATRF 231
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-224 |
8.26e-45 |
|
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: 150.03 E-value: 8.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWL---RRQ 78
Cdd:cd03256 1 IEVENLSKTY-PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqlRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 79 VGVVLQDNVLLNR-SIIDNI------------SLAN--PGMSVEKVIYAAKLAGahdfiseLREGYNTIVGEqgagLSGG 143
Cdd:cd03256 80 IGMIFQQFNLIERlSVLENVlsgrlgrrstwrSLFGlfPKEEKQRALAALERVG-------LLDKAYQRADQ----LSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 144 QRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKIC--KGRTVIIIAHRLSTVK-NADRIIVMEKGKIVEQGK 220
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINreEGITVIVSLHQVDLAReYADRIVGLKDGRIVFDGP 228
|
....
1MT0_A 221 HKEL 224
Cdd:cd03256 229 PAEL 232
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-231 |
2.28e-44 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 150.17 E-value: 2.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGhdLALADPN-W-LRRQV 79
Cdd:PRK13635 6 IRVEHISFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG--MVLSEETvWdVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 80 GVVLQ--DNVLLNRSIIDNI--SLANPGMS----VEKVIYAAKLAGAHDFIseLREgyntivgeqGAGLSGGQRQRIAIA 151
Cdd:PRK13635 84 GMVFQnpDNQFVGATVQDDVafGLENIGVPreemVERVDQALRQVGMEDFL--NRE---------PHRLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 152 RALVNNPKILIFDEATSALDYESEHVIMRNMHKIC--KGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEPE 229
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLKeqKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSGH 232
|
..
1MT0_A 230 SL 231
Cdd:PRK13635 233 ML 234
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
2-230 |
3.12e-44 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 148.70 E-value: 3.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDspVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGhdLALADPN----WLRR 77
Cdd:PRK09493 2 IEFKNVSKHFGPT--QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKvderLIRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 78 QVGVVLQDNVLLnrsiidnislanPGMS-VEKVIYA------AKLAGAHDFISEL--REGYNTIVGEQGAGLSGGQRQRI 148
Cdd:PRK09493 78 EAGMVFQQFYLF------------PHLTaLENVMFGplrvrgASKEEAEKQARELlaKVGLAERAHHYPSELSGGQQQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 149 AIARALVNNPKILIFDEATSALDYESEHVIMRNMHKIC-KGRTVIIIAHRLSTV-KNADRIIVMEKGKIVEQGKHKELLS 226
Cdd:PRK09493 146 AIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAeEGMTMVIVTHEIGFAeKVASRLIFIDKGRIAEDGDPQVLIK 225
|
....
1MT0_A 227 EPES 230
Cdd:PRK09493 226 NPPS 229
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-215 |
3.55e-44 |
|
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: 147.94 E-value: 3.55e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPViLDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPN---WLRRQ 78
Cdd:cd03292 1 IEFINVTKTYPNGTAA-LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 79 VGVVLQDNVLL-NRSIIDNISLA------NPGMSVEKVIYAAKLAGAHDFISELregyntivgeqGAGLSGGQRQRIAIA 151
Cdd:cd03292 80 IGVVFQDFRLLpDRNVYENVAFAlevtgvPPREIRKRVPAALELVGLSHKHRAL-----------PAELSGGEQQRVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1MT0_A 152 RALVNNPKILIFDEATSALDYESEHVIMRNMHKICK-GRTVIIIAHRLSTVKN-ADRIIVMEKGKI 215
Cdd:cd03292 149 RAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKaGTTVVVATHAKELVDTtRHRVIALERGKL 214
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-237 |
5.32e-44 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 157.98 E-value: 5.32e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLA---LADpnwLRRQ 78
Cdd:PLN03130 1238 IKFEDVVLRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISkfgLMD---LRKV 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 79 VGVVLQDNVLLNRSIIDNISLANPGMSVEkvIYAAkLAGAH--DFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVN 156
Cdd:PLN03130 1315 LGIIPQAPVLFSGTVRFNLDPFNEHNDAD--LWES-LERAHlkDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLR 1391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 157 NPKILIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEPESLYSYLY 236
Cdd:PLN03130 1392 RSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFSKMV 1471
|
.
1MT0_A 237 Q 237
Cdd:PLN03130 1472 Q 1472
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
2-231 |
7.15e-44 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 149.11 E-value: 7.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSP-VILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLAlADPNW-LRRQV 79
Cdd:PRK13650 5 IEVKNLTFKYKEDQEkYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT-EENVWdIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 80 GVVLQ--DNVLLNRSIIDNIS--LANPGMS----VEKVIYAAKLAGAHDFisELREgyntivgeqGAGLSGGQRQRIAIA 151
Cdd:PRK13650 84 GMVFQnpDNQFVGATVEDDVAfgLENKGIPheemKERVNEALELVGMQDF--KERE---------PARLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 152 RALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEPE 229
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGN 232
|
..
1MT0_A 230 SL 231
Cdd:PRK13650 233 DL 234
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
2-219 |
2.91e-43 |
|
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: 144.62 E-value: 2.91e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPV----ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLI--QRFYIPENGQVLIDGHDLalaDPNWL 75
Cdd:cd03213 4 LSFRNLTVTVKSSPSKsgkqLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKRSF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 76 RRQVGVVLQDNVLLnrsiidnislanPGMSVEKVIYaaklagahdFISELRegyntivgeqgaGLSGGQRQRIAIARALV 155
Cdd:cd03213 81 RKIIGYVPQDDILH------------PTLTVRETLM---------FAAKLR------------GLSGGERKRVSIALELV 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1MT0_A 156 NNPKILIFDEATSALDYESEHVIMRNMHKICK-GRTVIIIAHRLST--VKNADRIIVMEKGKIVEQG 219
Cdd:cd03213 128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-232 |
3.13e-43 |
|
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: 145.84 E-value: 3.13e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNwlRRQVGV 81
Cdd:cd03300 1 IELENVSKFY--GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLNR-SIIDNISLanpGMSVEKVIYAAKLAGAHDFISELR-EGYNTIVGEQgagLSGGQRQRIAIARALVNNPK 159
Cdd:cd03300 77 VFQNYALFPHlTVFENIAF---GLRLKKLPKAEIKERVAEALDLVQlEGYANRKPSQ---LSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1MT0_A 160 ILIFDEATSALDY---ESEHVIMRNMHKICkGRTVIIIAHRLS---TVknADRIIVMEKGKIVEQGKHKELLSEPESLY 232
Cdd:cd03300 151 VLLLDEPLGALDLklrKDMQLELKRLQKEL-GITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGTPEEIYEEPANRF 226
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
2-238 |
4.45e-43 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 155.57 E-value: 4.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRY--KPDSPvILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFY-------------------------- 53
Cdd:PTZ00265 1166 IEIMDVNFRYisRPNVP-IYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYdlkndhhivfknehtndmtneqdyqg 1244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 54 ----------------------------IPENGQVLIDGHDLALADPNWLRRQVGVVLQDNVLLNRSIIDNISLANPGMS 105
Cdd:PTZ00265 1245 deeqnvgmknvnefsltkeggsgedstvFKNSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDAT 1324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 106 VEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKI 185
Cdd:PTZ00265 1325 REDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDI 1404
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 186 CK--GRTVIIIAHRLSTVKNADRIIVMEK----GKIVE-QGKHKELLSEPESLYSYLYQL 238
Cdd:PTZ00265 1405 KDkaDKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLSVQDGVYKKYVKL 1464
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-228 |
6.27e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 145.23 E-value: 6.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALAdpnwlRRQVGV 81
Cdd:COG1121 7 IELENLTVSY--GGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQ-------------DNVLLNRSiidnislanPGMSV---------EKVIYAAKLAGAHDFISELregyntiVGEqgag 139
Cdd:COG1121 80 VPQraevdwdfpitvrDVVLMGRY---------GRRGLfrrpsradrEAVDEALERVGLEDLADRP-------IGE---- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 140 LSGGQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK-GRTVIIIAHRLSTV-KNADRIIVMEKGkIVE 217
Cdd:COG1121 140 LSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRReGKTILVVTHDLGAVrEYFDRVLLLNRG-LVA 218
|
250
....*....|.
1MT0_A 218 QGKHKELLSEP 228
Cdd:COG1121 219 HGPPEEVLTPE 229
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-228 |
7.94e-43 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 147.57 E-value: 7.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPN---WLRRQVGVVLQDnvllnrsiid 95
Cdd:COG4608 34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRelrPLRRRMQMVFQD---------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 96 niSLA--NPGMSVEkviyaaklagahDFISE-LRegYNTIVGEQGA-----------GL------------SGGQRQRIA 149
Cdd:COG4608 104 --PYAslNPRMTVG------------DIIAEpLR--IHGLASKAERrervaellelvGLrpehadryphefSGGQRQRIG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 150 IARALVNNPKILIFDEATSALDYESEHVIM-------RNMhkickGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKH 221
Cdd:COG4608 168 IARALALNPKLIVCDEPVSALDVSIQAQVLnlledlqDEL-----GLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPR 242
|
....*..
1MT0_A 222 KELLSEP 228
Cdd:COG4608 243 DELYARP 249
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-214 |
4.06e-42 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 142.22 E-value: 4.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPD---SPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHdlaladpnwlrrq 78
Cdd:cd03250 1 ISVEDASFTWDSGeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 79 VGVVLQDNVLLNRSIIDNISLANP--GMSVEKVIYAAKLagaHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVN 156
Cdd:cd03250 68 IAYVSQEPWIQNGTIRENILFGKPfdEERYEKVIKACAL---EPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 157 NPKILIFDEATSALDYESEHVIMRN--MHKICKGRTVIIIAHRLSTVKNADRIIVMEKGK 214
Cdd:cd03250 145 DADIYLLDDPLSAVDAHVGRHIFENciLGLLLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
9-232 |
4.83e-42 |
|
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: 149.45 E-value: 4.83e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 9 FRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFyIPENGQVLIDGHDLALADPNW---LRRQVGVVLQD 85
Cdd:COG4172 292 FRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRAlrpLRRRMQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 86 nvllnrsiiDNISLaNPGMSVEKVI------YAAKLAGA--HDFISE-LREgyntiVGEQGAGL-------SGGQRQRIA 149
Cdd:COG4172 371 ---------PFGSL-SPRMTVGQIIaeglrvHGPGLSAAerRARVAEaLEE-----VGLDPAARhryphefSGGQRQRIA 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 150 IARALVNNPKILIFDEATSALDyesehvimrnmhkickgRTV-------------------IIIAHRLSTVKN-ADRIIV 209
Cdd:COG4172 436 IARALILEPKLLVLDEPTSALD-----------------VSVqaqildllrdlqrehglayLFISHDLAVVRAlAHRVMV 498
|
250 260
....*....|....*....|...
1MT0_A 210 MEKGKIVEQGKHKELLSEPESLY 232
Cdd:COG4172 499 MKDGKVVEQGPTEQVFDAPQHPY 521
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
2-228 |
5.95e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 143.97 E-value: 5.95e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDlaLADPNWL---RRQ 78
Cdd:PRK13644 2 IRLENVSYSY-PDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID--TGDFSKLqgiRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 79 VGVVLQ--DNVLLNRSIIDNISLANPGMSVEKViyaaklagahdfisELREGYNTIVGEQGAG---------LSGGQRQR 147
Cdd:PRK13644 79 VGIVFQnpETQFVGRTVEEDLAFGPENLCLPPI--------------EIRKRVDRALAEIGLEkyrhrspktLSGGQGQC 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 148 IAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKIC-KGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLS 226
Cdd:PRK13644 145 VALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHeKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
..
1MT0_A 227 EP 228
Cdd:PRK13644 225 DV 226
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-232 |
1.53e-41 |
|
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: 142.78 E-value: 1.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 21 NINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWL----RRQVGVVLQDNVLL-NRSIID 95
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelrRKKISMVFQSFALLpHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 96 NISLanpGMSV---------EKVIYAAKLAGAHDFISELregyntiVGEqgagLSGGQRQRIAIARALVNNPKILIFDEA 166
Cdd:cd03294 122 NVAF---GLEVqgvpraereERAAEALELVGLEGWEHKY-------PDE----LSGGMQQRVGLARALAVDPDILLMDEA 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1MT0_A 167 TSALD----YESEHVIMRNMHKIckGRTVIIIAHRLS-TVKNADRIIVMEKGKIVEQGKHKELLSEPESLY 232
Cdd:cd03294 188 FSALDplirREMQDELLRLQAEL--QKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTNPANDY 256
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-229 |
6.24e-41 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 140.56 E-value: 6.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFY--IPEN---GQVLIDGHDL--ALADPNW 74
Cdd:COG1117 12 IEVRNLNVYY--GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNdlIPGArveGEILLDGEDIydPDVDVVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 75 LRRQVGVVLQDNVLLNRSIIDNislanpgmsvekVIYAAKLAGAHDfISELREgyntIV-----------------GEQG 137
Cdd:COG1117 90 LRRRVGMVFQKPNPFPKSIYDN------------VAYGLRLHGIKS-KSELDE----IVeeslrkaalwdevkdrlKKSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 138 AGLSGGQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAH------RLStvknaDRIIVME 211
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHnmqqaaRVS-----DYTAFFY 227
|
250
....*....|....*...
1MT0_A 212 KGKIVEQGKHKELLSEPE 229
Cdd:COG1117 228 LGELVEFGPTEQIFTNPK 245
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-234 |
1.19e-40 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 142.21 E-value: 1.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALadpnWL---RRQ 78
Cdd:COG1118 3 IEVRNISKRF--GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT----NLpprERR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 79 VGVVLQDNVLL-NRSIIDNISLanpGMSVEKVIYAAKLAGAHDFISELR-EGYntivgeqgAG-----LSGGQRQRIAIA 151
Cdd:COG1118 77 VGFVFQHYALFpHMTVAENIAF---GLRVRPPSKAEIRARVEELLELVQlEGL--------ADrypsqLSGGQRQRVALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 152 RALVNNPKILIFDEATSALDyesEHV------IMRNMHKICkGRTVIIIAH------RLstvknADRIIVMEKGKIVEQG 219
Cdd:COG1118 146 RALAVEPEVLLLDEPFGALD---AKVrkelrrWLRRLHDEL-GGTTVFVTHdqeealEL-----ADRVVVMNQGRIEQVG 216
|
250
....*....|....*
1MT0_A 220 KHKELLSEPESLYSY 234
Cdd:COG1118 217 TPDEVYDRPATPFVA 231
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-237 |
4.34e-40 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 146.66 E-value: 4.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGV 81
Cdd:PLN03232 1235 IKFEDVHLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSI 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLNRSI---IDNISLANPGMSVEkviyAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNP 158
Cdd:PLN03232 1315 IPQSPVLFSGTVrfnIDPFSEHNDADLWE----ALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRS 1390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1MT0_A 159 KILIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEPESLYSYLYQ 237
Cdd:PLN03232 1391 KILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVH 1469
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
2-231 |
1.52e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 137.91 E-value: 1.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPD----SPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNW-LR 76
Cdd:PRK13633 5 IKCKNVSYKYESNeestEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdIR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 77 RQVGVVLQ--DNVLLNRSIIDNISLANPGMSV------EKVIYAAKLAGahdfISELREGYNTIvgeqgagLSGGQRQRI 148
Cdd:PRK13633 85 NKAGMVFQnpDNQIVATIVEEDVAFGPENLGIppeeirERVDESLKKVG----MYEYRRHAPHL-------LSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 149 AIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLS 226
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233
|
....*
1MT0_A 227 EPESL 231
Cdd:PRK13633 234 EVEMM 238
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
19-230 |
2.92e-39 |
|
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: 135.54 E-value: 2.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNwlRRQVGVVLQDNVLL-NRSIIDNI 97
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 98 SLanpGMSVEKVIYAAKLAGAHDfISELReGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKILIFDEATSALDYESEHV 177
Cdd:cd03299 93 AY---GLKKRKVDKKEIERKVLE-IAEML-GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
1MT0_A 178 IMRNMHKICK--GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLSEPES 230
Cdd:cd03299 168 LREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKPKN 223
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
2-235 |
5.45e-39 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 134.88 E-value: 5.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkPDSPVildNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNwlRRQVGV 81
Cdd:COG3840 2 LRLDDLTYRY-GDFPL---RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--ERPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLNR-SIIDNISLA-NPGMSV-----EKVIYAAKLAGAHDFISELregyntivgeqGAGLSGGQRQRIAIARAL 154
Cdd:COG3840 76 LFQENNLFPHlTVAQNIGLGlRPGLKLtaeqrAQVEQALERVGLAGLLDRL-----------PGQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 155 VNNPKILIFDEATSALD----YEsehviMRNM-HKICK--GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLS 226
Cdd:COG3840 145 VRKRPILLLDEPFSALDpalrQE-----MLDLvDELCRerGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLD 219
|
250
....*....|.
1MT0_A 227 E--PESLYSYL 235
Cdd:COG3840 220 GepPPALAAYL 230
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
1-235 |
7.10e-39 |
|
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: 135.42 E-value: 7.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 1 DITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVG 80
Cdd:cd03288 19 EIKIHDLCVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 81 VVLQDNVLLNRSIIDNISlANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKI 160
Cdd:cd03288 99 IILQDPILFSGSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1MT0_A 161 LIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEPESLYSYL 235
Cdd:cd03288 178 LIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASL 252
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
18-226 |
4.21e-38 |
|
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: 133.78 E-value: 4.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 18 ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNW---LRRQVGVVLQDNvllnrsii 94
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQrraFRRDVQLVFQDS-------- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 95 dnISLANPGMSVEKVI-----------YAAKLAGAHDFIS--ELREgynTIVGEQGAGLSGGQRQRIAIARALVNNPKIL 161
Cdd:TIGR02769 98 --PSAVNPRMTVRQIIgeplrhltsldESEQKARIAELLDmvGLRS---EDADKLPRQLSGGQLQRINIARALAVKPKLI 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1MT0_A 162 IFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLS 226
Cdd:TIGR02769 173 VLDEAVSNLDMVLQAVILELLRKLQQafGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLS 240
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-232 |
4.90e-38 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 136.23 E-value: 4.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNwlRRQVGV 81
Cdd:PRK09452 15 VELRGISKSF--DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLnrsiidnislanPGMSV-EKVIYAAKLAG-AHDFISE-LREGYNTIVGEQGAG-----LSGGQRQRIAIARA 153
Cdd:PRK09452 91 VFQSYALF------------PHMTVfENVAFGLRMQKtPAAEITPrVMEALRMVQLEEFAQrkphqLSGGQQQRVAIARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 154 LVNNPKILIFDEATSALDYESEhVIMRNMHKICK---GRTVIIIAH----RLSTvknADRIIVMEKGKIVEQGKHKELLS 226
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLR-KQMQNELKALQrklGITFVFVTHdqeeALTM---SDRIVVMRDGRIEQDGTPREIYE 234
|
....*.
1MT0_A 227 EPESLY 232
Cdd:PRK09452 235 EPKNLF 240
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-216 |
6.59e-38 |
|
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: 129.86 E-value: 6.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkPDSPViLDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQ-VG 80
Cdd:cd03216 1 LELRGITKRF-GGVKA-LDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAgIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 81 VVLQdnvllnrsiidnislanpgmsvekviyaaklagahdfiselregyntivgeqgagLSGGQRQRIAIARALVNNPKI 160
Cdd:cd03216 79 MVYQ-------------------------------------------------------LSVGERQMVEIARALARNARL 103
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 161 LIFDEATSAL-DYESEHV--IMRNMHKicKGRTVIIIAHRLSTVKN-ADRIIVMEKGKIV 216
Cdd:cd03216 104 LILDEPTAALtPAEVERLfkVIRRLRA--QGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
2-233 |
9.26e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 133.25 E-value: 9.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSP---VILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLA-----LADpn 73
Cdd:PRK13637 3 IKIENLTHIYMEGTPfekKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvkLSD-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 74 wLRRQVGVVLQ--DNVLLNRSIIDNISLA--NPGMSVE----KVIYAAKLAGAHdfiselregYNTIVGEQGAGLSGGQR 145
Cdd:PRK13637 81 -IRKKVGLVFQypEYQLFEETIEKDIAFGpiNLGLSEEeienRVKRAMNIVGLD---------YEDYKDKSPFELSGGQK 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 146 QRIAIARALVNNPKILIFDEATSALDYESEHVIM---RNMHKIcKGRTVIIIAHRLSTV-KNADRIIVMEKGKIVEQGKH 221
Cdd:PRK13637 151 RRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILnkiKELHKE-YNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTP 229
|
250
....*....|..
1MT0_A 222 KELLSEPESLYS 233
Cdd:PRK13637 230 REVFKEVETLES 241
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-232 |
1.52e-37 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 134.43 E-value: 1.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 1 DITFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNwlRRQVG 80
Cdd:COG3839 3 SLELENVSKSY--GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 81 VVLQDNVLL-NRSIIDNIS--LANPGMS----VEKVIYAAKLAGahdfISELREGYntiVGEqgagLSGGQRQRIAIARA 153
Cdd:COG3839 79 MVFQSYALYpHMTVYENIAfpLKLRKVPkaeiDRRVREAAELLG----LEDLLDRK---PKQ----LSGGQRQRVALGRA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 154 LVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAH------RLstvknADRIIVMEKGKIVEQGKHKELL 225
Cdd:COG3839 148 LVREPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRrlGTTTIYVTHdqveamTL-----ADRIAVMNDGRIQQVGTPEELY 222
|
....*..
1MT0_A 226 SEPESLY 232
Cdd:COG3839 223 DRPANLF 229
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
2-229 |
2.06e-37 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 131.41 E-value: 2.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKpdSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADP--------N 73
Cdd:PRK11264 4 IEVKNLVKKFH--GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkgliR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 74 WLRRQVGVVLQD-NVLLNRSIIDNIsLANPgMSVEKVIYAAKLAGAHDFISELregynTIVGEQGA---GLSGGQRQRIA 149
Cdd:PRK11264 82 QLRQHVGFVFQNfNLFPHRTVLENI-IEGP-VIVKGEPKEEATARARELLAKV-----GLAGKETSyprRLSGGQQQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 150 IARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK-GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLSE 227
Cdd:PRK11264 155 IARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAD 234
|
..
1MT0_A 228 PE 229
Cdd:PRK11264 235 PQ 236
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
2-231 |
3.82e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 131.41 E-value: 3.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGV 81
Cdd:PRK13648 8 IVFKNVSFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQ--DNVLLNRSIIDNIS--LANPGMSVEKViyaaklagaHDFISELREGYNTI--VGEQGAGLSGGQRQRIAIARALV 155
Cdd:PRK13648 88 VFQnpDNQFVGSIVKYDVAfgLENHAVPYDEM---------HRRVSEALKQVDMLerADYEPNALSGGQKQRVAIAGVLA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1MT0_A 156 NNPKILIFDEATSALDYESEHVIMRNMHKI--CKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEPESL 231
Cdd:PRK13648 159 LNPSVIILDEATSMLDPDARQNLLDLVRKVksEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEEL 236
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-219 |
6.04e-37 |
|
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: 129.15 E-value: 6.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKpDSPVILDninLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNwlRRQVGV 81
Cdd:cd03298 1 VRLDKIRFSYG-EQPMHFD---LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLNR-SIIDNISLA-NPGMSV-----EKVIYAAKLAGAHDFISELREgyntivgeqgaGLSGGQRQRIAIARAL 154
Cdd:cd03298 75 LFQENNLFAHlTVEQNVGLGlSPGLKLtaedrQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVL 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1MT0_A 155 VNNPKILIFDEATSALDYESEHVIMRNMHKICKGR--TVIIIAHRLSTVKN-ADRIIVMEKGKIVEQG 219
Cdd:cd03298 144 VRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETkmTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-215 |
1.68e-36 |
|
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: 128.03 E-value: 1.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 6 NIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALAdpnwlRRQVGVVLQd 85
Cdd:cd03235 4 DLTVSY--GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVPQ- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 86 NVLLNR----SIIDNISLANPGMSV----------EKVIYAAKLAGAHDF----ISELregyntivgeqgaglSGGQRQR 147
Cdd:cd03235 76 RRSIDRdfpiSVRDVVLMGLYGHKGlfrrlskadkAKVDEALERVGLSELadrqIGEL---------------SGGQQQR 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 148 IAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKIC-KGRTVIIIAHRLSTV-KNADRIIVMEKGKI 215
Cdd:cd03235 141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRrEGMTILVVTHDLGLVlEYFDRVLLLNRTVV 210
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
1-231 |
3.27e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 129.37 E-value: 3.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 1 DITFRNIRFRYKPDSP---VILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNW--- 74
Cdd:PRK13634 2 DITFQKVEHRYQYKTPferRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKklk 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 75 -LRRQVGVVLQ--DNVLLNRSIIDNISLA--NPGMSVE----KVIYAAKLAGAHDFISElREGYNtivgeqgagLSGGQR 145
Cdd:PRK13634 82 pLRKKVGIVFQfpEHQLFEETVEKDICFGpmNFGVSEEdakqKAREMIELVGLPEELLA-RSPFE---------LSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 146 QRIAIARALVNNPKILIFDEATSALDYESEHVIMR---NMHKIcKGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKH 221
Cdd:PRK13634 152 RRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEmfyKLHKE-KGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTP 230
|
250
....*....|
1MT0_A 222 KELLSEPESL 231
Cdd:PRK13634 231 REIFADPDEL 240
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-224 |
5.78e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 132.83 E-value: 5.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQ-VGVVLQD-NVLLNRSIIDN 96
Cdd:COG1129 20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAgIAIIHQElNLVPNLSVAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 97 ISLANPGMSVEKVIYAAKLAGAHDFISELreGYN----TIVGEqgagLSGGQRQRIAIARALVNNPKILIFDEATSAL-D 171
Cdd:COG1129 100 IFLGREPRRGGLIDWRAMRRRARELLARL--GLDidpdTPVGD----LSVAQQQLVEIARALSRDARVLILDEPTASLtE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
1MT0_A 172 YESEHV--IMRNMHKicKGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKEL 224
Cdd:COG1129 174 REVERLfrIIRRLKA--QGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAEL 227
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-231 |
9.98e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 127.99 E-value: 9.98e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkPDSPV-ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPE---NGQVLIDGHDLAlADPNW-LR 76
Cdd:PRK13640 6 VEFKHVSFTY-PDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKITVDGITLT-AKTVWdIR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 77 RQVGVVLQ--DNVLLNRSIIDNIS--LANPGMSVEKVIYAAklagaHDFISELreGYNTIVGEQGAGLSGGQRQRIAIAR 152
Cdd:PRK13640 84 EKVGIVFQnpDNQFVGATVGDDVAfgLENRAVPRPEMIKIV-----RDVLADV--GMLDYIDSEPANLSGGQKQRVAIAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 153 ALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEPES 230
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFSKVEM 236
|
.
1MT0_A 231 L 231
Cdd:PRK13640 237 L 237
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
4-233 |
4.40e-35 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 132.21 E-value: 4.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 4 FRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGVVL 83
Cdd:PTZ00243 1311 FEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIP 1390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 84 QDNVLLN---RSIIDNISLANPgmsvEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKI 160
Cdd:PTZ00243 1391 QDPVLFDgtvRQNVDPFLEASS----AEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSG 1466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1MT0_A 161 LIF-DEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEPESLYS 233
Cdd:PTZ00243 1467 FILmDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIFH 1540
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-234 |
9.15e-35 |
|
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: 124.37 E-value: 9.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNwlRRQVGV 81
Cdd:cd03296 3 IEVRNVSKRF--GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLNR-SIIDNISLanpGMSVEKVIYAAKLAGAHDFISELREgyntIVGEQG------AGLSGGQRQRIAIARAL 154
Cdd:cd03296 79 VFQHYALFRHmTVFDNVAF---GLRVKPRSERPPEAEIRAKVHELLK----LVQLDWladrypAQLSGGQRQRVALARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 155 VNNPKILIFDEATSALDYESEHVI---MRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEPESL 231
Cdd:cd03296 152 AVEPKVLLLDEPFGALDAKVRKELrrwLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASP 231
|
...
1MT0_A 232 YSY 234
Cdd:cd03296 232 FVY 234
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
17-217 |
1.26e-34 |
|
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: 123.70 E-value: 1.26e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 17 VILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDL------ALADpnWLRRQVGVVLQDNVLLn 90
Cdd:COG4181 26 TILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLfaldedARAR--LRARHVGFVFQSFQLL- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 91 rsiidnislanPGMS-VEKVIYAAKLAGAHDFIS----ELREgyntiVGEQG------AGLSGGQRQRIAIARALVNNPK 159
Cdd:COG4181 103 -----------PTLTaLENVMLPLELAGRRDARAraraLLER-----VGLGHrldhypAQLSGGEQQRVALARAFATEPA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
1MT0_A 160 ILIFDEATSALDYE-SEHVI--MRNMHKIcKGRTVIIIAHRLSTVKNADRIIVMEKGKIVE 217
Cdd:COG4181 167 ILFADEPTGNLDAAtGEQIIdlLFELNRE-RGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-216 |
1.29e-34 |
|
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: 122.75 E-value: 1.29e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 6 NIRFRYKpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADpnwLRRQVGVVLQD 85
Cdd:cd03226 4 NISFSYK-KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKE---RRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 86 --NVLLNRSIIDNISLANPGMS-----VEKVIYAAKLAGAHDfiselregyntivgEQGAGLSGGQRQRIAIARALVNNP 158
Cdd:cd03226 80 vdYQLFTDSVREELLLGLKELDagneqAETVLKDLDLYALKE--------------RHPLSLSGGQKQRLAIAAALLSGK 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
1MT0_A 159 KILIFDEATSALDYESehviMRNMHKICK-----GRTVIIIAHRLSTVKN-ADRIIVMEKGKIV 216
Cdd:cd03226 146 DLLIFDEPTSGLDYKN----MERVGELIRelaaqGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-230 |
1.70e-34 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 123.58 E-value: 1.70e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLAL-ADPN-----WL 75
Cdd:COG4161 3 IQLKNINCFY--GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFsQKPSekairLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 76 RRQVGVVLQD-NVLLNRSIIDNISLAnP----GMSVEKVIYAAKLAGAHDFISELREGYNtivgeqgAGLSGGQRQRIAI 150
Cdd:COG4161 81 RQKVGMVFQQyNLWPHLTVMENLIEA-PckvlGLSKEQAREKAMKLLARLRLTDKADRFP-------LHLSGGQQQRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 151 ARALVNNPKILIFDEATSALDYE--SEHV-IMRNMHKIckGRTVIIIAHRLSTV-KNADRIIVMEKGKIVEQGKHkELLS 226
Cdd:COG4161 153 ARALMMEPQVLLFDEPTAALDPEitAQVVeIIRELSQT--GITQVIVTHEVEFArKVASQVVYMEKGRIIEQGDA-SHFT 229
|
....
1MT0_A 227 EPES 230
Cdd:COG4161 230 QPQT 233
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-230 |
1.89e-34 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 123.76 E-value: 1.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSpvILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLAL----------AD 71
Cdd:COG4598 9 LEVRDLHKSFGDLE--VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLkpdrdgelvpAD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 72 PNWLRR---QVGVVLQD-NVLLNRSIIDNISLAnPgMSVEKVIYAAKLAGAHDF-----ISELREGYNtivgeqgAGLSG 142
Cdd:COG4598 87 RRQLQRirtRLGMVFQSfNLWSHMTVLENVIEA-P-VHVLGRPKAEAIERAEALlakvgLADKRDAYP-------AHLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 143 GQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK-GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGK 220
Cdd:COG4598 158 GQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEeGRTMLVVTHEMGFARDvSSHVVFLHQGRIEEQGP 237
|
250
....*....|
1MT0_A 221 HKELLSEPES 230
Cdd:COG4598 238 PAEVFGNPKS 247
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-219 |
2.61e-34 |
|
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: 122.30 E-value: 2.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKpdSPVILDNINLSIKQGeVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDlALADPNWLRRQVGV 81
Cdd:cd03264 1 LQLENLTKRYG--KKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD-VLKQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNvllnrSIIDNISlanpgmSVEKVIYAAKLAGAHDfiSELRE---------GYNTIVGEQGAGLSGGQRQRIAIAR 152
Cdd:cd03264 77 LPQEF-----GVYPNFT------VREFLDYIAWLKGIPS--KEVKArvdevlelvNLGDRAKKKIGSLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1MT0_A 153 ALVNNPKILIFDEATSALDYEsEHVIMRNM-HKICKGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQG 219
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPE-ERIRFRNLlSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-224 |
4.84e-34 |
|
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: 121.84 E-value: 4.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLaLADPNWLRRQVGV 81
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLnrsiidnislanPGMSVEKVIYaaklagahdFISELREGYNTIVGEQGAG-----------------LSGGQ 144
Cdd:cd03263 80 CPQFDALF------------DELTVREHLR---------FYARLKGLPKSEIKEEVELllrvlgltdkankrartLSGGM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 145 RQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKE 223
Cdd:cd03263 139 KRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQE 218
|
.
1MT0_A 224 L 224
Cdd:cd03263 219 L 219
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-221 |
2.04e-33 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 120.89 E-value: 2.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSpvILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGH--DLAlADPN-----W 74
Cdd:PRK11124 3 IQLNGINCFYGAHQ--ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFS-KTPSdkairE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 75 LRRQVGVVLQD-NVLLNRSIIDNISLAnPgMSVEKVIYAAKLAGAHDFISELREgyntivgEQGAG-----LSGGQRQRI 148
Cdd:PRK11124 80 LRRNVGMVFQQyNLWPHLTVQQNLIEA-P-CRVLGLSKDQALARAEKLLERLRL-------KPYADrfplhLSGGQQQRV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1MT0_A 149 AIARALVNNPKILIFDEATSALDYEsehvIMRNMHKICK-----GRTVIIIAHRLSTV-KNADRIIVMEKGKIVEQGKH 221
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDPE----ITAQIVSIIRelaetGITQVIVTHEVEVArKTASRVVYMENGHIVEQGDA 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-231 |
2.31e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 121.34 E-value: 2.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 5 RNIRFRYkPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWL--RRQVGVV 82
Cdd:PRK13639 5 RDLKYSY-PDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTVGIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 83 LQ--DNVLLNRSIIDNISLA--NPGMSVE----KVIYAAKLAGAhdfiselrEGYNTIVGEQgagLSGGQRQRIAIARAL 154
Cdd:PRK13639 84 FQnpDDQLFAPTVEEDVAFGplNLGLSKEevekRVKEALKAVGM--------EGFENKPPHH---LSGGQKKRVAIAGIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1MT0_A 155 VNNPKILIFDEATSALDYESEHVIMRNMHKICK-GRTVIIIAHRLSTV-KNADRIIVMEKGKIVEQGKHKELLSEPESL 231
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKeGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDIETI 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-227 |
3.62e-33 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 119.46 E-value: 3.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 18 ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNW-LRRQVGVVLQD-NVLLNRSIID 95
Cdd:cd03224 15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGrRIFPELTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 96 NISLAnpGMSVEKVIYAAKLAGAHDFISELREGYNtivgeQGAG-LSGGQRQRIAIARALVNNPKILIFDEATSALDYES 174
Cdd:cd03224 95 NLLLG--AYARRRAKRKARLERVYELFPRLKERRK-----QLAGtLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKI 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
1MT0_A 175 EHVIMRNMHKICK-GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLSE 227
Cdd:cd03224 168 VEEIFEAIRELRDeGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
34-233 |
5.16e-33 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 121.83 E-value: 5.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 34 IVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNwlRRQVGVVLQDNVLLnrsiidnislanPGMSV-EKVIYA 112
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH--LRHINMVFQSYALF------------PHMTVeENVAFG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 113 AKLAG--AHDFISELREGYNTI-VGEQGAG----LSGGQRQRIAIARALVNNPKILIFDEATSALDY----ESEHVIMRN 181
Cdd:TIGR01187 67 LKMRKvpRAEIKPRVLEALRLVqLEEFADRkphqLSGGQQQRVALARALVFKPKILLLDEPLSALDKklrdQMQLELKTI 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
1MT0_A 182 MHKIckGRTVIIIAHRLS-TVKNADRIIVMEKGKIVEQGKHKELLSEPESLYS 233
Cdd:TIGR01187 147 QEQL--GITFVFVTHDQEeAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFV 197
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-233 |
7.92e-33 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 124.41 E-value: 7.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 6 NIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKS----TLTKLIQRFYIPENGQVLIDGHDLALADPNWLRR---- 77
Cdd:COG4172 13 SVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgn 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 78 QVGVVLQDNVllnrsiidnISLaNPGMSVEKVIYAA-----KLAG--AHDFISELREgyntIVG----EQGAG-----LS 141
Cdd:COG4172 93 RIAMIFQEPM---------TSL-NPLHTIGKQIAEVlrlhrGLSGaaARARALELLE----RVGipdpERRLDayphqLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 142 GGQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQ 218
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRelGMALLLITHDLGVVRRfADRVAVMRQGEIVEQ 238
|
250
....*....|....*
1MT0_A 219 GKHKELLSEPESLYS 233
Cdd:COG4172 239 GPTAELFAAPQHPYT 253
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-231 |
9.90e-33 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 119.49 E-value: 9.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 5 RNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGVVLQ 84
Cdd:PRK13548 6 RNLSVRL--GGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 85 dnvllnrsiidNISLANPgMSVEKVI----YAAKLAGAHDfiSELREGYNTIVGEQG-AG-----LSGGQRQRIAIARAL 154
Cdd:PRK13548 84 -----------HSSLSFP-FTVEEVVamgrAPHGLSRAED--DALVAAALAQVDLAHlAGrdypqLSGGEQQRVQLARVL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 155 V------NNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLS-TVKNADRIIVMEKGKIVEQGKHKELL 225
Cdd:PRK13548 150 AqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHerGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
....*.
1MT0_A 226 SePESL 231
Cdd:PRK13548 230 T-PETL 234
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-226 |
1.13e-32 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 118.53 E-value: 1.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 23 NLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNwlRRQVGVVLQDNVLLNR-SIIDNISLA- 100
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFSHlTVAQNIGLGl 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 101 NPGMSV-----EKVIYAAKLAGAHDFISELRegyntivgeqgAGLSGGQRQRIAIARALVNNPKILIFDEATSALDYESE 175
Cdd:PRK10771 97 NPGLKLnaaqrEKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
1MT0_A 176 HVIMRNMHKICKGR--TVIIIAHRLS-TVKNADRIIVMEKGKIVEQGKHKELLS 226
Cdd:PRK10771 166 QEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-241 |
1.44e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 119.88 E-value: 1.44e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSP---VILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDG----HDLALADPNW 74
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyehQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 75 LRRQVGVVLQ--------DNVllNRSIIdnISLANPGMSVEKViyaakLAGAHDFISELreGYNTIVGEQGA-GLSGGQR 145
Cdd:PRK13646 83 VRKRIGMVFQfpesqlfeDTV--EREII--FGPKNFKMNLDEV-----KNYAHRLLMDL--GFSRDVMSQSPfQMSGGQM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 146 QRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKIC--KGRTVIIIAHRLSTV-KNADRIIVMEKGKIVEQGKHK 222
Cdd:PRK13646 152 RKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPK 231
|
250 260
....*....|....*....|....*
1MT0_A 223 ELLSEPESLYSY------LYQLQSD 241
Cdd:PRK13646 232 ELFKDKKKLADWhiglpeIVQLQYD 256
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-219 |
1.86e-32 |
|
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: 117.36 E-value: 1.86e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNwlRRQVGV 81
Cdd:cd03301 1 VELENVTKRF--GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLL-NRSIIDNISL------ANPGMSVEKVIYAAKLAGahdfISELREGYNtivgeqgAGLSGGQRQRIAIARAL 154
Cdd:cd03301 77 VFQNYALYpHMTVYDNIAFglklrkVPKDEIDERVREVAELLQ----IEHLLDRKP-------KQLSGGQRQRVALGRAI 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 155 VNNPKILIFDEATSALDYESEhVIMR----NMHKICkGRTVIIIAH-RLSTVKNADRIIVMEKGKIVEQG 219
Cdd:cd03301 146 VREPKVFLMDEPLSNLDAKLR-VQMRaelkRLQQRL-GTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-223 |
2.63e-32 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 122.83 E-value: 2.63e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkpdSPVI-LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPN-WLRRQV 79
Cdd:COG3845 6 LELRGITKRF---GGVVaNDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRdAIALGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 80 GVVLQDNVLLNR-SIIDNISLANPGMSVEKViyaaKLAGAHDFISELREGY------NTIVGEqgagLSGGQRQRIAIAR 152
Cdd:COG3845 83 GMVHQHFMLVPNlTVAENIVLGLEPTKGGRL----DRKAARARIRELSERYgldvdpDAKVED----LSVGEQQRVEILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1MT0_A 153 ALVNNPKILIFDEATSAL-DYESEH--VIMRNMHKicKGRTVIIIAHRLSTVK-NADRIIVMEKGKIVEQGKHKE 223
Cdd:COG3845 155 ALYRGARILILDEPTAVLtPQEADElfEILRRLAA--EGKSIIFITHKLREVMaIADRVTVLRRGKVVGTVDTAE 227
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
2-171 |
1.69e-31 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 116.11 E-value: 1.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPD--SPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHdlALADPNWLRrqv 79
Cdd:COG4525 4 LTVRHVSVRYPGGgqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV--PVTGPGADR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 80 GVVLQDNVLLN-RSIIDNISLanpGMSVEKVIYAAKLAGAHDFISelregyntIVGEQGAG------LSGGQRQRIAIAR 152
Cdd:COG4525 79 GVVFQKDALLPwLNVLDNVAF---GLRLRGVPKAERRARAEELLA--------LVGLADFArrriwqLSGGMRQRVGIAR 147
|
170
....*....|....*....
1MT0_A 153 ALVNNPKILIFDEATSALD 171
Cdd:COG4525 148 ALAADPRFLLMDEPFGALD 166
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
2-219 |
2.01e-31 |
|
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: 114.77 E-value: 2.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPVI--LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDlALADPNWLRRQV 79
Cdd:cd03266 2 ITADALTKRFRDVKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFD-VVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 80 GVVLQDNVLLNRsiidnislanpgMSV-EKVIYAAKLAG-----AHDFISEL--REGYNTIVGEQGAGLSGGQRQRIAIA 151
Cdd:cd03266 81 GFVSDSTGLYDR------------LTArENLEYFAGLYGlkgdeLTARLEELadRLGMEELLDRRVGGFSTGMRQKVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 152 RALVNNPKILIFDEATSALDYESEHVIMRNMHKICK-GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQG 219
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
19-230 |
2.32e-31 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 116.09 E-value: 2.32e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGVVLQD-NVLLN-----RS 92
Cdd:COG4167 29 VKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQDpNTSLNprlniGQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 93 IIDNISLANPGMSV----EKVIYAAKLAG-----AHDFISELregyntivgeqgaglSGGQRQRIAIARALVNNPKILIF 163
Cdd:COG4167 109 ILEEPLRLNTDLTAeereERIFATLRLVGllpehANFYPHML---------------SSGQKQRVALARALILQPKIIIA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 164 DEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLSEPES 230
Cdd:COG4167 174 DEALAALDMSVRSQIINLMLELQEklGISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAEVFANPQH 243
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-231 |
2.40e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 116.47 E-value: 2.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPVI---LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNW---- 74
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEkkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 75 LRRQVGVVLQ--DNVLLNRSIIDNISLA--NPGMSVEKVIYAAKLAGAHDFISElregynTIVGEQGAGLSGGQRQRIAI 150
Cdd:PRK13641 83 LRKKVSLVFQfpEAQLFENTVLKDVEFGpkNFGFSEDEAKEKALKWLKKVGLSE------DLISKSPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 151 ARALVNNPKILIFDEATSALDYESEHVIM---RNMHKicKGRTVIIIAHRLSTV-KNADRIIVMEKGKIVEQGKHKELLS 226
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMqlfKDYQK--AGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPKEIFS 234
|
....*
1MT0_A 227 EPESL 231
Cdd:PRK13641 235 DKEWL 239
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
6-231 |
2.55e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 116.35 E-value: 2.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 6 NIRFRYKPDSPV-ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGVVLQ 84
Cdd:PRK13642 9 NLVFKYEKESDVnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 85 --DNVLLNRSIIDNIS--LANPGMSVEKVIYAAKLAGAHDFISELREgyntivgEQGAGLSGGQRQRIAIARALVNNPKI 160
Cdd:PRK13642 89 npDNQFVGATVEDDVAfgMENQGIPREEMIKRVDEALLAVNMLDFKT-------REPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1MT0_A 161 LIFDEATSALDYESEHVIMRNMHKICKGR--TVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEPESL 231
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSEDM 234
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-233 |
5.27e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 115.61 E-value: 5.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPV---ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPN----W 74
Cdd:PRK13649 3 INLQNVSYTYQAGTPFegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdikQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 75 LRRQVGVVLQ--DNVLLNRSIIDNISLA--NPGMSVEKVIYAAKLAGAHDFISElregynTIVGEQGAGLSGGQRQRIAI 150
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGpqNFGVSQEEAEALAREKLALVGISE------SLFEKNPFELSGGQMRRVAI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 151 ARALVNNPKILIFDEATSALDYESEHVIM---RNMHKicKGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLS 226
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPKGRKELMtlfKKLHQ--SGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIFQ 234
|
....*..
1MT0_A 227 EPESLYS 233
Cdd:PRK13649 235 DVDFLEE 241
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
2-227 |
8.35e-31 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 114.03 E-value: 8.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIP-ENGQVLIDGHDLALADPNWLRRQVG 80
Cdd:COG1119 4 LELRNVTVRR--GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVRLFGERRGGEDVWELRKRIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 81 VV---LQDNVllnrsiidnislaNPGMSVEKVIyaakLAGAHDFIselreG-YNTIVGEQ-----------GAG------ 139
Cdd:COG1119 82 LVspaLQLRF-------------PRDETVLDVV----LSGFFDSI-----GlYREPTDEQrerarellellGLAhladrp 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 140 ---LSGGQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKNA-DRIIVMEKG 213
Cdd:COG1119 140 fgtLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAegAPTLVLVTHHVEEIPPGiTHVLLLKDG 219
|
250
....*....|....
1MT0_A 214 KIVEQGKHKELLSE 227
Cdd:COG1119 220 RVVAAGPKEEVLTS 233
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
5-232 |
3.71e-30 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 114.82 E-value: 3.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 5 RNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDlaLADPNWLRRQVGVVLQ 84
Cdd:PRK11432 10 KNITKRF--GSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED--VTHRSIQQRDICMVFQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 85 DNVLL-NRSIIDNIS--LANPGMSVEKVIYAAK-------LAGAHD-FISElregyntivgeqgagLSGGQRQRIAIARA 153
Cdd:PRK11432 86 SYALFpHMSLGENVGygLKMLGVPKEERKQRVKealelvdLAGFEDrYVDQ---------------ISGGQQQRVALARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 154 LVNNPKILIFDEATSALDYEsehvIMRNMH-KICK-----GRTVIIIAHRLS-TVKNADRIIVMEKGKIVEQGKHKELLS 226
Cdd:PRK11432 151 LILKPKVLLFDEPLSNLDAN----LRRSMReKIRElqqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQELYR 226
|
....*.
1MT0_A 227 EPESLY 232
Cdd:PRK11432 227 QPASRF 232
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
18-217 |
4.85e-30 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 112.47 E-value: 4.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 18 ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLA-LADPNW--LRRQVGVVLQDNvllnrsii 94
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAkLNRAQRkaFRRDIQMVFQDS-------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 95 dnISLANPGMSVEKVIY-----------AAKLAGAHDFIS--ELREgynTIVGEQGAGLSGGQRQRIAIARALVNNPKIL 161
Cdd:PRK10419 99 --ISAVNPRKTVREIIReplrhllsldkAERLARASEMLRavDLDD---SVLDKRPPQLSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
1MT0_A 162 IFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVE 217
Cdd:PRK10419 174 ILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
14-233 |
5.68e-30 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 114.93 E-value: 5.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 14 DSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPnwLRRQVGVVLQDNVLLnrsi 93
Cdd:PRK11607 30 DGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP--YQRPINMMFQSYALF---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 94 idnislanPGMSVEKVIYAA----KLAGAhDFISELREGYNTIVGEQGAG-----LSGGQRQRIAIARALVNNPKILIFD 164
Cdd:PRK11607 104 --------PHMTVEQNIAFGlkqdKLPKA-EIASRVNEMLGLVHMQEFAKrkphqLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1MT0_A 165 EATSALDYESEHVIMRNMHKICK--GRTVIIIAH-RLSTVKNADRIIVMEKGKIVEQGKHKELLSEPESLYS 233
Cdd:PRK11607 175 EPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYS 246
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
23-220 |
6.15e-30 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 111.11 E-value: 6.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 23 NLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNwlRRQVGVVLQDNVLLNR-SIIDNISLA- 100
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPY--QRPVSMLFQENNLFAHlTVRQNIGLGl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 101 NPGMSV-----EKVIYAAKLAGAHDFISELREGyntivgeqgagLSGGQRQRIAIARALVNNPKILIFDEATSALDYESE 175
Cdd:TIGR01277 96 HPGLKLnaeqqEKVVDAAQQVGIADYLDRLPEQ-----------LSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
1MT0_A 176 HVIMRNMHKIC--KGRTVIIIAHRLS-TVKNADRIIVMEKGKIVEQGK 220
Cdd:TIGR01277 165 EEMLALVKQLCseRQRTLLMVTHHLSdARAIASQIAVVSQGKIKVVSD 212
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-229 |
1.09e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 111.16 E-value: 1.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRF--YIPE---NGQVLIDGHDLALADPNWLR 76
Cdd:PRK14247 4 IEIRDLKVSF--GQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQDIFKMDVIELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 77 RQVGVVLQ-DNVLLNRSIIDNISLA--------NPGMSVEKVIYAAKLAgahdfisELREGYNTIVGEQGAGLSGGQRQR 147
Cdd:PRK14247 82 RRVQMVFQiPNPIPNLSIFENVALGlklnrlvkSKKELQERVRWALEKA-------QLWDEVKDRLDAPAGKLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 148 IAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAH-RLSTVKNADRIIVMEKGKIVEQGKHKELLS 226
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
...
1MT0_A 227 EPE 229
Cdd:PRK14247 235 NPR 237
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
1-240 |
1.36e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 112.02 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 1 DITFRNIRFRYKPDSPV---ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDL-----ALADP 72
Cdd:PRK13645 6 DIILDNVSYTYAKKTPFefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlkKIKEV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 73 NWLRRQVGVVLQ--DNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFISeLREGYntiVGEQGAGLSGGQRQRIAI 150
Cdd:PRK13645 86 KRLRKEIGLVFQfpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQ-LPEDY---VKRSPFELSGGQKRRVAL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 151 ARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTV-KNADRIIVMEKGKIVEQG------KH 221
Cdd:PRK13645 162 AGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKVISIGspfeifSN 241
|
250 260
....*....|....*....|...
1MT0_A 222 KELLS----EPESLYSYLYQLQS 240
Cdd:PRK13645 242 QELLTkieiDPPKLYQLMYKLKN 264
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
9-233 |
1.43e-29 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 115.57 E-value: 1.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 9 FRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTlTKLIQRFYIPENGQVLIDGHDLALADPNWL---RRQVGVVLQD 85
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKST-TGLALLRLINSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQD 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 86 nvllnrsiiDNISLaNPGMSVEKVIyAAKLAGAHDFISELREGYNTIVGEQGAGL------------SGGQRQRIAIARA 153
Cdd:PRK15134 371 ---------PNSSL-NPRLNVLQII-EEGLRVHQPTLSAAQREQQVIAVMEEVGLdpetrhrypaefSGGQRQRIAIARA 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 154 LVNNPKILIFDEATSALDYESEHVIMRNMHKICKGRTV--IIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLSEPES 230
Cdd:PRK15134 440 LILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFAAPQQ 519
|
...
1MT0_A 231 LYS 233
Cdd:PRK15134 520 EYT 522
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
12-233 |
1.54e-29 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 112.88 E-value: 1.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 12 KPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDL-ALADPNWL--RRQVGVVLQDNVl 88
Cdd:PRK15079 30 PPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlGMKDDEWRavRSDIQMIFQDPL- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 89 lnrsiidnISLaNPGMSVEKVI------YAAKLAGAhdfisELREGYNTIVGEQGA----------GLSGGQRQRIAIAR 152
Cdd:PRK15079 109 --------ASL-NPRMTIGEIIaeplrtYHPKLSRQ-----EVKDRVKAMMLKVGLlpnlinryphEFSGGQCQRIGIAR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 153 ALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLSEPE 229
Cdd:PRK15079 175 ALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQRemGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEVYHNPL 254
|
....
1MT0_A 230 SLYS 233
Cdd:PRK15079 255 HPYT 258
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
19-229 |
2.46e-29 |
|
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).
Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 109.83 E-value: 2.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQ-VGVVLQDNVLLnrsiidni 97
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQIPRLF-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 98 slanPGMSV-EKVIYAAKLAGAHDFIS--------ELREGYNTI---VG------EQGAGLSGGQRQRIAIARALVNNPK 159
Cdd:cd03219 88 ----PELTVlENVMVAAQARTGSGLLLararreerEARERAEELlerVGladladRPAGELSYGQQRRLEIARALATDPK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1MT0_A 160 ILIFDEATSAL-DYESEHVI--MRNMHKicKGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLSEPE 229
Cdd:cd03219 164 LLLLDEPAAGLnPEETEELAelIRELRE--RGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-232 |
3.93e-29 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 112.82 E-value: 3.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 23 NLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWL----RRQVGVVLQDNVLL-NRSIIDNI 97
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELrevrRKKIAMVFQSFALMpHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 98 SLanpGMSVEKVIYAAKLAGAHDFISELreGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKILIFDEATSALD------ 171
Cdd:PRK10070 128 AF---GMELAGINAEERREKALDALRQV--GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDplirte 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
1MT0_A 172 YESEHVIMRNMHKickgRTVIIIAHRL-STVKNADRIIVMEKGKIVEQGKHKELLSEPESLY 232
Cdd:PRK10070 203 MQDELVKLQAKHQ----RTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDY 260
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
6-219 |
4.50e-29 |
|
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: 108.54 E-value: 4.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 6 NIRFRYKpdspviLDNINLSIK---QGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWL----RRQ 78
Cdd:cd03297 3 CVDIEKR------LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINlppqQRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 79 VGVVLQDNVLL-NRSIIDNISLANPGMS-VEKVIYAAKLAGAHDfISELREGYNtivgeqgAGLSGGQRQRIAIARALVN 156
Cdd:cd03297 77 IGLVFQQYALFpHLNVRENLAFGLKRKRnREDRISVDELLDLLG-LDHLLNRYP-------AQLSGGEKQRVALARALAA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1MT0_A 157 NPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTV-KNADRIIVMEKGKIVEQG 219
Cdd:cd03297 149 QPELLLLDEPFSALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
2-233 |
4.66e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 110.32 E-value: 4.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNW--LRRQV 79
Cdd:PRK13636 6 LKVEELNYNY-SDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLmkLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 80 GVVLQ--DNVLLNRSIIDNISLA--NPGMSVEKVIYAAKLAGAHDFISELREgyntivgEQGAGLSGGQRQRIAIARALV 155
Cdd:PRK13636 85 GMVFQdpDNQLFSASVYQDVSFGavNLKLPEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 156 NNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVK-NADRIIVMEKGKIVEQGKHKELLSEPESLY 232
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEKEMLR 237
|
.
1MT0_A 233 S 233
Cdd:PRK13636 238 K 238
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-231 |
6.21e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 110.56 E-value: 6.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPV---ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQV---LIDGHDLALADP--- 72
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEkek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 73 ------------------NWLRRQVGVVLQ--DNVLLNRSIIDNISLANPGMSVEKViYAAKLAGAHDFISELREGYnti 132
Cdd:PRK13651 83 vleklviqktrfkkikkiKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKE-EAKKRAAKYIELVGLDESY--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 133 VGEQGAGLSGGQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK-GRTVIIIAHRLSTV-KNADRIIVM 210
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKqGKTIILVTHDLDNVlEWTKRTIFF 238
|
250 260
....*....|....*....|.
1MT0_A 211 EKGKIVEQGKHKELLSEPESL 231
Cdd:PRK13651 239 KDGKIIKDGDTYDILSDNKFL 259
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
18-235 |
6.78e-29 |
|
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: 108.53 E-value: 6.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 18 ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWL-RRQVGVVLQDnvllnRSIIdn 96
Cdd:COG0410 18 VLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEG-----RRIF-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 97 islanPGMSVE------------KVIYAAKLAGAHDFISELREGYNtivgeQGAG-LSGGQRQRIAIARALVNNPKILIF 163
Cdd:COG0410 91 -----PSLTVEenlllgayarrdRAEVRADLERVYELFPRLKERRR-----QRAGtLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 164 DEATSALdyesEHVIMRNMHKICK-----GRTVIII---AHRLSTVknADRIIVMEKGKIVEQGKHKELLSEPESLYSYL 235
Cdd:COG0410 161 DEPSLGL----APLIVEEIFEIIRrlnreGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGTAAELLADPEVREAYL 234
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
5-216 |
8.59e-29 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 113.67 E-value: 8.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 5 RNIRFRYKP--DSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWL----RRQ 78
Cdd:PRK10535 8 KDIRRSYPSgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrREH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 79 VGVVLQDNVLLNR-SIIDNISLANPGMSVEKviyAAKLAGAHDFISELreGYNTIVGEQGAGLSGGQRQRIAIARALVNN 157
Cdd:PRK10535 88 FGFIFQRYHLLSHlTAAQNVEVPAVYAGLER---KQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 158 PKILIFDEATSALDYESEHVIMRNMHKIC-KGRTVIIIAHRLSTVKNADRIIVMEKGKIV 216
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRdRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
18-215 |
1.20e-28 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 108.61 E-value: 1.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 18 ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALAdpnwlRRQVGVVLQDNVLLN-RSIIDN 96
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLMFQDARLLPwKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 97 ISLANPGMSVEKVIYAAKLAGAHDfiselRegyntiVGEQGAGLSGGQRQRIAIARALVNNPKILIFDEATSALD----Y 172
Cdd:PRK11247 102 VGLGLKGQWRDAALQALAAVGLAD-----R------ANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDaltrI 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
1MT0_A 173 ESEHVIMRNMHKicKGRTVIIIAHRLS-TVKNADRIIVMEKGKI 215
Cdd:PRK11247 171 EMQDLIESLWQQ--HGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-219 |
1.53e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 107.86 E-value: 1.53e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 17 VILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADpnwlrrqVGVVLQ------DNVLLN 90
Cdd:COG1134 40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLE-------LGAGFHpeltgrENIYLN 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 91 RSIIdnislanpGMSVEKViyAAKLAGAHDFiSELREGYNTIVGeqgaGLSGGQRQRIAIARALVNNPKILIFDEATSAL 170
Cdd:COG1134 113 GRLL--------GLSRKEI--DEKFDEIVEF-AELGDFIDQPVK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVG 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
1MT0_A 171 DYE----SEHViMRNMHKicKGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQG 219
Cdd:COG1134 178 DAAfqkkCLAR-IRELRE--SGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDG 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
18-230 |
1.84e-28 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 108.13 E-value: 1.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 18 ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLAL----------ADPN---WLRRQVGVVLQ 84
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLvrdkdgqlkvADKNqlrLLRTRLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 85 D-NVLLNRSIIDNI--------SLANPGMSVEKVIYAAKLAgahdfISELREGyntivgEQGAGLSGGQRQRIAIARALV 155
Cdd:PRK10619 100 HfNLWSHMTVLENVmeapiqvlGLSKQEARERAVKYLAKVG-----IDERAQG------KYPVHLSGGQQQRVSIARALA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1MT0_A 156 NNPKILIFDEATSALDYESEHVIMRNMHKIC-KGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLSEPES 230
Cdd:PRK10619 169 MEPEVLLFDEPTSALDPELVGEVLRIMQQLAeEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFGNPQS 245
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
11-210 |
1.89e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 107.49 E-value: 1.89e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 11 YKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGVVLQDNVLLN 90
Cdd:PRK10247 15 YLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLFG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 91 RSIIDNisLANP----GMSVEKVIYAAKLAgahDFisELREgynTIVGEQGAGLSGGQRQRIAIARALVNNPKILIFDEA 166
Cdd:PRK10247 95 DTVYDN--LIFPwqirNQQPDPAIFLDDLE---RF--ALPD---TILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
1MT0_A 167 TSALDYESEHVIMRNMHKIC--KGRTVIIIAHRLSTVKNADRIIVM 210
Cdd:PRK10247 165 TSALDESNKHNVNEIIHRYVreQNIAVLWVTHDKDEINHADKVITL 210
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
19-228 |
1.93e-28 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 109.67 E-value: 1.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADP---NWLRRQVGVVLQDNV-LLN-RSI 93
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPeaqKLLRQKIQIVFQNPYgSLNpRKK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 94 IDNIsLANPGMSVEKVIYAAKLAGAHDFISE--LR-EGYntivGEQGAGLSGGQRQRIAIARALVNNPKILIFDEATSAL 170
Cdd:PRK11308 111 VGQI-LEEPLLINTSLSAAERREKALAMMAKvgLRpEHY----DRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSAL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
1MT0_A 171 DYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLSEP 228
Cdd:PRK11308 186 DVSVQAQVLNLMMDLQQelGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFNNP 246
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-229 |
2.40e-28 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 107.86 E-value: 2.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSP---VILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLAlADPNWLR-R 77
Cdd:COG1101 2 LELKNLSKTFNPGTVnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVT-KLPEYKRaK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 78 QVGVVLQDNVL---LNRSIIDNISLA-------NPGMSVEKviyaAKLAGAHDFISELREGY----NTIVGEqgagLSGG 143
Cdd:COG1101 81 YIGRVFQDPMMgtaPSMTIEENLALAyrrgkrrGLRRGLTK----KRRELFRELLATLGLGLenrlDTKVGL----LSGG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 144 QRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICKGR--TVIIIAHRLS-TVKNADRIIVMEKGKIVE--Q 218
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENnlTTLMVTHNMEqALDYGNRLIMMHEGRIILdvS 232
|
250
....*....|.
1MT0_A 219 GKHKELLSEPE 229
Cdd:COG1101 233 GEEKKKLTVED 243
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
18-219 |
5.64e-28 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 106.20 E-value: 5.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 18 ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLI----QRFYIpENGQVLIDGHDLalaDPNWLRRQVGVVLQDNVLLnrsi 93
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsgrvEGGGT-TSGQILFNGQPR---KPDQFQKCVAYVRQDDILL---- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 94 idnislanPGMSVEKVI-YAAKLAG----------AHDFISELREGYNTIVGEQG-AGLSGGQRQRIAIARALVNNPKIL 161
Cdd:cd03234 94 --------PGLTVRETLtYTAILRLprkssdairkKRVEDVLLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
1MT0_A 162 IFDEATSALDYESEHVIMRNMHKICK-GRTVIIIAH--RLSTVKNADRIIVMEKGKIVEQG 219
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQLARrNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
2-241 |
6.96e-28 |
|
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: 111.58 E-value: 6.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVgv 81
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDS-- 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 vLQDNVLLNRSIIDNislanpgmSVEKVIYAAKLAGAhdfISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKIL 161
Cdd:TIGR00957 715 -LRENILFGKALNEK--------YYQQVLEACALLPD---LEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIY 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 162 IFDEATSALDYES-----EHVImrNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEPESLYSYLY 236
Cdd:TIGR00957 783 LFDDPLSAVDAHVgkhifEHVI--GPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEFLR 860
|
....*
1MT0_A 237 QLQSD 241
Cdd:TIGR00957 861 TYAPD 865
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
19-229 |
1.12e-27 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 106.01 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRF--YIPE---NGQVLIDGHDL--ALADPNWLRRQVGVVLQDnvllnr 91
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIysPRTDTVDLRKEIGMVFQQ------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 92 siidnislANP-GMSV-EKVIYAAKLAGAHD--FISELREgyNTIVG------------EQGAGLSGGQRQRIAIARALV 155
Cdd:PRK14239 95 --------PNPfPMSIyENVVYGLRLKGIKDkqVLDEAVE--KSLKGasiwdevkdrlhDSALGLSGGQQQRVCIARVLA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1MT0_A 156 NNPKILIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLSEPE 229
Cdd:PRK14239 165 TSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
19-219 |
1.15e-27 |
|
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: 104.99 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDlaLADPNWLRRQVGvvlqdnvllnrSIIDNIS 98
Cdd:cd03268 16 LDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKS--YQKNIEALRRIG-----------ALIEAPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 99 LaNPGMS-VEKVIYAAKLAG-AHDFISELREgyntIVGEQGAG------LSGGQRQRIAIARALVNNPKILIFDEATSAL 170
Cdd:cd03268 83 F-YPNLTaRENLRLLARLLGiRKKRIDEVLD----VVGLKDSAkkkvkgFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
1MT0_A 171 DYESEHVIMRNMHKICK-GRTVIIIAHRLSTV-KNADRIIVMEKGKIVEQG 219
Cdd:cd03268 158 DPDGIKELRELILSLRDqGITVLISSHLLSEIqKVADRIGIINKGKLIEEG 208
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
17-229 |
2.17e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 106.86 E-value: 2.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 17 VILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLID----GHDLALADPNW------------LRRQVG 80
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELITnpyskkiknfkeLRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 81 VVLQ--DNVLLNRSIIDNISLANPGMSVEKvIYAAKLAGAHDFISELREGYntiVGEQGAGLSGGQRQRIAIARALVNNP 158
Cdd:PRK13631 120 MVFQfpEYQLFKDTIEKDIMFGPVALGVKK-SEAKKLAKFYLNKMGLDDSY---LERSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1MT0_A 159 KILIFDEATSALDYESEHVIMRNMHKICK-GRTVIIIAHRLSTV-KNADRIIVMEKGKIVEQGKHKELLSEPE 229
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLILDAKAnNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIFTDQH 268
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
2-232 |
3.90e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 104.39 E-value: 3.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGV 81
Cdd:COG4604 2 IEIKNVSKRY--GGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLNR-------------------SIIDNislanpgMSVEKVIYAAKLAG-AHDFISELregyntivgeqgaglS 141
Cdd:COG4604 80 LRQENHINSRltvrelvafgrfpyskgrlTAEDR-------EIIDEAIAYLDLEDlADRYLDEL---------------S 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 142 GGQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKIC--KGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQ 218
Cdd:COG4604 138 GGQRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdeLGKTVVIVLHDINFASCyADHIVAMKDGRVVAQ 217
|
250
....*....|....*.
1MT0_A 219 GKHKELLSEP--ESLY 232
Cdd:COG4604 218 GTPEEIITPEvlSDIY 233
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-213 |
4.15e-27 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 104.08 E-value: 4.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLrrqvgVVLQDNVLLN-RSIIDNI 97
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM-----VVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 98 SLA----NPGMSVEKviyAAKLAGAHDFISELREGYNTIVGEqgagLSGGQRQRIAIARALVNNPKILIFDEATSALDYE 173
Cdd:TIGR01184 76 ALAvdrvLPDLSKSE---RRAIVEEHIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDAL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
1MT0_A 174 SEHVIMRNMHKICK--GRTVIIIAHRL-STVKNADRIIVMEKG 213
Cdd:TIGR01184 149 TRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-225 |
4.63e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 105.66 E-value: 4.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNwLRRQVGV 81
Cdd:PRK13537 8 IDFRNVEKRY--GDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH-ARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQ-DNVLLNRSIIDNISLANP--GMSVEKViyAAKLAGAHDFiSELREGYNTIVGEqgagLSGGQRQRIAIARALVNNP 158
Cdd:PRK13537 85 VPQfDNLDPDFTVRENLLVFGRyfGLSAAAA--RALVPPLLEF-AKLENKADAKVGE----LSGGMKRRLTLARALVNDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1MT0_A 159 KILIFDEATSALDYESEHVIMRNMHKI-CKGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELL 225
Cdd:PRK13537 158 DVLVLDEPTTGLDPQARHLMWERLRSLlARGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALI 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-227 |
4.66e-27 |
|
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: 108.35 E-value: 4.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRY-KPDSPVI--LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQV-------LIDGHDLALAD 71
Cdd:TIGR03269 280 IKVRNVSKRYiSVDRGVVkaVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvrvgdeWVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 72 PNWLRRQVGVVLQDNVLL-NRSIIDN----ISLANPG-MSVEKVIYAAKLAGAHDfiselrEGYNTIVGEQGAGLSGGQR 145
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYpHRTVLDNlteaIGLELPDeLARMKAVITLKMVGFDE------EKAEEILDKYPDELSEGER 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 146 QRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHK 222
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDPE 513
|
....*
1MT0_A 223 ELLSE 227
Cdd:TIGR03269 514 EIVEE 518
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
18-219 |
4.70e-27 |
|
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: 103.77 E-value: 4.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 18 ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNwlrrqVGVVLQ----DNVLLNRSI 93
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLG-----GGFNPEltgrENIYLNGRL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 94 IdnislanpGMSVEKViyAAKLAGAHDFiSELREGYNTIVGEqgagLSGGQRQRIAIARALVNNPKILIFDEATSALD-- 171
Cdd:cd03220 112 L--------GLSRKEI--DEKIDEIIEF-SELGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDEVLAVGDaa 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
1MT0_A 172 -YESEHVIMRNMHKicKGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQG 219
Cdd:cd03220 177 fQEKCQRRLRELLK--QGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-226 |
6.23e-27 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 108.21 E-value: 6.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 18 ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQrFYIPEN----GQVLIDGHDLalaDPNWLRRQVGVVLQDNVLLnrsi 93
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKGvkgsGSVLLNGMPI---DAKEMRAISAYVQQDDLFI---- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 94 idnislanPGMSV-EKVIYAAKL-AGAHDFISE-------------LREGYNTIVGEQGA--GLSGGQRQRIAIARALVN 156
Cdd:TIGR00955 112 --------PTLTVrEHLMFQAHLrMPRRVTKKEkrervdevlqalgLRKCANTRIGVPGRvkGLSGGERKRLAFASELLT 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1MT0_A 157 NPKILIFDEATSALDYESEHVIMRNMHKIC-KGRTVIIIAHRLST--VKNADRIIVMEKGKIVEQGKHKELLS 226
Cdd:TIGR00955 184 DPPLLFCDEPTSGLDSFMAYSVVQVLKGLAqKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-207 |
6.63e-27 |
|
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: 102.56 E-value: 6.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWlRRQVGV 81
Cdd:COG4133 3 LEAENLSCRR--GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLlnrsiidnislaNPGMSV-EKVIYAAKLAGAHDFISELRE--------GY-NTIVGEqgagLSGGQRQRIAIA 151
Cdd:COG4133 80 LGHADGL------------KPELTVrENLRFWAALYGLRADREAIDEaleavglaGLaDLPVRQ----LSAGQKRRVALA 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
1MT0_A 152 RALVNNPKILIFDEATSALDYESEHVIMRNMHKIC-KGRTVIIIAHRLSTVKNADRI 207
Cdd:COG4133 144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLaRGGAVLLTTHQPLELAAARVL 200
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
11-224 |
7.46e-27 |
|
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: 103.22 E-value: 7.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 11 YKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDlALADPNWLRRQVGVVLQDnvlln 90
Cdd:cd03265 8 KKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHD-VVREPREVRRRIGIVFQD----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 91 rSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGY------NTIVGEqgagLSGGQRQRIAIARALVNNPKILIFD 164
Cdd:cd03265 82 -LSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVglleaaDRLVKT----YSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
1MT0_A 165 EATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTV-KNADRIIVMEKGKIVEQGKHKEL 224
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEefGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-219 |
8.18e-27 |
|
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: 102.74 E-value: 8.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDspVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADpnwlRRQVGV 81
Cdd:cd03269 1 LEVENVTKRFGRV--TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVL-LNRSIIDNIslanpgmsvekvIYAAKLAG--AHDFISELRE--------GYNTIVGEQgagLSGGQRQRIAI 150
Cdd:cd03269 75 LPEERGLyPKMKVIDQL------------VYLAQLKGlkKEEARRRIDEwlerlelsEYANKRVEE---LSKGNQQKVQF 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1MT0_A 151 ARALVNNPKILIFDEATSALDYESEHVIMRNMHKIC-KGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQG 219
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELArAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-231 |
1.16e-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: 105.57 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 21 NINLSIKQGEVIGIVGRSGSGKSTLTKLI---QRfyiPENGQVLIDGHDLALADPN-WL---RRQVGVVLQDNVLLnrsi 93
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIaglER---PDSGRIRLGGEVLQDSARGiFLpphRRRIGYVFQEARLF---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 94 idnislanPGMSVEK-VIYAAKLAGAhdfiSELREGYNTIVGEQG---------AGLSGGQRQRIAIARALVNNPKILIF 163
Cdd:COG4148 90 --------PHLSVRGnLLYGRKRAPR----AERRISFDEVVELLGighlldrrpATLSGGERQRVAIGRALLSSPRLLLM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 164 DEATSALDYESEHVIM---RNMHKickgRT---VIIIAH------RLstvknADRIIVMEKGKIVEQGKHKELLSEPESL 231
Cdd:COG4148 158 DEPLAALDLARKAEILpylERLRD----ELdipILYVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVLSRPDLL 228
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
18-230 |
1.60e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 105.17 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 18 ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNwlRRQVGVVLQDNVLLNR-SIIDN 96
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFRHmTVFDN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 97 ISLanpGMSV-------EKVIYAAKLAGAHDFI--SELREGYNtivgeqgAGLSGGQRQRIAIARALVNNPKILIFDEAT 167
Cdd:PRK10851 95 IAF---GLTVlprrerpNAAAIKAKVTQLLEMVqlAHLADRYP-------AQLSGGQKQRVALARALAVEPQILLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1MT0_A 168 SALDYESEHVI---MRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEPES 230
Cdd:PRK10851 165 GALDAQVRKELrrwLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPAT 230
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
18-227 |
2.61e-26 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 102.40 E-value: 2.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 18 ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGVVLQdnvllnrsiidnI 97
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQ------------H 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 98 SLANPGMSVEKVI---------YAAKLAGAHDFISEL---REGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKILIFDE 165
Cdd:PRK11231 85 HLTPEGITVRELVaygrspwlsLWGRLSAEDNARVNQameQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
1MT0_A 166 ATSALDYESEHVIMRNMHKI-CKGRTVIIIAHRLSTV-KNADRIIVMEKGKIVEQGKHKELLSE 227
Cdd:PRK11231 165 PTTYLDINHQVELMRLMRELnTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPEEVMTP 228
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
19-223 |
2.83e-26 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 101.49 E-value: 2.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHD---LALADPNWLRRQVGVVLQDN-VLLNRSII 94
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDitrLKNREVPFLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 95 DNIS--LANPGMSVEKViyAAKLAGAHDFISELREGYNTIVGeqgagLSGGQRQRIAIARALVNNPKILIFDEATSALDY 172
Cdd:PRK10908 98 DNVAipLIIAGASGDDI--RRRVSAALDKVGLLDKAKNFPIQ-----LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
1MT0_A 173 ESEHVIMRNMHKICK-GRTVIIIAHRLSTVKNAD-RIIVMEKGKIVEqGKHKE 223
Cdd:PRK10908 171 ALSEGILRLFEEFNRvGVTVLMATHDIGLISRRSyRMLTLSDGHLHG-GVGGE 222
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
9-213 |
3.95e-26 |
|
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: 101.25 E-value: 3.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 9 FRYKPDSPViLDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVL----IDGHDLALADPNWLRRQVGVVLQ 84
Cdd:cd03290 8 FSWGSGLAT-LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 85 DNVLLNRSIIDNISLANP--GMSVEKVIYAAKLAGAHDFiseLREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKILI 162
Cdd:cd03290 87 KPWLLNATVEENITFGSPfnKQRYKAVTDACSLQPDIDL---LPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
1MT0_A 163 FDEATSALD-YESEHVIMRNMHKICKG--RTVIIIAHRLSTVKNADRIIVMEKG 213
Cdd:cd03290 164 LDDPFSALDiHLSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-213 |
4.20e-26 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 106.04 E-value: 4.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 1 DITFRNIRFRyKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLI-----------------------QRFYIPEn 57
Cdd:COG4178 362 ALALEDLTLR-TPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpygsgriarpagarvlflpQRPYLPL- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 58 gQVLIDghdlALADPNwlrrqvgvvlqdnvllnrsiidnislANPGMSVEKVIYAAKLAGAHDFISELREGYNTivgeqG 137
Cdd:COG4178 440 -GTLRE----ALLYPA--------------------------TAEAFSDAELREALEAVGLGHLAERLDEEADW-----D 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
1MT0_A 138 AGLSGGQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKG 213
Cdd:COG4178 484 QVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-234 |
5.97e-26 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 103.57 E-value: 5.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 1 DITFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDG---HDLALADpnwlrR 77
Cdd:PRK11000 3 SVTLRNVTKAY--GDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEkrmNDVPPAE-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 78 QVGVVLQDNVLL-NRSIIDNISLanpGMsvekviyaaKLAGAHDfiSELREGYNTI---------VGEQGAGLSGGQRQR 147
Cdd:PRK11000 76 GVGMVFQSYALYpHLSVAENMSF---GL---------KLAGAKK--EEINQRVNQVaevlqlahlLDRKPKALSGGQRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 148 IAIARALVNNPKILIFDEATSALDyESEHVIMR----NMHKICkGRTVIIIAH-RLSTVKNADRIIVMEKGKIVEQGKhk 222
Cdd:PRK11000 142 VAIGRTLVAEPSVFLLDEPLSNLD-AALRVQMRieisRLHKRL-GRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVGK-- 217
|
250
....*....|..
1MT0_A 223 ellsePESLYSY 234
Cdd:PRK11000 218 -----PLELYHY 224
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
2-231 |
1.20e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 101.42 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPViLDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGV 81
Cdd:PRK13652 4 IETRDLCYSYSGSKEA-LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQ--DNVLLNRSIIDNISLA--NPGMSVEKVIYAAKLAGAHDFISELREgyntivgEQGAGLSGGQRQRIAIARALVNN 157
Cdd:PRK13652 83 VFQnpDDQIFSPTVEQDIAFGpiNLGLDEETVAHRVSSALHMLGLEELRD-------RVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1MT0_A 158 PKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLSEPESL 231
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVEEIFLQPDLL 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
13-171 |
1.37e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 100.54 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 13 PDSPViLDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGhdLALADPNWLRrqvGVVLQDNVLLN-R 91
Cdd:PRK11248 12 GGKPA-LEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG--KPVEGPGAER---GVVFQNEGLLPwR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 92 SIIDNISLanpGMSVEKVIYAAKLAGAHDFISElregyntiVGEQGAG------LSGGQRQRIAIARALVNNPKILIFDE 165
Cdd:PRK11248 86 NVQDNVAF---GLQLAGVEKMQRLEIAHQMLKK--------VGLEGAEkryiwqLSGGQRQRVGIARALAANPQLLLLDE 154
|
....*.
1MT0_A 166 ATSALD 171
Cdd:PRK11248 155 PFGALD 160
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-230 |
1.47e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.51 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 14 DSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFY------IPENGQVLIDGHDLALADPNWLRRQVGVVLQD-N 86
Cdd:PRK14246 21 NDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQpN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 87 VLLNRSIIDNIS--LANPGMSVEKVIYAAkLAGAHDFISELREGYNTIvGEQGAGLSGGQRQRIAIARALVNNPKILIFD 164
Cdd:PRK14246 101 PFPHLSIYDNIAypLKSHGIKEKREIKKI-VEECLRKVGLWKEVYDRL-NSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1MT0_A 165 EATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTV-KNADRIIVMEKGKIVEQGKHKELLSEPES 230
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIFTSPKN 245
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
2-234 |
1.69e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 100.96 E-value: 1.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPVI---LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDghDLALADPNW---- 74
Cdd:PRK13643 2 IKFEKVNYTYQPNSPFAsraLFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVG--DIVVSSTSKqkei 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 75 --LRRQVGVVLQ--DNVLLNRSIIDNISLA--NPGMSVEKV--IYAAKLagahDFISELREGYNTIVGEqgagLSGGQRQ 146
Cdd:PRK13643 80 kpVRKKVGVVFQfpESQLFEETVLKDVAFGpqNFGIPKEKAekIAAEKL----EMVGLADEFWEKSPFE----LSGGQMR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 147 RIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK-GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKEL 224
Cdd:PRK13643 152 RVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDV 231
|
250
....*....|
1MT0_A 225 LSEPESLYSY 234
Cdd:PRK13643 232 FQEVDFLKAH 241
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-227 |
4.35e-25 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 101.06 E-value: 4.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKpDSPVIlDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLAlADPNWLRRQVGV 81
Cdd:PRK13536 42 IDLAGVSKSYG-DKAVV-NGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP-ARARLARARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQ-DNVLLNRSIIDNISLANP--GMSVEKViyAAKLAGAHDFiSELREGYNTIVGEqgagLSGGQRQRIAIARALVNNP 158
Cdd:PRK13536 119 VPQfDNLDLEFTVRENLLVFGRyfGMSTREI--EAVIPSLLEF-ARLESKADARVSD----LSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1MT0_A 159 KILIFDEATSALDYESEHVIMRNMHK-ICKGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLSE 227
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHALIDE 262
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-224 |
4.77e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 100.18 E-value: 4.77e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADpnwlRRQVGV 81
Cdd:COG4152 2 LELKGLTKRF--GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDnvllnRSIidnislaNPGMSV-EKVIYAAKLAG--AHDFISELRE--------GY-NTIVGEqgagLSGGQRQRIA 149
Cdd:COG4152 76 LPEE-----RGL-------YPKMKVgEQLVYLARLKGlsKAEAKRRADEwlerlglgDRaNKKVEE----LSKGNQQKVQ 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1MT0_A 150 IARALVNNPKILIFDEATSALDYESEHVIM---RNMHKicKGRTVIIIAHRLSTV-KNADRIIVMEKGKIVEQGKHKEL 224
Cdd:COG4152 140 LIAALLHDPELLILDEPFSGLDPVNVELLKdviRELAA--KGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEI 216
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-229 |
6.61e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 99.04 E-value: 6.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGV 81
Cdd:PRK13647 5 IEVEDLHFRYK-DGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQ--DNVLLNRSIIDNISLA--NPGMS----VEKVIYAAKLAGAHDFISelREGYNtivgeqgagLSGGQRQRIAIARA 153
Cdd:PRK13647 84 VFQdpDDQVFSSTVWDDVAFGpvNMGLDkdevERRVEEALKAVRMWDFRD--KPPYH---------LSYGQKKRVAIAGV 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1MT0_A 154 LVNNPKILIFDEATSALDYESEHVIMRNMHKICK-GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKhKELLSEPE 229
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNqGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGD-KSLLTDED 229
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
18-224 |
6.66e-25 |
|
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: 97.98 E-value: 6.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 18 ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWL-RRQVGVVLQdnvllNRSIIdn 96
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVPQ-----GREIF-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 97 islanPGMSVEKVIY--AAKLAGAH----DFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKILIFDEATSAL 170
Cdd:TIGR03410 88 -----PRLTVEENLLtgLAALPRRSrkipDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
1MT0_A 171 D----YESEHVIMRNMHKicKGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKEL 224
Cdd:TIGR03410 163 QpsiiKDIGRVIRRLRAE--GGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-215 |
1.81e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 100.91 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 4 FRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIdghdlalaDPNWlrrQVGVVL 83
Cdd:COG0488 1 LENLSKSF--GGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI--------PKGL---RIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 84 QDNVLL-NRSIIDNI----------------SLANPGMSVEKVIYAAKL------AGAHDFISELR----------EGYN 130
Cdd:COG0488 68 QEPPLDdDLTVLDTVldgdaelraleaeleeLEAKLAEPDEDLERLAELqeefeaLGGWEAEARAEeilsglgfpeEDLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 131 TIVGEqgagLSGGQRQRIAIARALVNNPKILIFDEATSALDYES-----EHVIMRnmhkicKGrTVIIIAH-R--LSTVk 202
Cdd:COG0488 148 RPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewleEFLKNY------PG-TVLVVSHdRyfLDRV- 215
|
250
....*....|...
1MT0_A 203 nADRIIVMEKGKI 215
Cdd:COG0488 216 -ATRILELDRGKL 227
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-217 |
2.87e-24 |
|
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: 100.64 E-value: 2.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKP---DSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQ 78
Cdd:COG4615 328 LELRGVTYRYPGedgDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 79 VGVVLQDNVLLNRsiidnisLANP-GMSVEKVI--YAAKLAGAH------DFISELRegyntivgeqgagLSGGQRQRIA 149
Cdd:COG4615 408 FSAVFSDFHLFDR-------LLGLdGEADPARAreLLERLELDHkvsvedGRFSTTD-------------LSQGQRKRLA 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 150 IARALVNNPKILIFDEATSALD-------YeseHVIMRNMHKicKGRTVIIIAH-----RLstvknADRIIVMEKGKIVE 217
Cdd:COG4615 468 LLVALLEDRPILVFDEWAADQDpefrrvfY---TELLPELKA--RGKTVIAISHddryfDL-----ADRVLKMDYGKLVE 537
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
22-228 |
2.97e-24 |
|
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: 99.03 E-value: 2.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 22 INLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWL----RRQVGVVLQDNVLLnrsiidni 97
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFlppeKRRIGYVFQEARLF-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 98 slanPGMSV-EKVIYAAKLA-GAHDFISELRE----GYNTIVGEQGAGLSGGQRQRIAIARALVNNPKILIFDEATSALD 171
Cdd:TIGR02142 88 ----PHLSVrGNLRYGMKRArPSERRISFERViellGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALD 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
1MT0_A 172 YESEHVIM---RNMH---KIckgrTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLSEP 228
Cdd:TIGR02142 164 DPRKYEILpylERLHaefGI----PILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
18-218 |
3.01e-24 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 96.42 E-value: 3.01e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 18 ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDL----ALADPNWLRRQVGVVLQDNVLLNrsi 93
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMsklsSAAKAELRNQKLGFIYQFHHLLP--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 94 iDNISLANPGMSVekVIYAAKLAGAHDFISELRE--GYNTIVGEQGAGLSGGQRQRIAIARALVNNPKILIFDEATSALD 171
Cdd:PRK11629 101 -DFTALENVAMPL--LIGKKKPAEINSRALEMLAavGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
1MT0_A 172 YESEHVIMRNMHKI--CKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQ 218
Cdd:PRK11629 178 ARNADSIFQLLGELnrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
19-215 |
3.76e-24 |
|
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: 94.81 E-value: 3.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADP-NWLRRQVGVV----LQDNVLLNRSI 93
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVpedrKREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 94 IDNISLanpgmsvekviyaaklagahdfiselregyntivgeqGAGLSGGQRQRIAIARALVNNPKILIFDEATSALDYE 173
Cdd:cd03215 96 AENIAL-------------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
1MT0_A 174 SEHVIMRNMHKIC-KGRTVIIIAHRLSTV-KNADRIIVMEKGKI 215
Cdd:cd03215 139 AKAEIYRLIRELAdAGKAVLLISSELDELlGLCDRILVMYEGRI 182
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
5-235 |
6.41e-24 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 95.69 E-value: 6.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 5 RNIRFRYKpdSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLAlADPNWLRRQVGVVL- 83
Cdd:cd03218 4 ENLSKRYG--KRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDIT-KLPMHKRARLGIGYl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 84 --QDNVLLNRSIIDNISLANPGMSVEKVIYAAKLagaHDFISELreGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKIL 161
Cdd:cd03218 81 pqEASIFRKLTVEENILAVLEIRGLSKKEREEKL---EELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1MT0_A 162 IFDEATSALDYESEHVImRNMHKICKGRT--VIIIAHRLS-TVKNADRIIVMEKGKIVEQGKHKELLSEPESLYSYL 235
Cdd:cd03218 156 LLDEPFAGVDPIAVQDI-QKIIKILKDRGigVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYL 231
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-226 |
1.27e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 99.04 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRY--KPDSPViLDNINLSIKQGEVIGIVGRSGSGKSTL-TKLIQRFYIPENGQVLIDGhdlaladpnwlrrQ 78
Cdd:PLN03130 615 ISIKNGYFSWdsKAERPT-LSNINLDVPVGSLVAIVGSTGEGKTSLiSAMLGELPPRSDASVVIRG-------------T 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 79 VGVVLQDNVLLNRSIIDNISLANPGMSV--EKVIYAAKLAgaHDfISELREGYNTIVGEQGAGLSGGQRQRIAIARALVN 156
Cdd:PLN03130 681 VAYVPQVSWIFNATVRDNILFGSPFDPEryERAIDVTALQ--HD-LDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYS 757
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1MT0_A 157 NPKILIFDEATSALDyesEHViMRNMHKIC-----KGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLS 226
Cdd:PLN03130 758 NSDVYIFDDPLSALD---AHV-GRQVFDKCikdelRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSN 828
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
18-227 |
1.97e-23 |
|
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: 93.36 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 18 ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRF--YIPENGQVLIDGHDLALADPNwLRRQVGVVL--QDNVllnrsi 93
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGIFLafQYPP------ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 94 idnislANPGMSVEkviyaaklagahDFISELREGyntivgeqgagLSGGQRQRIAIARALVNNPKILIFDEATSALDYE 173
Cdd:cd03217 88 ------EIPGVKNA------------DFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDID 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
1MT0_A 174 SEHVIMRNMHKIC-KGRTVIIIAH--RLSTVKNADRIIVMEKGKIVEQGKhKELLSE 227
Cdd:cd03217 139 ALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD-KELALE 194
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
18-217 |
3.34e-23 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 93.48 E-value: 3.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 18 ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFY--IPENGQVlidghdlaladpnwlrrqvgVVLQDNVLLNRSIID 95
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCV--------------------DVPDNQFGREASLID 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 96 NISLANPGMSVEKVIYAAKLAGAHDFISELREgyntivgeqgagLSGGQRQRIAIARALVNNPKILIFDEATSALDYESE 175
Cdd:COG2401 105 AIGRKGDFKDAVELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
1MT0_A 176 HVIMRNMHKICK--GRTVIIIAHRlSTVKNA---DRIIVMEKGKIVE 217
Cdd:COG2401 173 KRVARNLQKLARraGITLVVATHH-YDVIDDlqpDLLIFVGYGGVPE 218
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-231 |
3.81e-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: 94.54 E-value: 3.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPEnGQVLIDGHDLALADPNWLRRQVGV 81
Cdd:cd03289 3 MTVKDLTAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLNRSIIDNISlANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKIL 161
Cdd:cd03289 82 IPQKVFIFSGTFRKNLD-PYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 162 IFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEPESL 231
Cdd:cd03289 161 LLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
7-233 |
6.98e-23 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 96.70 E-value: 6.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 7 IRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFyIPE------NGQVLIDGHDLALADPNWLRR--- 77
Cdd:PRK15134 13 VAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRL-LPSppvvypSGDIRFHGESLLHASEQTLRGvrg 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 78 -QVGVVLQDNVllnrsiidnISLaNPGMSVEKVIYAA--------KLAGAHDFISELREgyntiVG-EQGAG-------- 139
Cdd:PRK15134 92 nKIAMIFQEPM---------VSL-NPLHTLEKQLYEVlslhrgmrREAARGEILNCLDR-----VGiRQAAKrltdyphq 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 140 LSGGQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKN-ADRIIVMEKGKIV 216
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKlADRVAVMQNGRCV 236
|
250
....*....|....*..
1MT0_A 217 EQGKHKELLSEPESLYS 233
Cdd:PRK15134 237 EQNRAATLFSAPTHPYT 253
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-224 |
7.04e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 96.97 E-value: 7.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRY--KPDSPViLDNINLSIKQGEVIGIVGRSGSGKSTL-TKLIQRFYIPENGQVLIDGhdlaladpnwlrrQ 78
Cdd:PLN03232 615 ISIKNGYFSWdsKTSKPT-LSDINLEIPVGSLVAIVGGTGEGKTSLiSAMLGELSHAETSSVVIRG-------------S 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 79 VGVVLQDNVLLNRSIIDNISLanpGMSVEKVIYAAKL---AGAHDFisELREGYN-TIVGEQGAGLSGGQRQRIAIARAL 154
Cdd:PLN03232 681 VAYVPQVSWIFNATVRENILF---GSDFESERYWRAIdvtALQHDL--DLLPGRDlTEIGERGVNISGGQKQRVSMARAV 755
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1MT0_A 155 VNNPKILIFDEATSALDYESEHVIMRN-MHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKEL 224
Cdd:PLN03232 756 YSNSDIYIFDDPLSALDAHVAHQVFDScMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-216 |
8.65e-23 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 96.24 E-value: 8.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQvGVVL------QDNVLLNRS 92
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRA-GIAYvpedrkGEGLVLDLS 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 93 IIDNISLAN-PGMSVEKVI-YAAKLAGAHDFISELR---EGYNTIVGEqgagLSGGQRQRIAIARALVNNPKILIFDEAT 167
Cdd:COG1129 347 IRENITLASlDRLSRGGLLdRRRERALAEEYIKRLRiktPSPEQPVGN----LSGGNQQKVVLAKWLATDPKVLILDEPT 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
1MT0_A 168 SALDYESEHVIMRNMHKICK-GRTVIIIahrlST-----VKNADRIIVMEKGKIV 216
Cdd:COG1129 423 RGIDVGAKAEIYRLIRELAAeGKAVIVI----SSelpelLGLSDRILVMREGRIV 473
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
9-219 |
1.03e-22 |
|
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: 92.40 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 9 FRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHdLALADPNWLRRQVGVVL-QDNV 87
Cdd:cd03267 27 FKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL-VPWKRRKKFLRRIGVVFgQKTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 88 LL-NRSIIDNISLANPGMSVEKVIYAAKLAGAHDFIsELREGYNTIVGEqgagLSGGQRQRIAIARALVNNPKILIFDEA 166
Cdd:cd03267 106 LWwDLPVIDSFYLLAAIYDLPPARFKKRLDELSELL-DLEELLDTPVRQ----LSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
1MT0_A 167 TSALDYESEHVIMRNMHKICKGR--TVIIIAHRLSTV-KNADRIIVMEKGKIVEQG 219
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
3-171 |
1.67e-22 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 91.39 E-value: 1.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 3 TFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPE---NGQVLIDGHDLALADPnwLRRQV 79
Cdd:COG4136 3 SLENLTITL--GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPA--EQRRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 80 GVVLQDNVLL-NRSIIDNISLANPG--------MSVEKVIYAAKLAG-AHDFISELregyntivgeqgaglSGGQRQRIA 149
Cdd:COG4136 79 GILFQDDLLFpHLSVGENLAFALPPtigraqrrARVEQALEEAGLAGfADRDPATL---------------SGGQRARVA 143
|
170 180
....*....|....*....|..
1MT0_A 150 IARALVNNPKILIFDEATSALD 171
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLD 165
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-226 |
2.37e-22 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 95.04 E-value: 2.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGV 81
Cdd:PRK10522 323 LELRNVTFAY-QDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLNRsiidnisLANP-GMSVEKVIYAA---------KLAGAHDFISELRegyntivgeqgagLSGGQRQRIAIA 151
Cdd:PRK10522 402 VFTDFHLFDQ-------LLGPeGKPANPALVEKwlerlkmahKLELEDGRISNLK-------------LSKGQKKRLALL 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 152 RALVNNPKILIFDEATSALD-------YESEHVIMRNMhkickGRTVIIIAHRLSTVKNADRIIVMEKGKIVE-QGKHKE 223
Cdd:PRK10522 462 LALAEERDILLLDEWAADQDphfrrefYQVLLPLLQEM-----GKTIFAISHDDHYFIHADRLLEMRNGQLSElTGEERD 536
|
...
1MT0_A 224 LLS 226
Cdd:PRK10522 537 AAS 539
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
16-213 |
3.20e-22 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 90.96 E-value: 3.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 16 PViLDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGH----DLALADPN---WLRRQ-VGVVLQD-N 86
Cdd:COG4778 25 PV-LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPReilALRRRtIGYVSQFlR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 87 VLLNRSIIDNIslANP----GMSVEkviyaAKLAGAHDFISELRegyntiVGEQGAGL-----SGGQRQRIAIARALVNN 157
Cdd:COG4778 104 VIPRVSALDVV--AEPllerGVDRE-----EARARARELLARLN------LPERLWDLppatfSGGEQQRVNIARGFIAD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
1MT0_A 158 PKILIFDEATSALDYESEHVIMRNMHKIC-KGRTVIIIAHRLSTVKN-ADRIIVMEKG 213
Cdd:COG4778 171 PPLLLLDEPTASLDAANRAVVVELIEEAKaRGTAIIGIFHDEEVREAvADRVVDVTPF 228
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
21-228 |
3.37e-22 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 91.77 E-value: 3.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 21 NINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGVVLQD--NVLLNRSIIDNIs 98
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDpsTSLNPRQRISQI- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 99 LANP--------GMSVEKVIYAAklagahdfiseLREgyntiVG--EQGAG-----LSGGQRQRIAIARALVNNPKILIF 163
Cdd:PRK15112 110 LDFPlrlntdlePEQREKQIIET-----------LRQ-----VGllPDHASyyphmLAPGQKQRLGLARALILRPKVIIA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1MT0_A 164 DEATSALDYESEHVIMRNMHKI--CKGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLSEP 228
Cdd:PRK15112 174 DEALASLDMSMRSQLINLMLELqeKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLASP 241
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-228 |
4.32e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 91.64 E-value: 4.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPEN-----GQVLIDGHDL--ALADPNW 74
Cdd:PRK14258 8 IKVNNLSFYY--DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 75 LRRQVGVVLQDNVLLNRSIIDNISLA------NPGMSVEKVIYAAKLAgahdfiSELREGYNTIVGEQGAGLSGGQRQRI 148
Cdd:PRK14258 86 LRRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEIDDIVESALKD------ADLWDEIKHKIHKSALDLSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 149 AIARALVNNPKILIFDEATSALD----YESEHVImrNMHKICKGRTVIIIAHRLSTVK-----------NADRIivmekG 213
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDpiasMKVESLI--QSLRLRSELTMVIVSHNLHQVSrlsdftaffkgNENRI-----G 232
|
250
....*....|....*
1MT0_A 214 KIVEQGKHKELLSEP 228
Cdd:PRK14258 233 QLVEFGLTKKIFNSP 247
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
5-233 |
5.20e-22 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 92.48 E-value: 5.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 5 RNIRFRYK-PDSPVILDN-INLSIKQGEVIGIVGRSGSGKS----TLTKLIQRfyipeNGQV----LIDGHD---LALAD 71
Cdd:PRK09473 16 KDLRVTFStPDGDVTAVNdLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-----NGRIggsaTFNGREilnLPEKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 72 PNWLR-RQVGVVLQDNVllnrsiidnISLaNPGMSV-----EKVIYAAKLAGAHDF-----------ISELREGYNTIVG 134
Cdd:PRK09473 91 LNKLRaEQISMIFQDPM---------TSL-NPYMRVgeqlmEVLMLHKGMSKAEAFeesvrmldavkMPEARKRMKMYPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 135 EqgagLSGGQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKN-ADRIIVME 211
Cdd:PRK09473 161 E----FSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMY 236
|
250 260
....*....|....*....|..
1MT0_A 212 KGKIVEQGKHKELLSEPESLYS 233
Cdd:PRK09473 237 AGRTMEYGNARDVFYQPSHPYS 258
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-235 |
5.32e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 91.14 E-value: 5.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 5 RNIRFRYKPDspVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHD--------LALADPNWL- 75
Cdd:PRK11701 10 RGLTKLYGPR--KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrdlyaLSEAERRRLl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 76 RRQVGVVLQ---DNVLLNRSIIDNIslANPGMSVEKVIYAAKLAGAHDFISELREGYNTIvGEQGAGLSGGQRQRIAIAR 152
Cdd:PRK11701 88 RTEWGFVHQhprDGLRMQVSAGGNI--GERLMAVGARHYGDIRATAGDWLERVEIDAARI-DDLPTTFSGGMQQRLQIAR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 153 ALVNNPKILIFDEATSALDYESEHVIM-------RNMhkickGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKEL 224
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDVSVQARLLdllrglvREL-----GLAVVIVTHDLAVARLlAHRLLVMKQGRVVESGLTDQV 239
|
250
....*....|.
1MT0_A 225 LSEPESLYSYL 235
Cdd:PRK11701 240 LDDPQHPYTQL 250
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-233 |
6.36e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 92.11 E-value: 6.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFyIPENGQVL-----IDGHDLALADPNWLRRQVG----VVLQDNVL- 88
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGL-IDYPGRVMaekleFNGQDLQRISEKERRNLVGaevaMIFQDPMTs 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 89 LNRS------IIDNISL---ANPGMSVEKVIYAAKLAGAHDFISELregynTIVGEQgagLSGGQRQRIAIARALVNNPK 159
Cdd:PRK11022 102 LNPCytvgfqIMEAIKVhqgGNKKTRRQRAIDLLNQVGIPDPASRL-----DVYPHQ---LSGGMSQRVMIAMAIACRPK 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 160 ILIFDEATSALDYESEHVIM---------RNMhkickgrTVIIIAHRLSTV-KNADRIIVMEKGKIVEQGKHKELLSEPE 229
Cdd:PRK11022 174 LLIADEPTTALDVTIQAQIIelllelqqkENM-------ALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDIFRAPR 246
|
....
1MT0_A 230 SLYS 233
Cdd:PRK11022 247 HPYT 250
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
19-237 |
1.64e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 90.07 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTK----LIQRFYIPENgQVLIDGHDLALA-----DPNWLRRQVGVVLQDNVLL 89
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGS-HIELLGRTVQREgrlarDIRKSRANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 90 NR-SIIDNISLANPGMSV---EKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKILIFDE 165
Cdd:PRK09984 99 NRlSVLENVLIGALGSTPfwrTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1MT0_A 166 ATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLS-TVKNADRIIVMEKGKIVEQGKHKELLSEPeslYSYLYQ 237
Cdd:PRK09984 179 PIASLDPESARIVMDTLRDINQndGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNER---FDHLYR 250
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
13-228 |
2.11e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 90.74 E-value: 2.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 13 PDSPV-ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFyIPENGQVLID-----GHDLALADP----NWLRRQVGVV 82
Cdd:COG4170 16 PQGRVkAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGI-TKDNWHVTADrfrwnGIDLLKLSPrerrKIIGREIAMI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 83 LQD-------NVLLNRSIIDNIslanPGMSVEKVIYAAKLAGAHDFISEL-REG---YNTIVGEQGAGLSGGQRQRIAIA 151
Cdd:COG4170 95 FQEpsscldpSAKIGDQLIEAI----PSWTFKGKWWQRFKWRKKRAIELLhRVGikdHKDIMNSYPHELTEGECQKVMIA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 152 RALVNNPKILIFDEATSALDYESEHVIMR---NMHKIcKGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLSE 227
Cdd:COG4170 171 MAIANQPRLLIADEPTNAMESTTQAQIFRllaRLNQL-QGTSILLISHDLESISQwADTITVLYCGQTVESGPTEQILKS 249
|
.
1MT0_A 228 P 228
Cdd:COG4170 250 P 250
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-229 |
2.51e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 89.13 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSpvILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFyIPEN------GQVLIDGHDLAL--ADPN 73
Cdd:PRK14267 5 IETVNLRVYYGSNH--VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRL-LELNeearveGEVRLFGRNIYSpdVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 74 WLRRQVGVVLQ-DNVLLNRSIIDNIS-------LANPGMSV-EKVIYAAKLAGAHDfisELREGYNtivgEQGAGLSGGQ 144
Cdd:PRK14267 82 EVRREVGMVFQyPNPFPHLTIYDNVAigvklngLVKSKKELdERVEWALKKAALWD---EVKDRLN----DYPSNLSGGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 145 RQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHR-LSTVKNADRIIVMEKGKIVEQGKHKE 223
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRK 234
|
....*.
1MT0_A 224 LLSEPE 229
Cdd:PRK14267 235 VFENPE 240
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
10-228 |
2.55e-21 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 92.53 E-value: 2.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 10 RYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTK-LIQRFYIPEnGQVlidghdlaladpnWLRRQVGVVLQDNVL 88
Cdd:PTZ00243 667 FFELEPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQsLLSQFEISE-GRV-------------WAERSIAYVPQQAWI 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 89 LNRSIIDNISLANPgmsvEKviyAAKLAGA-------HDfISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKIL 161
Cdd:PTZ00243 733 MNATVRGNILFFDE----ED---AARLADAvrvsqleAD-LAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVY 804
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1MT0_A 162 IFDEATSALDyesEHVIMRNMHKICKGR----TVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEP 228
Cdd:PTZ00243 805 LLDDPLSALD---AHVGERVVEECFLGAlagkTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-229 |
1.29e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 87.84 E-value: 1.29e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 18 ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFY-----IPENGQVLIDGHDL-ALADPNWLRRQVGVVLQDNVLLNR 91
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNdkvsgYRYSGDVLLGGRSIfNYRDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 92 SIIDNIsLAnpGMSVEKVIYAAKLAG-AHDFISE--LREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKILIFDEATS 168
Cdd:PRK14271 116 SIMDNV-LA--GVRAHKLVPRKEFRGvAQARLTEvgLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
1MT0_A 169 ALDYESEHVIMRNMHKICKGRTVIIIAHRLS-TVKNADRIIVMEKGKIVEQGKHKELLSEPE 229
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFSSPK 254
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
19-198 |
1.71e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 87.14 E-value: 1.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRF--YIPE---NGQVLIDGHDL--ALADPNWLRRQVGVVLQDNVLLNR 91
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNLyaPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 92 SIIDNISlanpgmsvekviYAAKLAGAHDFISELREG----------YNTIVGEQGAGLSGGQRQRIAIARALVNNPKIL 161
Cdd:PRK14243 106 SIYDNIA------------YGARINGYKGDMDELVERslrqaalwdeVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVI 173
|
170 180 190
....*....|....*....|....*....|....*..
1MT0_A 162 IFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRL 198
Cdd:PRK14243 174 LMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-232 |
1.74e-20 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 87.15 E-value: 1.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 1 DITF--RNIRFRYkPDSpVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQ 78
Cdd:PRK10575 9 DTTFalRNVSFRV-PGR-TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 79 VGVVLQDnvllnrsiidniSLANPGMSV-----------------------EKVIYAAKLAGAHDFISELREgyntivge 135
Cdd:PRK10575 87 VAYLPQQ------------LPAAEGMTVrelvaigrypwhgalgrfgaadrEKVEEAISLVGLKPLAHRLVD-------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 136 qgaGLSGGQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKIC--KGRTVIIIAHRLS-TVKNADRIIVMEK 212
Cdd:PRK10575 147 ---SLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSqeRGLTVIAVLHDINmAARYCDYLVALRG 223
|
250 260
....*....|....*....|..
1MT0_A 213 GKIVEQGKHKELLSEP--ESLY 232
Cdd:PRK10575 224 GEMIAQGTPAELMRGEtlEQIY 245
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
2-217 |
1.94e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIdGHDLaladpnwlrrQVGV 81
Cdd:COG0488 316 LELEGLSKSY--GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLL--NRSIIDNISLANPGMsveKVIYAAKLAGAHDFISELREgynTIVGEqgagLSGGQRQRIAIARALVNNPK 159
Cdd:COG0488 383 FDQHQEELdpDKTVLDELRDGAPGG---TEQEVRGYLGRFLFSGDDAF---KPVGV----LSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
1MT0_A 160 ILIFDEATSALDYES----EHVIMRnmhkiCKGrTVIIIAH-R--LSTVknADRIIVMEKGKIVE 217
Cdd:COG0488 453 VLLLDEPTNHLDIETlealEEALDD-----FPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
14-229 |
2.00e-20 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 89.48 E-value: 2.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 14 DSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRF--YIPENGQVL------------------------------ 61
Cdd:TIGR03269 11 DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvgepcpvcggtle 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 62 ---IDGHDLALADPNWLRRQVGVVLQDNVLL--NRSIIDNI--SLANPGMSVEKVIYAAKlagahDFISELREGYNtiVG 134
Cdd:TIGR03269 91 peeVDFWNLSDKLRRRIRKRIAIMLQRTFALygDDTVLDNVleALEEIGYEGKEAVGRAV-----DLIEMVQLSHR--IT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 135 EQGAGLSGGQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKN-ADRIIVME 211
Cdd:TIGR03269 164 HIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKasGISMVLTSHWPEVIEDlSDKAIWLE 243
|
250 260
....*....|....*....|....*
1MT0_A 212 KGKIVEQG-------KHKELLSEPE 229
Cdd:TIGR03269 244 NGEIKEEGtpdevvaVFMEGVSEVE 268
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
5-213 |
4.00e-20 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 89.01 E-value: 4.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 5 RNIRF--RYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTK-LIQRF---YIpENGQVLIDGHDLalaDPNWLRRq 78
Cdd:TIGR00956 763 RNLTYevKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNvLAERVttgVI-TGGDRLVNGRPL---DSSFQRS- 837
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 79 VGVVLQDNVLLNRSII-------------DNISLANPGMSVEKVIYaaklagahdfISELREGYNTIVGEQGAGLSGGQR 145
Cdd:TIGR00956 838 IGYVQQQDLHLPTSTVreslrfsaylrqpKSVSKSEKMEYVEEVIK----------LLEMESYADAVVGVPGEGLNVEQR 907
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1MT0_A 146 QRIAIARALVNNPKILIF-DEATSALDYESEHVIMRNMHKICK-GRTVIIIAHRLSTVKNA--DRIIVMEKG 213
Cdd:TIGR00956 908 KRLTIGVELVAKPKLLLFlDEPTSGLDSQTAWSICKLMRKLADhGQAILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
15-240 |
4.10e-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: 86.45 E-value: 4.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 15 SPViLDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGhdlaladpnwlrrQVGVVLQDNVLLNRSII 94
Cdd:cd03291 50 APV-LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-------------RISFSSQFSWIMPGTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 95 DNISLanpGMSVEK-----VIYAAKLagaHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKILIFDEATSA 169
Cdd:cd03291 116 ENIIF---GVSYDEyryksVVKACQL---EEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGY 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1MT0_A 170 LDYESEHVIMRN-MHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEPESLYSYLYQLQS 240
Cdd:cd03291 190 LDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKLMGYDT 261
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
20-235 |
4.56e-20 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 85.81 E-value: 4.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 20 DNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLAlADPNWLRRQVGVV--LQdNVLLNRS--IID 95
Cdd:PRK11300 22 NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE-GLPGHQIARMGVVrtFQ-HVRLFREmtVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 96 NISLANPGMSVEKVIY------------AAKLAGAHDFISelREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKILIF 163
Cdd:PRK11300 100 NLLVAQHQQLKTGLFSgllktpafrraeSEALDRAATWLE--RVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1MT0_A 164 DEATSALD----YESEHVI--MRNMHKIckgrTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLSEPESLYSYL 235
Cdd:PRK11300 178 DEPAAGLNpketKELDELIaeLRNEHNV----TVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEIRNNPDVIKAYL 252
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-240 |
4.63e-20 |
|
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: 88.81 E-value: 4.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 4 FRNIRFRYKPdspvILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGhdlaladpnwlrrQVGVVL 83
Cdd:TIGR01271 431 FSNFSLYVTP----VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-------------RISFSP 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 84 QDNVLLNRSIIDNISLanpGMSVEK-----VIYAAKLagaHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNP 158
Cdd:TIGR01271 494 QTSWIMPGTIKDNIIF---GLSYDEyrytsVIKACQL---EEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDA 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 159 KILIFDEATSALDYESEHVIM-RNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSEPESLYSYLYQ 237
Cdd:TIGR01271 568 DLYLLDSPFTHLDVVTEKEIFeSCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLLG 647
|
...
1MT0_A 238 LQS 240
Cdd:TIGR01271 648 LEA 650
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
17-224 |
4.64e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.18 E-value: 4.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 17 VILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNwLRRQVGVVL--QDNVLL-NRSI 93
Cdd:PRK15439 25 EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIYLvpQEPLLFpNLSV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 94 IDNI--SLANPGMSVEKViyAAKLAgahdfisELREGYNTIVgeQGAGLSGGQRQRIAIARALVNNPKILIFDEATSALD 171
Cdd:PRK15439 104 KENIlfGLPKRQASMQKM--KQLLA-------ALGCQLDLDS--SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
1MT0_A 172 -YESEHVIMRNMHKICKGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKEL 224
Cdd:PRK15439 173 pAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-214 |
7.13e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 87.68 E-value: 7.13e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYiPE---NGQVLIDGHDLALADpnwLR--RQVGVVL--QDNVLL-N 90
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASN---IRdtERAGIAIihQELALVkE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 91 RSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELREGYN--TIVGEqgagLSGGQRQRIAIARALVNNPKILIFDEATS 168
Cdd:PRK13549 97 LSVLENIFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINpaTPVGN----LGLGQQQLVEIAKALNKQARLLILDEPTA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
1MT0_A 169 AL-DYESEHV--IMRNMHKicKGRTVIIIAHRLSTVKN-ADRIIVMEKGK 214
Cdd:PRK13549 173 SLtESETAVLldIIRDLKA--HGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-212 |
7.42e-20 |
|
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: 82.97 E-value: 7.42e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFrYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQ--------RFYIPENGQVL--------IDGH 65
Cdd:cd03223 1 IELENLSL-ATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAglwpwgsgRIGMPEGEDLLflpqrpylPLGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 66 dlaladpnwLRRQvgvvlqdnvllnrsiidnisLANPGMSVekviyaaklagahdfiselregyntivgeqgagLSGGQR 145
Cdd:cd03223 80 ---------LREQ--------------------LIYPWDDV---------------------------------LSGGEQ 97
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1MT0_A 146 QRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKicKGRTVIIIAHRLSTVKNADRIIVMEK 212
Cdd:cd03223 98 QRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKE--LGITVISVGHRPSLWKFHDRVLDLDG 162
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
9-231 |
1.11e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 85.06 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 9 FRYKpDSPViLDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWL--RRQVGVVLQD- 85
Cdd:PRK13638 9 FRYQ-DEPV-LKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLalRQQVATVFQDp 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 86 -NVLLNRSIIDNI--SLANPGMSVEKViyAAKLAGAHDFISELREGYNTIvgeqgAGLSGGQRQRIAIARALVNNPKILI 162
Cdd:PRK13638 87 eQQIFYTDIDSDIafSLRNLGVPEAEI--TRRVDEALTLVDAQHFRHQPI-----QCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1MT0_A 163 FDEATSALDYESEHVIMRNMHKIC-KGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLSEPESL 231
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVaQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFACTEAM 230
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-214 |
1.70e-19 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 81.73 E-value: 1.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGhdlaladpnwlRRQVGV 81
Cdd:cd03221 1 IELENLSKTY--GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGY 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQdnvllnrsiidnislanpgmsvekviyaaklagahdfiselregyntivgeqgagLSGGQRQRIAIARALVNNPKIL 161
Cdd:cd03221 68 FEQ-------------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
1MT0_A 162 IFDEATSALDYES-EHVImrNMHKICKGrTVIIIAH-R--LSTVknADRIIVMEKGK 214
Cdd:cd03221 93 LLDEPTNHLDLESiEALE--EALKEYPG-TVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
2-232 |
1.75e-19 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 85.67 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPVIlDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDG---HDLALADpnwlrRQ 78
Cdd:PRK11650 4 LKLQAVRKSYDGKTQVI-KGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGrvvNELEPAD-----RD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 79 VGVVLQDNVLL-NRSIIDNIS--LANPGMS----VEKVIYAAKlagahdfISEL--------REgyntivgeqgagLSGG 143
Cdd:PRK11650 78 IAMVFQNYALYpHMSVRENMAygLKIRGMPkaeiEERVAEAAR-------ILELeplldrkpRE------------LSGG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 144 QRQRIAIARALVNNPKILIFDEATSALDyESEHVIMR----NMHKickgrtviiiahRLST----VKN--------ADRI 207
Cdd:PRK11650 139 QRQRVAMGRAIVREPAVFLFDEPLSNLD-AKLRVQMRleiqRLHR------------RLKTtslyVTHdqveamtlADRV 205
|
250 260
....*....|....*....|....*.
1MT0_A 208 IVMEKGKIvEQ-GKHKELLSEPESLY 232
Cdd:PRK11650 206 VVMNGGVA-EQiGTPVEVYEKPASTF 230
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
18-228 |
2.17e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 86.05 E-value: 2.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 18 ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGVVLQDNVLL----NRSI 93
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLSfefdVRQV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 94 ID--------NISLANPG--MSVEKVIYAAKLA--GAHDFISelregyntivgeqgagLSGGQRQRIAIARALVNNPKIL 161
Cdd:PRK09536 98 VEmgrtphrsRFDTWTETdrAAVERAMERTGVAqfADRPVTS----------------LSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1MT0_A 162 IFDEATSALDYesEHVImRNMHKICK----GRTVIIIAHRLS-TVKNADRIIVMEKGKIVEQGKHKELLSEP 228
Cdd:PRK09536 162 LLDEPTASLDI--NHQV-RTLELVRRlvddGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-227 |
3.63e-19 |
|
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: 86.12 E-value: 3.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPEnGQVLIDGHDLALADPNWLRRQVGV 81
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGV 1296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLNRSIIDNISlANPGMSVEKVIYAAKLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKIL 161
Cdd:TIGR01271 1297 IPQKVFIFSGTFRKNLD-PYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKIL 1375
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1MT0_A 162 IFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQGKHKELLSE 227
Cdd:TIGR01271 1376 LLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNE 1441
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
2-219 |
4.55e-19 |
|
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: 81.93 E-value: 4.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNI--RFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLI---QRFYIPENGQVLIDGHDlALADPNWLR 76
Cdd:cd03233 4 LSWRNIsfTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrTEGNVSVEGDIHYNGIP-YKEFAEKYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 77 RQVGVVLQDNVllnrsiidnislANPGMSVEKVIYAAKLAGAHDFISelregyntivgeqgaGLSGGQRQRIAIARALVN 156
Cdd:cd03233 83 GEIIYVSEEDV------------HFPTLTVRETLDFALRCKGNEFVR---------------GISGGERKRVSIAEALVS 135
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
1MT0_A 157 NPKILIFDEATSALDYESEHVI---MRNMHKICKGRTVIII-AHRLSTVKNADRIIVMEKGKIVEQG 219
Cdd:cd03233 136 RASVLCWDNSTRGLDSSTALEIlkcIRTMADVLKTTTFVSLyQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
19-225 |
7.53e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 83.60 E-value: 7.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHdlalaDPnWLRR-----QVGVV----------- 82
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY-----VP-FKRRkefarRIGVVfgqrsqlwwdl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 83 -LQDNVLLNRSIIDnislanpgmsVEKVIYAAKLagahDFISE---LREGYNTIVGEqgagLSGGQRQRIAIARALVNNP 158
Cdd:COG4586 112 pAIDSFRLLKAIYR----------IPDAEYKKRL----DELVElldLGELLDTPVRQ----LSLGQRMRCELAAALLHRP 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 159 KILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELL 225
Cdd:COG4586 174 KILFLDEPTIGLDVVSKEAIREFLKEYNRerGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELK 243
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
17-226 |
8.16e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 82.73 E-value: 8.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 17 VILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGVVLQDnvllnrsiidn 96
Cdd:PRK10253 21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN----------- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 97 isLANPG-MSVEKVIYAAKLAGAHDFISELRE------------GYNTIVGEQGAGLSGGQRQRIAIARALVNNPKILIF 163
Cdd:PRK10253 90 --ATTPGdITVQELVARGRYPHQPLFTRWRKEdeeavtkamqatGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1MT0_A 164 DEATSALDYESEHVIMRNMHKI--CKGRTVIIIAHRLS-TVKNADRIIVMEKGKIVEQGKHKELLS 226
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELnrEKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVT 233
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
2-213 |
1.13e-18 |
|
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: 80.75 E-value: 1.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRY--KPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTK-LIQRF---YIpeNGQVLIDGHDLalaDPNwL 75
Cdd:cd03232 4 LTWKNLNYTVpvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDvLAGRKtagVI--TGEILINGRPL---DKN-F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 76 RRQVGVVLQDNVLlnrsiidnislaNPGMSVEKVIyaaklagahDFISELRegyntivgeqgaGLSGGQRQRIAIARALV 155
Cdd:cd03232 78 QRSTGYVEQQDVH------------SPNLTVREAL---------RFSALLR------------GLSVEQRKRLTIGVELA 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
1MT0_A 156 NNPKILIFDEATSALDYESEHVIMRNMHKIC-KGRTVIIIAHRLSTV--KNADRIIVMEKG 213
Cdd:cd03232 125 AKPSILFLDEPTSGLDSQAAYNIVRFLKKLAdSGQAILCTIHQPSASifEKFDRLLLLKRG 185
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
18-231 |
1.32e-18 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 84.16 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 18 ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPEN--GQVLIDGHDLAladpNWLRRQVGVVLQDNVLLN----R 91
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT----KQILKRTGFVTQDDILYPhltvR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 92 SIIDNISLANPGMSVEKviyAAKLAGAHDFISEL--REGYNTIVGEQGA-GLSGGQRQRIAIARALVNNPKILIFDEATS 168
Cdd:PLN03211 159 ETLVFCSLLRLPKSLTK---QEKILVAESVISELglTKCENTIIGNSFIrGISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1MT0_A 169 ALDYESEHVIMRNMHKIC-KGRTVIIIAHRLST--VKNADRIIVMEKGKIVEQGKHKELLSEPESL 231
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAqKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMAYFESV 301
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4-223 |
2.11e-18 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 84.00 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 4 FRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLI----QRFYIPENGQVLIDGHDLALADPNWLRRQV 79
Cdd:TIGR00956 62 FRKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIKKHYRGDVV 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 80 GVVLQDNVLLNRSIIDNISLA-------NPGMSVEKVIYAAKLAGAHDFISELREGYNTIVG-EQGAGLSGGQRQRIAIA 151
Cdd:TIGR00956 142 YNAETDVHFPHLTVGETLDFAarcktpqNRPDGVSREEYAKHIADVYMATYGLSHTRNTKVGnDFVRGVSGGERKRVSIA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 152 RALVNNPKILIFDEATSALDYESEHVIMRNMhkickgRTVIIIAHRLSTV------KNA----DRIIVMEKGKIVEQGKH 221
Cdd:TIGR00956 222 EASLGGAKIQCWDNATRGLDSATALEFIRAL------KTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGYQIYFGPA 295
|
..
1MT0_A 222 KE 223
Cdd:TIGR00956 296 DK 297
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-224 |
2.30e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 83.30 E-value: 2.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNwLRRQ--VGVVLQDNVLLNR-SIID 95
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQlgIGIIYQELSVIDElTVLE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 96 NI----SLANPGMSVEKVIYAAKLAGAHDFIseLREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKILIFDEATSAL- 170
Cdd:PRK09700 100 NLyigrHLTKKVCGVNIIDWREMRVRAAMML--LRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLt 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
1MT0_A 171 DYESEHV--IMRNMHKicKGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKEL 224
Cdd:PRK09700 178 NKEVDYLflIMNQLRK--EGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSGMVSDV 232
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
16-230 |
3.23e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 80.90 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 16 PVILDNINLSIKQGEVIGIVGRSGSGKStLTKLIQRFYIPE-----NGQVLIDGHDLALADpnwLR-RQVGVVLQDNvll 89
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKS-LTCAAALGILPAgvrqtAGRVLLDGKPVAPCA---LRgRKIATIMQNP--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 90 nRSIIdnislaNP--GM---SVEKVIYAAKLAGAHDFISELREgyntiVGEQGAG---------LSGGQRQRIAIARALV 155
Cdd:PRK10418 89 -RSAF------NPlhTMhthARETCLALGKPADDATLTAALEA-----VGLENAArvlklypfeMSGGMLQRMMIALALL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1MT0_A 156 NNPKILIFDEATSALDYESEHVIMRNMHKICKGRT--VIIIAHRLSTV-KNADRIIVMEKGKIVEQGKHKELLSEPES 230
Cdd:PRK10418 157 CEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETLFNAPKH 234
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
19-217 |
5.70e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 82.27 E-value: 5.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADP-NWLRRQVGVVLQDNVLLnrsiidni 97
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTtAALAAGVAIIYQELHLV-------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 98 slanPGMSVEKVIYAAKLAGAHDFI--SELREGyntiVGEQGAG-------------LSGGQRQRIAIARALVNNPKILI 162
Cdd:PRK11288 92 ----PEMTVAENLYLGQLPHKGGIVnrRLLNYE----AREQLEHlgvdidpdtplkyLSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
1MT0_A 163 FDEATSALDY-ESEHV--IMRNMHKicKGRTVIIIAHRLSTV-KNADRIIVMEKGKIVE 217
Cdd:PRK11288 164 FDEPTSSLSArEIEQLfrVIRELRA--EGRVILYVSHRMEEIfALCDAITVFKDGRYVA 220
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
11-215 |
1.50e-17 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 81.13 E-value: 1.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 11 YKPDSPVI--LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPEN-GQVLIDGHDLALADPNWLRRQvGVVL---- 83
Cdd:PRK13549 268 WDPVNPHIkrVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKIRNPQQAIAQ-GIAMvped 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 84 --QDNVLLNRSIIDNISLAN----PGMSVekVIYAAKLAGAHDFISELRegYNTIVGEQG-AGLSGGQRQRIAIARALVN 156
Cdd:PRK13549 347 rkRDGIVPVMGVGKNITLAAldrfTGGSR--IDDAAELKTILESIQRLK--VKTASPELAiARLSGGNQQKAVLAKCLLL 422
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
1MT0_A 157 NPKILIFDEATSALDYESEHVIMRNMHKICK-GRTVIIIAHRLSTVKN-ADRIIVMEKGKI 215
Cdd:PRK13549 423 NPKILILDEPTRGIDVGAKYEIYKLINQLVQqGVAIIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
10-216 |
1.54e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.84 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 10 RYKPDSPVI-LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQ---------- 78
Cdd:COG3845 264 SVRDDRGVPaLKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgvayipedrl 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 79 -VGVV----LQDNVLLNRsiIDNISLANPGMSVEKVI--YAAKLAGAHDfiseLR-EGYNTIVGeqgaGLSGGQRQRIAI 150
Cdd:COG3845 344 gRGLVpdmsVAENLILGR--YRRPPFSRGGFLDRKAIraFAEELIEEFD----VRtPGPDTPAR----SLSGGNQQKVIL 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1MT0_A 151 ARALVNNPKILIFDEATSALDYES-----EHVI-MRNmhkicKGRTVIIIAHRLSTVKN-ADRIIVMEKGKIV 216
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLDVGAiefihQRLLeLRD-----AGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-233 |
1.59e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.05 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 6 NIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLidghdlalADPNWLRRQ------- 78
Cdd:PRK10261 19 NIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQ--------CDKMLLRRRsrqviel 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 79 ---------------VGVVLQDNVL-LN------RSIIDNISLaNPGMSVEKVIYAAKLAGAHDFISELRegynTIVGEQ 136
Cdd:PRK10261 91 seqsaaqmrhvrgadMAMIFQEPMTsLNpvftvgEQIAESIRL-HQGASREEAMVEAKRMLDQVRIPEAQ----TILSRY 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 137 GAGLSGGQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICKGRT--VIIIAHRLSTVKN-ADRIIVMEKG 213
Cdd:PRK10261 166 PHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEiADRVLVMYQG 245
|
250 260
....*....|....*....|
1MT0_A 214 KIVEQGKHKELLSEPESLYS 233
Cdd:PRK10261 246 EAVETGSVEQIFHAPQHPYT 265
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
18-235 |
1.61e-17 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.78 E-value: 1.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 18 ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNW-LRRQVGVVLQDNVLLNR-SIID 95
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFRRlSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 96 NIslanpgMSVEKVIYAAKLAGAHDFISELREGYNT--IVGEQGAGLSGGQRQRIAIARALVNNPKILIFDEATSALDYE 173
Cdd:PRK10895 98 NL------MAVLQIRDDLSAEQREDRANELMEEFHIehLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
1MT0_A 174 SEHVIMRNM-HKICKGRTVIIIAHRL-STVKNADRIIVMEKGKIVEQGKHKELLSEPESLYSYL 235
Cdd:PRK10895 172 SVIDIKRIIeHLRDSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYL 235
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-219 |
1.65e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 81.21 E-value: 1.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLAlADPNWLRRQVGV 81
Cdd:TIGR01257 929 VCVKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE-TNLDAVRQSLGM 1007
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVLLNRSIIdnislanpgmsVEKVIYAAKLAGAHDFISELR-------EGYNTIVGEQGAGLSGGQRQRIAIARAL 154
Cdd:TIGR01257 1008 CPQHNILFHHLTV-----------AEHILFYAQLKGRSWEEAQLEmeamledTGLHHKRNEEAQDLSGGMQRKLSVAIAF 1076
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1MT0_A 155 VNNPKILIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQG 219
Cdd:TIGR01257 1077 VGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSG 1142
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-210 |
2.09e-17 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 77.27 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 13 PDSPViLDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHD--------LALAD--PNWLRRQVGVV 82
Cdd:NF040873 3 GGRPV-LHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGArvayvpqrSEVPDslPLTVRDLVAMG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 83 L-QDNVLLNRSIIDNISLANPGMsvEKViyaaklaGAHDFiselregyntiVGEQGAGLSGGQRQRIAIARALVNNPKIL 161
Cdd:NF040873 82 RwARRGLWRRLTRDDRAAVDDAL--ERV-------GLADL-----------AGRQLGELSGGQRQRALLAQGLAQEADLL 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
1MT0_A 162 IFDEATSALDYESE---HVIMRNMHKicKGRTVIIIAHRLSTVKNADRIIVM 210
Cdd:NF040873 142 LLDEPTTGLDAESReriIALLAEEHA--RGATVVVVTHDLELVRRADPCVLL 191
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-233 |
2.53e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 80.67 E-value: 2.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWL---RRQVGVVLQD-------NVL 88
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLqalRRDIQFIFQDpyasldpRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 89 LNRSIIDNI---SLANPGMSVEKVIYAAKLAG---------AHDFiselregyntivgeqgaglSGGQRQRIAIARALVN 156
Cdd:PRK10261 420 VGDSIMEPLrvhGLLPGKAAAARVAWLLERVGllpehawryPHEF-------------------SGGQRQRICIARALAL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 157 NPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLSEPESLYS 233
Cdd:PRK10261 481 NPKVIIADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIGPRRAVFENPQHPYT 560
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
21-220 |
1.03e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.99 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 21 NINLSIKQGEVIGIVGRSGSGKSTLTKLI------QRFYIPENGQVLIDGH-DLALAdPNwlRRQVGVVLQDNVLLnrsi 93
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAIsgltrpQKGRIVLNGRVLFDAEkGICLP-PE--KRRIGYVFQDARLF---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 94 idnislanPGMSVEKVI---YAAKLAGAHDFISELReGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKILIFDEATSAL 170
Cdd:PRK11144 89 --------PHYKVRGNLrygMAKSMVAQFDKIVALL-GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
1MT0_A 171 DYESEHVIMRNMHKICKGRTVIII--AHRLSTV-KNADRIIVMEKGKIVEQGK 220
Cdd:PRK11144 160 DLPRKRELLPYLERLAREINIPILyvSHSLDEIlRLADRVVVLEQGKVKAFGP 212
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-233 |
1.56e-16 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 77.15 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 5 RNIRFRYK-PDSPV-ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFyIPENGQVLIDGH-----DLALADPNWLRR 77
Cdd:PRK15093 7 RNLTIEFKtSDGWVkAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTADRMrfddiDLLRLSPRERRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 78 QVG----VVLQD-------NVLLNRSIIDNIslanPGMSVeKVIYAAKLAGAHDFISEL--REG---YNTIVGEQGAGLS 141
Cdd:PRK15093 86 LVGhnvsMIFQEpqscldpSERVGRQLMQNI----PGWTY-KGRWWQRFGWRKRRAIELlhRVGikdHKDAMRSFPYELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 142 GGQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTV-KNADRIIVMEKGKIVEQ 218
Cdd:PRK15093 161 EGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQTVET 240
|
250
....*....|....*
1MT0_A 219 GKHKELLSEPESLYS 233
Cdd:PRK15093 241 APSKELVTTPHHPYT 255
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
19-216 |
1.70e-16 |
|
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: 77.94 E-value: 1.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYiPE---NGQVLIDGHDLALADPNWLRRQVGVVLQDNVLL--NRSI 93
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTERAGIVIIHQELTLvpELSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 94 IDNISLAN----PGMSVEkviYAAKLAGAHDFISELR---EGYNTIVGEQGaglsGGQRQRIAIARALVNNPKILIFDEA 166
Cdd:TIGR02633 96 AENIFLGNeitlPGGRMA---YNAMYLRAKNLLRELQldaDNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEP 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
1MT0_A 167 TSALDyESEHVIMRNMHKICKGRTV--IIIAHRLSTVKN-ADRIIVMEKGKIV 216
Cdd:TIGR02633 169 SSSLT-EKETEILLDIIRDLKAHGVacVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-215 |
1.77e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 77.74 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADP-NWLRRqvGVVL------QDNVLLNR 91
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPqDGLAN--GIVYisedrkRDGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 92 SIIDNISL------ANPGMSVEkviYAAKLAGAHDFIselrEGYN--TIVGEQGAG-LSGGQRQRIAIARALVNNPKILI 162
Cdd:PRK10762 346 SVKENMSLtalryfSRAGGSLK---HADEQQAVSDFI----RLFNikTPSMEQAIGlLSGGNQQKVAIARGLMTRPKVLI 418
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
1MT0_A 163 FDEATSALDYESEHVIMR--NMHKiCKGRTVIIIAHRLSTVKN-ADRIIVMEKGKI 215
Cdd:PRK10762 419 LDEPTRGVDVGAKKEIYQliNQFK-AEGLSIILVSSEMPEVLGmSDRILVMHEGRI 473
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
17-171 |
1.84e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.91 E-value: 1.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 17 VILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGvvLQDNVLLNRSIIDN 96
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG--HRNAMKPALTVAEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 97 IS-----LANPGMSVEKVIYAAKLAGahdfISELREGYntivgeqgagLSGGQRQRIAIARALVNNPKILIFDEATSALD 171
Cdd:PRK13539 94 LEfwaafLGGEELDIAAALEAVGLAP----LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
14-226 |
2.69e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 76.02 E-value: 2.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 14 DSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTK-LIQRFYIPE-------NGQVLIDGHDLALADPNWLRRQVGVVLQD 85
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKaLAGDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 86 nvllnrsiidnislANPG--MSVEKVIYA-----AKLAGA-----HDFISEL--REGYNTIVGEQGAGLSGGQRQRIAIA 151
Cdd:PRK13547 92 --------------AQPAfaFSAREIVLLgryphARRAGAlthrdGEIAWQAlaLAGATALVGRDVTTLSGGELARVQFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 152 RALVN---------NPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLS-TVKNADRIIVMEKGKIVEQG 219
Cdd:PRK13547 158 RVLAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNlAARHADRIAMLADGAIVAHG 237
|
....*..
1MT0_A 220 KHKELLS 226
Cdd:PRK13547 238 APADVLT 244
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-195 |
3.27e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 74.45 E-value: 3.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 14 DSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGVVLQDNVLLNRSI 93
Cdd:cd03231 11 DGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 94 IDNISLANPGMSVEKVIYA---AKLAGAHDFISelregyntivgeqgAGLSGGQRQRIAIARALVNNPKILIFDEATSAL 170
Cdd:cd03231 91 LENLRFWHADHSDEQVEEAlarVGLNGFEDRPV--------------AQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156
|
170 180
....*....|....*....|....*
1MT0_A 171 DYESEHVIMRNMHKICKGRTVIIIA 195
Cdd:cd03231 157 DKAGVARFAEAMAGHCARGGMVVLT 181
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
18-219 |
5.14e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 74.68 E-value: 5.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 18 ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLI--QRFYIPENGQVLIDGHDLALADPNwLRRQVGVVLQDNVLLNRSIID 95
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPE-ERAHLGIFLAFQYPIEIPGVS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 96 NISLANPGMSVEKVIYAAKLAGAHDFISELREGYNtIVGEQGA--------GLSGGQRQRIAIARALVNNPKILIFDEAT 167
Cdd:CHL00131 101 NADFLRLAYNSKRKFQGLPELDPLEFLEIINEKLK-LVGMDPSflsrnvneGFSGGEKKRNEILQMALLDSELAILDETD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
1MT0_A 168 SALDYESEHVIMRNMHKIC-KGRTVIIIAH--RLSTVKNADRIIVMEKGKIVEQG 219
Cdd:CHL00131 180 SGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTG 234
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
19-227 |
5.24e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 76.37 E-value: 5.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYiPE---NGQVLIDGHDLALADpnwLR--RQVGVVL--QDNVLL-N 90
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHgsyEGEILFDGEVCRFKD---IRdsEALGIVIihQELALIpY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 91 RSIIDNISLANPgMSVEKVI-YAAKLAGAHDFISE--LREGYNTIVGEQGAGlsggQRQRIAIARALVNNPKILIFDEAT 167
Cdd:NF040905 93 LSIAENIFLGNE-RAKRGVIdWNETNRRARELLAKvgLDESPDTLVTDIGVG----KQQLVEIAKALSKDVKLLILDEPT 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
1MT0_A 168 SAL-DYESEHVIMRNMHKICKGRTVIIIAHRLSTV-KNADRIIVMEKGKIVEQ-GKHKELLSE 227
Cdd:NF040905 168 AALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIETlDCRADEVTE 230
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
18-218 |
6.05e-16 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 74.05 E-value: 6.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 18 ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNW---LR-RQVGVVLQDNVLLnrsi 93
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRaKHVGFVFQSFMLI---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 94 idnislanPGM-SVEKVIYAAKLAGAHDfiSELREGYNTIVGEQGAG---------LSGGQRQRIAIARALVNNPKILIF 163
Cdd:PRK10584 101 --------PTLnALENVELPALLRGESS--RQSRNGAKALLEQLGLGkrldhlpaqLSGGEQQRVALARAFNGRPDVLFA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
1MT0_A 164 DEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKNADRIIVMEKGKIVEQ 218
Cdd:PRK10584 171 DEPTGNLDRQTGDKIADLLFSLNRehGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-165 |
6.56e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 74.30 E-value: 6.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 5 RNIRFRYKpdSPVILDNINLSIKQGEVIGIVGRSGSGKSTLtkliqrFYI------PENGQVLIDGHDLAlADPNWLRRQ 78
Cdd:COG1137 7 ENLVKSYG--KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYMivglvkPDSGRIFLDGEDIT-HLPMHKRAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 79 VGV--VLQDNvllnrSIIDnislanpGMSVEKVIYAA----KLAGA----------HDF-ISELREgyntivgEQGAGLS 141
Cdd:COG1137 78 LGIgyLPQEA-----SIFR-------KLTVEDNILAVlelrKLSKKereerleellEEFgITHLRK-------SKAYSLS 138
|
170 180
....*....|....*....|....
1MT0_A 142 GGQRQRIAIARALVNNPKILIFDE 165
Cdd:COG1137 139 GGERRRVEIARALATNPKFILLDE 162
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-216 |
1.01e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 75.72 E-value: 1.01e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 22 INLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQvGVVL------QDNVLLNRSIID 95
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRA-GIMLcpedrkAEGIIPVHSVAD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 96 NISLA-----NPGMSVEKVIYAAKLagAHDFISELRegYNTIVGEQGAG-LSGGQRQRIAIARALVNNPKILIFDEATSA 169
Cdd:PRK11288 351 NINISarrhhLRAGCLINNRWEAEN--ADRFIRSLN--IKTPSREQLIMnLSGGNQQKAILGRWLSEDMKVILLDEPTRG 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
1MT0_A 170 LDYESEHVIMRNMHKICK-GRTVIIIAHRLSTVKN-ADRIIVMEKGKIV 216
Cdd:PRK11288 427 IDVGAKHEIYNVIYELAAqGVAVLFVSSDLPEVLGvADRIVVMREGRIA 475
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
19-235 |
1.05e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 73.76 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLAladpNW-----LRRQVGVVLQDNVLLNRSI 93
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT----DWqtakiMREAVAIVPEGRRVFSRMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 94 IDNiSLANPGMSVEKVIYAAKLAGAHDFISELREGYNtivgeQGAG-LSGGQRQRIAIARALVNNPKILIFDEATSALdy 172
Cdd:PRK11614 97 VEE-NLAMGGFFAERDQFQERIKWVYELFPRLHERRI-----QRAGtMSGGEQQMLAIGRALMSQPRLLLLDEPSLGL-- 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1MT0_A 173 eSEHVIMRNMHKICK----GRTVIIIAHRLS-TVKNADRIIVMEKGKIVEQGKHKELLSEPESLYSYL 235
Cdd:PRK11614 169 -APIIIQQIFDTIEQlreqGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYL 235
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
11-215 |
3.61e-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: 74.09 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 11 YKPDSPVI--LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPE-NGQVLIDGHDLALADP-NWLRRQVGVVLQD- 85
Cdd:TIGR02633 266 WDVINPHRkrVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPaQAIRAGIAMVPEDr 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 86 ---NVLLNRSIIDNISLA--NPGMSVEKVIYAAKLAGAHDFISELR----EGYNTIvgeqgAGLSGGQRQRIAIARALVN 156
Cdd:TIGR02633 346 krhGIVPILGVGKNITLSvlKSFCFKMRIDAAAELQIIGSAIQRLKvktaSPFLPI-----GRLSGGNQQKAVLAKMLLT 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
1MT0_A 157 NPKILIFDEATSALDYESEHVIMRNMHKIC-KGRTVIIIAHRLSTVKN-ADRIIVMEKGKI 215
Cdd:TIGR02633 421 NPRVLILDEPTRGVDVGAKYEIYKLINQLAqEGVAIIVVSSELAEVLGlSDRVLVIGEGKL 481
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-228 |
5.64e-15 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.89 E-value: 5.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 22 INLSIKQGEVIGIVGRSGSGKSTLTKLIQRFyIPENGQVLIDGHDLALADPN-------WLRRQVGVVLQDNVL--LNRS 92
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAelarhraYLSQQQTPPFAMPVFqyLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 93 IIDNISLANPGMSVEKVIYAAKLAgahdfiSELREGYNTivgeqgagLSGGQRQRIAIARAL-----VNNP--KILIFDE 165
Cdd:PRK03695 94 QPDKTRTEAVASALNEVAEALGLD------DKLGRSVNQ--------LSGGEWQRVRLAAVVlqvwpDINPagQLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
1MT0_A 166 ATSALDYESEHVIMRNMHKIC-KGRTVIIIAHRLS-TVKNADRIIVMEKGKIVEQGKHKELLSEP 228
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELCqQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPE 224
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-216 |
8.21e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 72.84 E-value: 8.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLAL-ADPNWLRRQVGVVLQD-NVLLNRSIIDN 96
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFkSSKEALENGISMVHQElNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 97 ISLAN---PGMSV-EKVIYAAKLAgahdFISELreGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKILIFDEATSAL-D 171
Cdd:PRK10982 94 MWLGRyptKGMFVdQDKMYRDTKA----IFDEL--DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
1MT0_A 172 YESEHV--IMRNMHKicKGRTVIIIAHRLSTV-KNADRIIVMEKGKIV 216
Cdd:PRK10982 168 KEVNHLftIIRKLKE--RGCGIVYISHKMEEIfQLCDEITILRDGQWI 213
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-213 |
9.37e-15 |
|
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: 69.32 E-value: 9.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 28 QGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIdghdlaladpnwlrrqvgvvlqdnvllnrsiidnislanpgmsve 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 108 kviyaakLAGAHDFISELREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMH---- 183
Cdd:smart00382 36 -------IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrll 108
|
170 180 190
....*....|....*....|....*....|....*....
1MT0_A 184 ---KICKGRTVIIIAHRLSTVKNA------DRIIVMEKG 213
Cdd:smart00382 109 lllKSEKNLTVILTTNDEKDLGPAllrrrfDRRIVLLLI 147
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
2-229 |
3.28e-14 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 70.18 E-value: 3.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWL---RRQ 78
Cdd:PRK11831 8 VDMRGVSFTR--GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 79 VGVVLQDNVLL-NRSIIDNIS--------LANPGM--SVEKVIYAAKLAGAHDFISelregyntivgeqgAGLSGGQRQR 147
Cdd:PRK11831 86 MSMLFQSGALFtDMNVFDNVAyplrehtqLPAPLLhsTVMMKLEAVGLRGAAKLMP--------------SELSGGMARR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 148 IAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK--GRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKEL 224
Cdd:PRK11831 152 AALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
....*
1MT0_A 225 LSEPE 229
Cdd:PRK11831 232 QANPD 236
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
17-196 |
1.88e-13 |
|
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: 66.61 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 17 VILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGVVLQDNVLLNRSIIDN 96
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELSALEN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 97 ISLanpgmsvekviYAAKLAGAHDFISELRE--GYNTIVGEQGAGLSGGQRQRIAIARALVNNPKILIFDEATSALDYES 174
Cdd:TIGR01189 94 LHF-----------WAAIHGGAQRTIEDALAavGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
170 180
....*....|....*....|....
1MT0_A 175 EHVIMRNM--HkICKGRTVIIIAH 196
Cdd:TIGR01189 163 VALLAGLLraH-LARGGIVLLTTH 185
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-227 |
4.60e-13 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 67.99 E-value: 4.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVgvvlqdnvllnrSIIDNIS 98
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQL------------TGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 99 LANPGMSVEK---------VIYAAKLAgahDFISELREGYntivgeqgaglSGGQRQRIAIARALVNNPKILIFDEATSA 169
Cdd:PRK13545 108 LKGLMMGLTKekikeiipeIIEFADIG---KFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 170 LDYESEHVIMRNMHKIC-KGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLSE 227
Cdd:PRK13545 174 GDQTFTKKCLDKMNEFKeQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
6-205 |
7.24e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 65.36 E-value: 7.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 6 NIRFRYKpDSPvILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLAlADPNWLRRQVGVV--- 82
Cdd:PRK13540 6 ELDFDYH-DQP-LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK-KDLCTYQKQLCFVghr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 83 --LQDNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDFISELregyntivgeqgagLSGGQRQRIAIARALVNNPKI 160
Cdd:PRK13540 83 sgINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMSKAKL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
1MT0_A 161 LIFDEATSALDYESEHVIMRNM--HKiCKGRTVIIIAHRLSTVKNAD 205
Cdd:PRK13540 149 WLLDEPLVALDELSLLTIITKIqeHR-AKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
14-216 |
9.09e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.28 E-value: 9.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 14 DSPvILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGhDLALA----DP----------------- 72
Cdd:PRK11147 15 DAP-LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ-DLIVArlqqDPprnvegtvydfvaegie 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 73 ---------NWLRRQVGVVLQDNvLLNR-----SIIDNISLANPGMSVEKVIYAAKLAGAhdfiSELREgyntivgeqga 138
Cdd:PRK11147 93 eqaeylkryHDISHLVETDPSEK-NLNElaklqEQLDHHNLWQLENRINEVLAQLGLDPD----AALSS----------- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 139 gLSGGQRQRIAIARALVNNPKILIFDEATSALDYESehvI--MRNMHKICKGrTVIIIAHRLSTVKN-ADRIIVMEKGKI 215
Cdd:PRK11147 157 -LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET---IewLEGFLKTFQG-SIIFISHDRSFIRNmATRIVDLDRGKL 231
|
.
1MT0_A 216 V 216
Cdd:PRK11147 232 V 232
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
18-196 |
1.81e-12 |
|
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: 66.11 E-value: 1.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 18 ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQvlidghdlALADPNwlrRQVGVVLQD-----------N 86
Cdd:TIGR03719 20 ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE--------ARPQPG---IKVGYLPQEpqldptktvreN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 87 V---------LLNRsiIDNIS--LANPGMSVEKVIY-AAKL------AGAHDFISELREGYNTI---VGEQGAG-LSGGQ 144
Cdd:TIGR03719 89 VeegvaeikdALDR--FNEISakYAEPDADFDKLAAeQAELqeiidaADAWDLDSQLEIAMDALrcpPWDADVTkLSGGE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
1MT0_A 145 RQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKIcKGrTVIIIAH 196
Cdd:TIGR03719 167 RRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEY-PG-TVVAVTH 216
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
11-216 |
2.50e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 65.58 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 11 YKPDSP--VILDNINLSIKQGEVIGIVGRSGSGKSTLT-KLIQRFY-IPENGQVLIDG-------------HDLALADPN 73
Cdd:NF040905 266 YHPLHPerKVVDDVSLNVRRGEIVGIAGLMGAGRTELAmSVFGRSYgRNISGTVFKDGkevdvstvsdaidAGLAYVTED 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 74 wlRRQVGVVLQDNvllnrsIIDNISLAN-PGMSVEKVIYAAK-LAGAHDFISELREGYNTIvgEQGAG-LSGGQRQRIAI 150
Cdd:NF040905 346 --RKGYGLNLIDD------IKRNITLANlGKVSRRGVIDENEeIKVAEEYRKKMNIKTPSV--FQKVGnLSGGNQQKVVL 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1MT0_A 151 ARALVNNPKILIFDEATSALD----YESeHVIMRNMHKicKGRTVIIIAHRLSTV-KNADRIIVMEKGKIV 216
Cdd:NF040905 416 SKWLFTDPDVLILDEPTRGIDvgakYEI-YTIINELAA--EGKGVIVISSELPELlGMCDRIYVMNEGRIT 483
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-233 |
2.66e-12 |
|
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: 64.35 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 25 SIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALaDPNWLRRQVGVVLQDnvLLnrSIIDNISLANPGM 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY-KPQYIKADYEGTVRD--LL--SSITKDFYTHPYF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 105 SVEkVIYAAKLAGAHDfiSELREgyntivgeqgagLSGGQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHK 184
Cdd:cd03237 96 KTE-IAKPLQIEQILD--REVPE------------LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
1MT0_A 185 IC--KGRTVIIIAHRLSTVKN-ADRIIVMEkGKIVEQGkhkeLLSEPESLYS 233
Cdd:cd03237 161 FAenNEKTAFVVEHDIIMIDYlADRLIVFE-GEPSVNG----VANPPQSLRS 207
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
21-229 |
2.85e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 65.58 E-value: 2.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 21 NINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADP-NWLRRQVGVVLQ---DNVLL-NRSIID 95
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYITEsrrDNGFFpNFSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 96 NislanpgMSVEKVIYAAKLAGAHDFISELRE----------------GYNTIVGEqgagLSGGQRQRIAIARALVNNPK 159
Cdd:PRK09700 361 N-------MAISRSLKDGGYKGAMGLFHEVDEqrtaenqrellalkchSVNQNITE----LSGGNQQKVLISKWLCCCPE 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
1MT0_A 160 ILIFDEATSALDYESEHVIMRNMHKIC-KGRTVIIIAHRLSTVKNA-DRIIVMEKGKIVEQGKHKELLSEPE 229
Cdd:PRK09700 430 VIIFDEPTRGIDVGAKAEIYKVMRQLAdDGKVILMVSSELPEIITVcDRIAVFCEGRLTQILTNRDDMSEEE 501
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-224 |
7.64e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.25 E-value: 7.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQ-VGVVLQD-NVLLNRSIIDN 96
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAgIGIIHQElNLIPQLTIAEN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 97 ISLA----NP-GMSVEKVIYA------AKLagahdfisELREGYNTIVGEqgagLSGGQRQRIAIARALVNNPKILIFDE 165
Cdd:PRK10762 100 IFLGrefvNRfGRIDWKKMYAeadkllARL--------NLRFSSDKLVGE----LSIGEQQMVEIAKVLSFESKVIIMDE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1MT0_A 166 ATSAL-DYESE---HVI--MRNmhkicKGRTVIIIAHRLSTV-KNADRIIVMEKGKIVEQGKHKEL 224
Cdd:PRK10762 168 PTDALtDTETEslfRVIreLKS-----QGRGIVYISHRLKEIfEICDDVTVFRDGQFIAEREVADL 228
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-215 |
9.24e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.92 E-value: 9.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 21 NINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNwLRRQVGVVL------QDNVLLNRSII 94
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTA-QRLARGLVYlpedrqSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 95 DNI-SLA--NPGMSVEKVIYAAKLagahdfiselrEGYNTIVG------EQGA-GLSGGQRQRIAIARALVNNPKILIFD 164
Cdd:PRK15439 360 WNVcALThnRRGFWIKPARENAVL-----------ERYRRALNikfnhaEQAArTLSGGNQQKVLIAKCLEASPQLLIVD 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
1MT0_A 165 EATSALDYESEHVIMRNMHKICK-GRTVIIIAHRLSTV-KNADRIIVMEKGKI 215
Cdd:PRK15439 429 EPTRGVDVSARNDIYQLIRSIAAqNVAVLFISSDLEEIeQMADRVLVMHQGEI 481
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-219 |
2.53e-11 |
|
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: 60.41 E-value: 2.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIqrfyIPENGQVLIDGhDLALADPNwlrrqvgvvlqdnvllnrsiidnis 98
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG----LYASGKARLIS-FLPKFSRN------------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 99 lanpgmsveKVIYAAKLAgahdFISELREGYNTIvGEQGAGLSGGQRQRIAIARALVNNPK--ILIFDEATSALDYESEH 176
Cdd:cd03238 61 ---------KLIFIDQLQ----FLIDVGLGYLTL-GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDIN 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
1MT0_A 177 VIMRNMHK-ICKGRTVIIIAHRLSTVKNADRIIVMEK------GKIVEQG 219
Cdd:cd03238 127 QLLEVIKGlIDLGNTVILIEHNLDVLSSADWIIDFGPgsgksgGKVVFSG 176
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
17-171 |
3.94e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.20 E-value: 3.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 17 VILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLA------LADPNWLRRQVGVvlqdNVLLN 90
Cdd:PRK13538 15 ILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRrqrdeyHQDLLYLGHQPGI----KTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 91 rsiidnislanpgmSVEKVIYAAKLAG-AHDF--ISELREgyntiVGEQG------AGLSGGQRQRIAIARALVNNPKIL 161
Cdd:PRK13538 91 --------------ALENLRFYQRLHGpGDDEalWEALAQ-----VGLAGfedvpvRQLSAGQQRRVALARLWLTRAPLW 151
|
170
....*....|
1MT0_A 162 IFDEATSALD 171
Cdd:PRK13538 152 ILDEPFTAID 161
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
124-213 |
1.65e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 60.63 E-value: 1.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 124 ELREGYNTIVGEQG-AGLSGGQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNM-HKICKGRTVIIIAHRLS-- 199
Cdd:PLN03140 1003 ELDNLKDAIVGLPGvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSid 1082
|
90
....*....|....
1MT0_A 200 TVKNADRIIVMEKG 213
Cdd:PLN03140 1083 IFEAFDELLLMKRG 1096
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
17-196 |
5.61e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 58.59 E-value: 5.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 17 VILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQvlidghdlALADPNWlrrQVGVVLQ-----------D 85
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGE--------ARPAPGI---KVGYLPQepqldpektvrE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 86 NV---------LLNRsiIDNIS--LANPGMSVEKVI-YAAKL------AGAHDFISELregyntivgEQGA--------- 138
Cdd:PRK11819 90 NVeegvaevkaALDR--FNEIYaaYAEPDADFDALAaEQGELqeiidaADAWDLDSQL---------EIAMdalrcppwd 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
1MT0_A 139 ----GLSGGQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKIcKGrTVIIIAH 196
Cdd:PRK11819 159 akvtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDY-PG-TVVAVTH 218
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-219 |
9.86e-10 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 57.20 E-value: 9.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALA-------------DPNWlrrQVGVVLQD 85
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAlqknlvayvpqseEVDW---SFPVLVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 86 NVLLNRsiIDNISLANPGMSVEKVIYAAKLAGAHdfISELRegyNTIVGEqgagLSGGQRQRIAIARALVNNPKILIFDE 165
Cdd:PRK15056 100 VVMMGR--YGHMGWLRRAKKRDRQIVTAALARVD--MVEFR---HRQIGE----LSGGQKKRVFLARAIAQQGQVILLDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
1MT0_A 166 ATSALDYESEHVIMRNMHKI-CKGRTVIIIAHRLSTVKNADRIIVMEKGKIVEQG 219
Cdd:PRK15056 169 PFTGVDVKTEARIISLLRELrDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
18-239 |
9.95e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 57.11 E-value: 9.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 18 ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLI--QRFYIPENGQVLIDGHDLALADPNwLRRQVGVVLQ----------D 85
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPE-DRAGEGIFMAfqypveipgvS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 86 NVLLNRSIIDNISLANPGMSVEKVIYAaklagahDFISE----LREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKIL 161
Cdd:PRK09580 95 NQFFLQTALNAVRSYRGQEPLDRFDFQ-------DLMEEkialLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPELC 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 162 IFDEATSALDYESEHVIMRNMHKICKG-RTVIIIAH--RLSTVKNADRIIVMEKGKIVEQGKHKELLSEPESLYSYLYQL 238
Cdd:PRK09580 168 ILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFTLVKQLEEQGYGWLTEQ 247
|
.
1MT0_A 239 Q 239
Cdd:PRK09580 248 Q 248
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
19-219 |
1.05e-09 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 57.24 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLtkLIQRFYipengQVLIDGHDLALADPNWLRRQVGVVLQDNVL-LNRSIIDNI 97
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSL--INDTLY-----PALARRLHLKKEQPGNHDRIEGLEHIDKVIvIDQSPIGRT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 98 SLANP-----------------------------------------GMSVEK-VIYAAKLAGAHDFISELRE---GYNTI 132
Cdd:cd03271 84 PRSNPatytgvfdeirelfcevckgkrynretlevrykgksiadvlDMTVEEaLEFFENIPKIARKLQTLCDvglGYIKL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 133 vGEQGAGLSGGQRQRIAIARALVN---NPKILIFDEATSALDYESEHVIMRNMHKIC-KGRTVIIIAHRLSTVKNADRII 208
Cdd:cd03271 164 -GQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVdKGNTVVVIEHNLDVIKCADWII 242
|
250
....*....|....*..
1MT0_A 209 VM------EKGKIVEQG 219
Cdd:cd03271 243 DLgpeggdGGGQVVASG 259
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-211 |
1.12e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.90 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 26 IKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDghdLALA-DPNWLRRQVGVVLQDnvLLnRSIIDNIS------ 98
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE---LKISyKPQYIKPDYDGTVED--LL-RSITDDLGssyyks 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 99 -LANPgMSVEKViyaaklagahdFISELREgyntivgeqgagLSGGQRQRIAIARALVNNPKILIFDEATSALDYESEHV 177
Cdd:PRK13409 436 eIIKP-LQLERL-----------LDKNVKD------------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLA 491
|
170 180 190
....*....|....*....|....*....|....*..
1MT0_A 178 IMRNMHKICKGR--TVIIIAHRLSTVKN-ADRIIVME 211
Cdd:PRK13409 492 VAKAIRRIAEEReaTALVVDHDIYMIDYiSDRLMVFE 528
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-198 |
3.36e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 56.36 E-value: 3.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 26 IKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLidghdlalADPNW---LRRQVGVVLQDNV--LLNRSI------- 93
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYE--------EEPSWdevLKRFRGTELQNYFkkLYNGEIkvvhkpq 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 94 -IDNISLANPGmSVEKVIYAAKLAGAHD-FISELreGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKILIFDEATSALD 171
Cdd:PRK13409 168 yVDLIPKVFKG-KVRELLKKVDERGKLDeVVERL--GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
|
170 180
....*....|....*....|....*..
1MT0_A 172 YESEHVIMRNMHKICKGRTVIIIAHRL 198
Cdd:PRK13409 245 IRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-171 |
3.49e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 56.67 E-value: 3.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 20 DNINLSIKQGEVIGIVGRSGSGKST----LTKLIQrfyiPENGQVL-----IDGHDLAladpnwLRRQVG---------- 80
Cdd:NF033858 283 DHVSFRIRRGEIFGFLGSNGCGKSTtmkmLTGLLP----ASEGEAWlfgqpVDAGDIA------TRRRVGymsqafslyg 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 81 --VVLQdNVLLNrsiidnislanpgmsvekviyaAKL-----AGAHDFISEL--REGYNTIVGEQGAGLSGGQRQRIAIA 151
Cdd:NF033858 353 elTVRQ-NLELH----------------------ARLfhlpaAEIAARVAEMleRFDLADVADALPDSLPLGIRQRLSLA 409
|
170 180
....*....|....*....|
1MT0_A 152 RALVNNPKILIFDEATSALD 171
Cdd:NF033858 410 VAVIHKPELLILDEPTSGVD 429
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-199 |
4.76e-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: 55.07 E-value: 4.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 27 KQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQvlidgHDlalADPNW---LRRQVGVVLQD--NVLLNRSI-------- 93
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK-----FD---DPPDWdeiLDEFRGSELQNyfTKLLEGDVkvivkpqy 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 94 IDNISLANPGmSVEKVIYAAKLAGAHDFISElREGYNTIVGEQGAGLSGGQRQRIAIARALVNNPKILIFDEATSALDYE 173
Cdd:cd03236 96 VDLIPKAVKG-KVGELLKKKDERGKLDELVD-QLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
170 180
....*....|....*....|....*..
1MT0_A 174 SEHVIMRNMHKICK-GRTVIIIAHRLS 199
Cdd:cd03236 174 QRLNAARLIRELAEdDNYVLVVEHDLA 200
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
140-224 |
6.60e-09 |
|
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: 55.79 E-value: 6.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 140 LSGGQRQRIAIARAL---VNNPKILIFDEATSALDYESEHVIMRNMHK-ICKGRTVIIIAHRLSTVKNADRIIVM----- 210
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRlVDKGNTVVVIEHNLDVIKTADYIIDLgpegg 909
|
90
....*....|....*
1MT0_A 211 -EKGKIVEQGKHKEL 224
Cdd:TIGR00630 910 dGGGTVVASGTPEEV 924
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-200 |
8.01e-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: 55.18 E-value: 8.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 27 KQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLidghdlalADPNW---LRRQVGVVLQD--NVLLNRSI-------- 93
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYD--------EEPSWdevLKRFRGTELQDyfKKLANGEIkvahkpqy 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 94 IDNISLANPGmsveKVIYAAKLAGAHDFISELRE--GYNTIVGEQGAGLSGGQRQRIAIARALVNNPKILIFDEATSALD 171
Cdd:COG1245 169 VDLIPKVFKG----TVRELLEKVDERGKLDELAEklGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180 190
....*....|....*....|....*....|..
1MT0_A 172 -YESEHV--IMRNMHKicKGRTVIIIAHRLST 200
Cdd:COG1245 245 iYQRLNVarLIRELAE--EGKYVLVVEHDLAI 274
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
2-202 |
1.21e-08 |
|
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: 54.75 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFrYKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPNWLRRQVGV 81
Cdd:TIGR00954 452 IKFENIPL-VTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKLFYVPQRPYMTLGT 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 vLQDNVLLNRSIIDnisLANPGMS---VEKVIYAAKLagahDFISElREGYNTIVGEQGAGLSGGQRQRIAIARALVNNP 158
Cdd:TIGR00954 531 -LRDQIIYPDSSED---MKRRGLSdkdLEQILDNVQL----THILE-REGGWSAVQDWMDVLSGGEKQRIAMARLFYHKP 601
|
170 180 190 200
....*....|....*....|....*....|....*....|....
1MT0_A 159 KILIFDEATSALDYESEHVIMRNMHKicKGRTVIIIAHRLSTVK 202
Cdd:TIGR00954 602 QFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHRKSLWK 643
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-229 |
1.27e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 54.05 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGhdlaladpnwlrrQVGVVlQDNVLLNRSI--IDN 96
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-------------EVSVI-AISAGLSGQLtgIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 97 ISLANPGMSVEKVIYAAKLAGAHDFiSELREGYNTIVGEqgagLSGGQRQRIAIARALVNNPKILIFDEATSALDYESEH 176
Cdd:PRK13546 106 IEFKMLCMGFKRKEIKAMTPKIIEF-SELGEFIYQPVKK----YSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
1MT0_A 177 VIMRNMHKI-CKGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLSEPE 229
Cdd:PRK13546 181 KCLDKIYEFkEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPKYE 235
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-221 |
1.59e-08 |
|
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: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 25 SIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDghdLALA-DPNWLRRQVGVVLQDnvLLNRSIIDNIS----- 98
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED---LKISyKPQYISPDYDGTVEE--FLRSANTDDFGssyyk 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 99 --LANPgMSVEKViyaaklagahdFISELREgyntivgeqgagLSGGQRQRIAIARALVNNPKILIFDEATSALDYESE- 175
Cdd:COG1245 437 teIIKP-LGLEKL-----------LDKNVKD------------LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRl 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
1MT0_A 176 ---HVIMRNMHKicKGRTVIIIAHRLSTVKN-ADRIIVMEkGkivEQGKH 221
Cdd:COG1245 493 avaKAIRRFAEN--RGKTAMVVDHDIYLIDYiSDRLMVFE-G---EPGVH 536
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
11-213 |
1.59e-08 |
|
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: 54.63 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 11 YKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLaLADPNWLRRQVGVVLQ----DN 86
Cdd:TIGR01257 1947 YSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-LTNISDVHQNMGYCPQfdaiDD 2025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 87 VLLNRsiiDNISL-----ANPGMSVEKV-----------IYAAKLAGAHdfiselregyntivgeqgaglSGGQRQRIAI 150
Cdd:TIGR01257 2026 LLTGR---EHLYLyarlrGVPAEEIEKVanwsiqslglsLYADRLAGTY---------------------SGGNKRKLST 2081
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
1MT0_A 151 ARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK-GRTVIIIAHRLSTVKN-ADRIIVMEKG 213
Cdd:TIGR01257 2082 AIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIReGRAVVLTSHSMEECEAlCTRLAIMVKG 2146
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
18-171 |
2.89e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 52.81 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 18 ILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLidgHDLALadpnwlrrQVGVVLQdNVLLNRSI---I 94
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---RNGKL--------RIGYVPQ-KLYLDTTLpltV 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1MT0_A 95 DNISLANPGMSVEKVIYAAKLAGAHDFISELREGyntivgeqgagLSGGQRQRIAIARALVNNPKILIFDEATSALD 171
Cdd:PRK09544 87 NRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNRPQLLVLDEPTQGVD 152
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
19-219 |
2.89e-08 |
|
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: 52.65 E-value: 2.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLT-KLI----QRFYIpengQVLidghdlaladPNWLRRQVGVVLQDNVllnrsi 93
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfDTIyaegQRRYV----ESL----------SAYARQFLGQMDKPDV------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 94 iDNISLANPGMSVE----------------------KVIYA-AKLAGAHDFISELREGYNTiVGEQGAGLSGGQRQRIAI 150
Cdd:cd03270 71 -DSIEGLSPAIAIDqkttsrnprstvgtvteiydylRLLFArVGIRERLGFLVDVGLGYLT-LSRSAPTLSGGEAQRIRL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1MT0_A 151 ARALVNNPK--ILIFDEATSALDYESEHVIMRNMHKI-CKGRTVIIIAHRLSTVKNADRIIVM------EKGKIVEQG 219
Cdd:cd03270 149 ATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLrDLGNTVLVVEHDEDTIRAADHVIDIgpgagvHGGEIVAQG 226
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-220 |
9.77e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 52.04 E-value: 9.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVIGIVGRSGSGKSTLTKLIqrFYIPE--NGQVLIDGHDLALADPNWL-----------RRQVGVVLQD 85
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETL--FGIREksAGTITLHGKKINNHNANEAinhgfalvteeRRSTGIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 86 NVLLNrSIIDNIS--------LANPGMS--VEKVIYAAKLAgahdfiselREGYNTIVGEqgagLSGGQRQRIAIARALV 155
Cdd:PRK10982 342 DIGFN-SLISNIRnyknkvglLDNSRMKsdTQWVIDSMRVK---------TPGHRTQIGS----LSGGNQQKVIIGRWLL 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 156 NNPKILIFDEATSALDYESEHVIMRNMHKIC-KGRTVIIIAHRLSTVKN-ADRIIVMEKGK---IVEQGK 220
Cdd:PRK10982 408 TQPEILMLDEPTRGIDVGAKFEIYQLIAELAkKDKGIIIISSEMPELLGiTDRILVMSNGLvagIVDTKT 477
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-211 |
1.58e-07 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 49.88 E-value: 1.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 26 IKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLAladpnwlrrqvgvvlqdnvllnrsiidnislanpgms 105
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV------------------------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 106 vekviyaaklagahdfiselregyntiVGEQGAGLSGGQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKI 185
Cdd:cd03222 65 ---------------------------YKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180
....*....|....*....|....*....
1MT0_A 186 CK--GRTVIIIAHRLSTVKN-ADRIIVME 211
Cdd:cd03222 118 SEegKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
2-174 |
1.80e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.40 E-value: 1.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGhdlaladpnwlRRQVGV 81
Cdd:PLN03073 509 ISFSDASFGY-PGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSA-----------KVRMAV 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 VLQDNVllnrsiiDNISLanpgmSVEKVIYAAK-LAGAHDfiSELRE--GYNTIVG----EQGAGLSGGQRQRIAIARAL 154
Cdd:PLN03073 577 FSQHHV-------DGLDL-----SSNPLLYMMRcFPGVPE--QKLRAhlGSFGVTGnlalQPMYTLSGGQKSRVAFAKIT 642
|
170 180
....*....|....*....|
1MT0_A 155 VNNPKILIFDEATSALDYES 174
Cdd:PLN03073 643 FKKPHILLLDEPSNHLDLDA 662
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
134-224 |
3.67e-07 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 50.12 E-value: 3.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 134 GEQGAGLSGGQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICK-GRTVIIIAHRLSTVKN-ADRIIVME 211
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRdGATVLLTTQYMEEAEQlAHELTVID 218
|
90
....*....|...
1MT0_A 212 KGKIVEQGKHKEL 224
Cdd:NF000106 219 RGRVIADGKVDEL 231
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
130-230 |
3.87e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 50.61 E-value: 3.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 130 NTIVG-EQGAGLSGGQRQRIAIARALVNNPKILIFDEATSALDYESEHVIMRNMHKICKGRTVIIIAHRLS----TVKNA 204
Cdd:PLN03140 326 DTIVGdEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQpapeTFDLF 405
|
90 100
....*....|....*....|....*.
1MT0_A 205 DRIIVMEKGKIVEQGKHKELLSEPES 230
Cdd:PLN03140 406 DDIILLSEGQIVYQGPRDHILEFFES 431
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
23-235 |
3.90e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.01 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 23 NLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLA---------LADPNWLRRQ---VGVVLQDNVLLN 90
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITrlsfeqlqkLVSDEWQRNNtdmLSPGEDDTGRTT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 91 RSIIDNiSLANPGMSVEkviYAAKLAgahdfISEL---REGYntivgeqgagLSGGQRQRIAIARALVNNPKILIFDEAT 167
Cdd:PRK10938 103 AEIIQD-EVKDPARCEQ---LAQQFG-----ITALldrRFKY----------LSTGETRKTLLCQALMSEPDLLILDEPF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 168 SALDYESEHVIMRNMHKIC-KGRTVIIIAHRLSTVKN-ADRIIVMEKGKIVEQGKHKELLSepESLYSYL 235
Cdd:PRK10938 164 DGLDVASRQQLAELLASLHqSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQ--QALVAQL 231
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
139-212 |
6.37e-07 |
|
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: 47.74 E-value: 6.37e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
1MT0_A 139 GLSGGQRQRIAIARAL----VNNPKILIFDEATSALDYESEHVIMRN-MHKICKGRTVIIIAHRLSTVKNADRIIVMEK 212
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAiLEHLVKGAQVIVITHLPELAELADKLIHIKK 155
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-173 |
9.31e-07 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 49.16 E-value: 9.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYkpDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLI-DGHDLALADPNwlrrqvg 80
Cdd:TIGR03719 323 IEAENLTKAF--GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAYVDQS------- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 81 vvlQDNVLLNRSIIDNISLANPGMSVEKVIYAAK-LAGAHDFISELREGYntiVGEqgagLSGGQRQRIAIARALVNNPK 159
Cdd:TIGR03719 394 ---RDALDPNKTVWEEISGGLDIIKLGKREIPSRaYVGRFNFKGSDQQKK---VGQ----LSGGERNRVHLAKTLKSGGN 463
|
170
....*....|....
1MT0_A 160 ILIFDEATSALDYE 173
Cdd:TIGR03719 464 VLLLDEPTNDLDVE 477
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
140-230 |
1.54e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 48.48 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 140 LSGGQRQRIAIARAL--VNNPKIL-IFDEATSALDYESEHVIMRNMHK-ICKGRTVIIIAHRLSTVKNADRIIVM----- 210
Cdd:COG0178 827 LSGGEAQRVKLASELskRSTGKTLyILDEPTTGLHFHDIRKLLEVLHRlVDKGNTVVVIEHNLDVIKTADWIIDLgpegg 906
|
90 100
....*....|....*....|.
1MT0_A 211 EK-GKIVEQGKHKELLSEPES 230
Cdd:COG0178 907 DGgGEIVAEGTPEEVAKVKAS 927
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
23-196 |
2.41e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.96 E-value: 2.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 23 NLSIKQGE--VIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDghdlaladPNwlrRQVGVVLQDNVLL-NRSIIDNISL 99
Cdd:PRK15064 19 NISVKFGGgnRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD--------PN---ERLGKLRQDQFAFeEFTVLDTVIM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 100 ----------------ANPGMSVEKVIYAAKLAGAH----DFISELREGYNTI-VG---EQGAGL----SGGQRQRIAIA 151
Cdd:PRK15064 88 ghtelwevkqerdriyALPEMSEEDGMKVADLEVKFaemdGYTAEARAGELLLgVGipeEQHYGLmsevAPGWKLRVLLA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
1MT0_A 152 RALVNNPKILIFDEATSALDYeseHVImRNMHKICKGR--TVIIIAH 196
Cdd:PRK15064 168 QALFSNPDILLLDEPTNNLDI---NTI-RWLEDVLNERnsTMIIISH 210
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
19-196 |
3.62e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.55 E-value: 3.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 19 LDNINLSIKQGEVI-------------GIVGRSGSGKSTLTKLIQRFYI---PENGQVLIDGHDLALADPNWLRrqvgVV 82
Cdd:PLN03073 180 MENFSISVGGRDLIvdasvtlafgrhyGLVGRNGTGKTTFLRYMAMHAIdgiPKNCQILHVEQEVVGDDTTALQ----CV 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 83 LQDNVLLNRSIIDNISLANPGMSVEKVIYAAKLAGAH------DFISE-LREGYNTI-----------VGEQGAGLS--- 141
Cdd:PLN03073 256 LNTDIERTQLLEEEAQLVAQQRELEFETETGKGKGANkdgvdkDAVSQrLEEIYKRLelidaytaearAASILAGLSftp 335
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
1MT0_A 142 -----------GGQRQRIAIARALVNNPKILIFDEATSALDYESehVIMRNMHKICKGRTVIIIAH 196
Cdd:PLN03073 336 emqvkatktfsGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA--VLWLETYLLKWPKTFIVVSH 399
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-217 |
4.09e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.09 E-value: 4.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 17 VILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGhdlaladpNWlrrQVGVVLQDNVLLNRSIIDN 96
Cdd:PRK10636 15 VLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPG--------NW---QLAWVNQETPALPQPALEY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 97 I------------SLA-----NPGMSVekviyaAKLAGAHDFI---------SELREGY---NTIVGEQGAGLSGGQRQR 147
Cdd:PRK10636 84 VidgdreyrqleaQLHdanerNDGHAI------ATIHGKLDAIdawtirsraASLLHGLgfsNEQLERPVSDFSGGWRMR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1MT0_A 148 IAIARALVNNPKILIFDEATSALDYESehVIMrnMHKICKGR--TVIIIAHR---LSTVknADRIIVMEKGKIVE 217
Cdd:PRK10636 158 LNLAQALICRSDLLLLDEPTNHLDLDA--VIW--LEKWLKSYqgTLILISHDrdfLDPI--VDKIIHIEQQSLFE 226
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
140-230 |
2.48e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 45.06 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 140 LSGGQRQRIAIARALVNNP--KIL-IFDEATSALDYESEHVIMRNMHKIC-KGRTVIIIAHRLSTVKNADRIIVM----- 210
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgKTLyILDEPTTGLHFEDIRKLLEVLHRLVdKGNTVVVIEHNLDVIKTADWIIDLgpegg 910
|
90 100
....*....|....*....|.
1MT0_A 211 -EKGKIVEQGKHKELLSEPES 230
Cdd:PRK00349 911 dGGGEIVATGTPEEVAKVEAS 931
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
140-231 |
3.04e-05 |
|
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: 44.62 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 140 LSGGQRQRIAIAR----ALVNnpKILIFDEATSALDYESEHVIM---RNMHKicKGRTVIIIAHRLSTVKNADRIIVM-- 210
Cdd:TIGR00630 489 LSGGEAQRIRLATqigsGLTG--VLYVLDEPSIGLHQRDNRRLIntlKRLRD--LGNTLIVVEHDEDTIRAADYVIDIgp 564
|
90 100
....*....|....*....|....*
1MT0_A 211 ----EKGKIVEQGKHKELLSEPESL 231
Cdd:TIGR00630 565 gageHGGEVVASGTPEEILANPDSL 589
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
140-208 |
3.93e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 3.93e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
1MT0_A 140 LSGGQRQRIAIARALVN---NPKILIFDEATSALDYESEHVIMRNMHKIC-KGRTVIIIAHRLSTVKNADRII 208
Cdd:PRK00635 810 LSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLThQGHTVVIIEHNMHVVKVADYVL 882
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-171 |
4.17e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.01 E-value: 4.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 17 VILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQV-LIDGHDLALadpnWLRRQVGVVLQDnvllnRSIID 95
Cdd:PRK10636 326 IILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGIKLGY----FAQHQLEFLRAD-----ESPLQ 396
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1MT0_A 96 NISLANPGMSVEKViyaaklagaHDFISELreGYN-TIVGEQGAGLSGGQRQRIAIARALVNNPKILIFDEATSALD 171
Cdd:PRK10636 397 HLARLAPQELEQKL---------RDYLGGF--GFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
11-183 |
7.76e-05 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 42.53 E-value: 7.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 11 YKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDLALADPN----WLRRQVGVVLQDN 86
Cdd:PRK13543 19 FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSrfmaYLGHLPGLKADLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 87 VLLNRSIIDNISLANPGMSVEKVIYAAKLAGAHDfiselregynTIVGEqgagLSGGQRQRIAIARALVNNPKILIFDEA 166
Cdd:PRK13543 99 TLENLHFLCGLHGRRAKQMPGSALAIVGLAGYED----------TLVRQ----LSAGQKKRLALARLWLSPAPLWLLDEP 164
|
170 180
....*....|....*....|.
1MT0_A 167 TSALDYES----EHVIMRNMH 183
Cdd:PRK13543 165 YANLDLEGitlvNRMISAHLR 185
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
140-212 |
8.07e-05 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.21 E-value: 8.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 140 LSGGQRQ------RIAIARALVNNPKILIFDEATSALD----YESEHVIMRNMHKIcKGRTVIIIAHRLSTVKNADRIIV 209
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDeeniEESLAEIIEERKSQ-KNFQLIVITHDEELVDAADHIYR 194
|
...
1MT0_A 210 MEK 212
Cdd:cd03240 195 VEK 197
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-171 |
1.07e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 42.69 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKpDSPvILDNINLSIKQGEVIGIVGRSGSGKSTLTKLI-----QRFyipENGQVLIdGHDLALADPNW-L 75
Cdd:PRK10938 261 IVLNNGVVSYN-DRP-ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpQGY---SNDLTLF-GRRRGSGETIWdI 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 76 RRQVGVVLQDNVLLNRsiidnISlanpgMSVEKVIyaakLAGAHDFIS----------ELREGYNTIVGEQGA------- 138
Cdd:PRK10938 335 KKHIGYVSSSLHLDYR-----VS-----TSVRNVI----LSGFFDSIGiyqavsdrqqKLAQQWLDILGIDKRtadapfh 400
|
170 180 190
....*....|....*....|....*....|....
1MT0_A 139 GLSGGQrQRIA-IARALVNNPKILIFDEATSALD 171
Cdd:PRK10938 401 SLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLD 433
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-171 |
1.39e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.80 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 2 ITFRNIRFRYKpdSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDlaLADPNWlRRQV-- 79
Cdd:NF033858 2 ARLEGVSHRYG--KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGD--MADARH-RRAVcp 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 80 -------GvvLQDNVLLNRSIIDNISlanpgmsvekviYAAKLAGaHDF------ISELREGynTivG-----EQGAG-L 140
Cdd:NF033858 77 riaympqG--LGKNLYPTLSVFENLD------------FFGRLFG-QDAaerrrrIDELLRA--T--GlapfaDRPAGkL 137
|
170 180 190
....*....|....*....|....*....|.
1MT0_A 141 SGGQRQRIAIARALVNNPKILIFDEATSALD 171
Cdd:NF033858 138 SGGMKQKLGLCCALIHDPDLLILDEPTTGVD 168
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
138-240 |
2.96e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 138 AGLSGGQRQRIAIARALVNNPK--ILIFDEATSALDYESEHVIMRNMHKI-CKGRTVIIIAHRLSTVKNADRIIVMEK-- 212
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLrDQGNTVLLVEHDEQMISLADRIIDIGPga 554
|
90 100 110
....*....|....*....|....*....|...
1MT0_A 213 ----GKIVEQGKHKELLSEPESLY-SYLYQLQS 240
Cdd:PRK00635 555 gifgGEVLFNGSPREFLAKSDSLTaKYLRQELT 587
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
11-173 |
5.44e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 40.70 E-value: 5.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 11 YKPDSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLI---------DGHDLALaDPNwlrrqvgv 81
Cdd:PRK11147 327 YQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCgtklevayfDQHRAEL-DPE-------- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 82 vlqdnvllnRSIIDNisLANPGMSVEkvIYAAK---LAGAHDFI-SELREgyNTIVgeqgAGLSGGQRQRIAIARALVNN 157
Cdd:PRK11147 398 ---------KTVMDN--LAEGKQEVM--VNGRPrhvLGYLQDFLfHPKRA--MTPV----KALSGGERNRLLLARLFLKP 458
|
170
....*....|....*.
1MT0_A 158 PKILIFDEATSALDYE 173
Cdd:PRK11147 459 SNLLILDEPTNDLDVE 474
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
34-204 |
6.45e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.47 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 34 IVGRSGSGKSTLTKLIQRFYIPENGQVLIDGHDL-ALADP--NWLRRQVGVVLQDNVLLNRSIIDNISlaNPGMSVEKVI 110
Cdd:PRK13541 31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNInNIAKPycTYIGHNLGLKLEMTVFENLKFWSEIY--NSAETLYAAI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 111 YAAKLagaHDFISElregyntivgeQGAGLSGGQRQRIAIARALVNNPKILIFDEATSALDYESEHvIMRNM--HKICKG 188
Cdd:PRK13541 109 HYFKL---HDLLDE-----------KCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRD-LLNNLivMKANSG 173
|
170
....*....|....*.
1MT0_A 189 RTVIIIAHRLSTVKNA 204
Cdd:PRK13541 174 GIVLLSSHLESSIKSA 189
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-238 |
8.94e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.20 E-value: 8.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 133 VGEQGAGLSGGQRQRIAIARALVNNPK---ILIFDEATSALDYESEHVIMRNMHK-ICKGRTVIIIAHRLSTVKNADRII 208
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTlVSLGHSVIYIDHDPALLKQADYLI 1772
|
90 100 110
....*....|....*....|....*....|....*..
1MT0_A 209 VM------EKGKIVEQGKHKEL-LSEPESLYSYLYQL 238
Cdd:PRK00635 1773 EMgpgsgkTGGKILFSGPPKDIsASKDSLLKTYMCNL 1809
|
|
| MobB |
COG1763 |
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; ... |
31-52 |
9.06e-04 |
|
Molybdopterin-guanine dinucleotide biosynthesis protein [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 441369 [Multi-domain] Cd Length: 162 Bit Score: 38.62 E-value: 9.06e-04
10 20
....*....|....*....|...
1MT0_A 31 VIGIVGRSGSGKSTL-TKLIQRF 52
Cdd:COG1763 3 VLGIVGYSGSGKTTLlEKLIPEL 25
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
140-231 |
2.02e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.24 E-value: 2.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 140 LSGGQRQRI----AIARALVNnpkIL-IFDEATSAL---DyeSEHVI-----MRNMhkickGRTVIIIAHRLSTVKNADR 206
Cdd:COG0178 486 LSGGEAQRIrlatQIGSGLVG---VLyVLDEPSIGLhqrD--NDRLIetlkrLRDL-----GNTVIVVEHDEDTIRAADY 555
|
90 100 110
....*....|....*....|....*....|.
1MT0_A 207 IIVM------EKGKIVEQGKHKELLSEPESL 231
Cdd:COG0178 556 IIDIgpgageHGGEVVAQGTPEEILKNPDSL 586
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
14-225 |
2.97e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 38.33 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 14 DSPVILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQV----------LIDGH------DLALADpnWLR- 76
Cdd:PRK15064 330 DNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkwsenanigyYAQDHaydfenDLTLFD--WMSq 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 77 -RQVGvvlqDNVLLNRSIIDNIslanpgmsvekviyaakLAGAHDfiselregyntiVGEQGAGLSGGQRQRIAIARALV 155
Cdd:PRK15064 408 wRQEG----DDEQAVRGTLGRL-----------------LFSQDD------------IKKSVKVLSGGEKGRMLFGKLMM 454
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1MT0_A 156 NNPKILIFDEATSALDYESehvI--MRNMHKICKGrTVIIIAHRLSTVKN-ADRIIVMEKGKIVE-QGKHKELL 225
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDMES---IesLNMALEKYEG-TLIFVSHDREFVSSlATRIIEITPDGVVDfSGTYEEYL 524
|
|
| Udk |
COG0572 |
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ... |
31-61 |
3.14e-03 |
|
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage
Pssm-ID: 440337 [Multi-domain] Cd Length: 206 Bit Score: 37.51 E-value: 3.14e-03
10 20 30
....*....|....*....|....*....|.
1MT0_A 31 VIGIVGRSGSGKSTLTKLIQRFYIPENGQVL 61
Cdd:COG0572 9 IIGIAGPSGSGKTTFARRLAEQLGADKVVVI 39
|
|
| CooC |
COG3640 |
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, ... |
32-73 |
3.29e-03 |
|
CO dehydrogenase nickel-insertion accessory protein CooC1 [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 442857 [Multi-domain] Cd Length: 249 Bit Score: 37.84 E-value: 3.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
1MT0_A 32 IGIVGRSGSGKSTLTKLIQRFYIPENGQVL-IDghdlalADPN 73
Cdd:COG3640 3 IAVAGKGGVGKTTLSALLARYLAEKGKPVLaVD------ADPN 39
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
17-173 |
4.16e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 37.79 E-value: 4.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 17 VILDNINLSIKQGEVIGIVGRSGSGKSTLTKLIQRFYIPENGQVLIdGHDLaladpnwlrrQVGVVLQdnvllNRSIIDn 96
Cdd:PRK11819 338 LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLAYVDQ-----SRDALD- 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1MT0_A 97 islanPGMSVEKVIyaaklAGAHDFIselREGYNTI-------------------VGEqgagLSGGQRQRIAIARALVNN 157
Cdd:PRK11819 401 -----PNKTVWEEI-----SGGLDII---KVGNREIpsrayvgrfnfkggdqqkkVGV----LSGGERNRLHLAKTLKQG 463
|
170
....*....|....*.
1MT0_A 158 PKILIFDEATSALDYE 173
Cdd:PRK11819 464 GNVLLLDEPTNDLDVE 479
|
|
| MobB |
pfam03205 |
Molybdopterin guanine dinucleotide synthesis protein B; This protein contains a P-loop. |
31-52 |
4.51e-03 |
|
Molybdopterin guanine dinucleotide synthesis protein B; This protein contains a P-loop.
Pssm-ID: 427196 [Multi-domain] Cd Length: 133 Bit Score: 36.37 E-value: 4.51e-03
10 20
....*....|....*....|...
1MT0_A 31 VIGIVGRSGSGKSTL-TKLIQRF 52
Cdd:pfam03205 1 ILGIVGWSGSGKTTLlEKLIPEL 23
|
|
| PRK07429 |
PRK07429 |
phosphoribulokinase; Provisional |
12-57 |
5.51e-03 |
|
phosphoribulokinase; Provisional
Pssm-ID: 180975 Cd Length: 327 Bit Score: 37.30 E-value: 5.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
1MT0_A 12 KPDSPVIldninlsikqgevIGIVGRSGSGKSTLTKLIQRFYIPEN 57
Cdd:PRK07429 4 MPDRPVL-------------LGVAGDSGCGKTTFLRGLADLLGEEL 36
|
|
| PRK |
cd02026 |
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or ... |
31-61 |
6.01e-03 |
|
Phosphoribulokinase (PRK) is an enzyme involved in the Benson-Calvin cycle in chloroplasts or photosynthetic prokaryotes. This enzyme catalyzes the phosphorylation of D-ribulose 5-phosphate to form D-ribulose 1, 5-biphosphate, using ATP and NADPH produced by the primary reactions of photosynthesis.
Pssm-ID: 238984 [Multi-domain] Cd Length: 273 Bit Score: 36.93 E-value: 6.01e-03
10 20 30
....*....|....*....|....*....|.
1MT0_A 31 VIGIVGRSGSGKSTLTKLIQRFYIPENGQVL 61
Cdd:cd02026 1 IIGVAGDSGCGKSTFLRRLTSLFGSDLVTVI 31
|
|
| VirB11-like_ATPase |
cd01130 |
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ... |
24-76 |
6.27e-03 |
|
Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, and related ATPases. The homohexamer, VirB11 is one of eleven Vir (virulence) proteins, which are required for T-pilus biogenesis and virulence in the transfer of T-DNA from the bacterial Ti (tumor-inducing)-plasmid into plant cells. The pilus is a fibrous cell surface organelle, which mediates adhesion between bacteria during conjugative transfer or between bacteria and host eukaryotic cells during infection. VirB11-related ATPases include Sulfolobus acidocaldarius FlaI, which plays key roles in archaellum (archaeal flagellum) assembly and motility functions, and the pilus assembly proteins CpaF/TadA and TrbB. This alignment contains the C-terminal domain, which is the ATPase.
Pssm-ID: 410874 [Multi-domain] Cd Length: 177 Bit Score: 36.36 E-value: 6.27e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
1MT0_A 24 LSIKQGEVIGIVGRSGSGKSTLTKLIQRFyIPENGQVLI--DGHDLALADPNWLR 76
Cdd:cd01130 7 LAVRARKNILISGGTGSGKTTLLNALLSF-IPPDERIVTieDTRELQLPHPNVVH 60
|
|
| PRK07261 |
PRK07261 |
DNA topology modulation protein; |
32-95 |
9.74e-03 |
|
DNA topology modulation protein;
Pssm-ID: 180911 [Multi-domain] Cd Length: 171 Bit Score: 35.85 E-value: 9.74e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
1MT0_A 32 IGIVGRSGSGKSTLTKLIQRFYipeNGQVLidgH-DLALADPNWLRRQV--GVVLQDNVLLNRS-IID 95
Cdd:PRK07261 3 IAIIGYSGSGKSTLARKLSQHY---NCPVL---HlDTLHFQPNWQERDDddMIADISNFLLKHDwIID 64
|
|
| NRK1 |
cd02024 |
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide ... |
31-57 |
9.94e-03 |
|
Nicotinamide riboside kinase (NRK) is an enzyme involved in the metabolism of nicotinamide adenine dinucleotide (NAD+). This enzyme catalyzes the phosphorylation of nicotinamide riboside (NR) to form nicotinamide mononucleotide (NMN). It defines the NR salvage pathway of NAD+ biosynthesis in addition to the pathways through nicotinic acid mononucleotide (NaMN). This enzyme can also phosphorylate the anticancer drug tiazofurin, which is an analog of nicotinamide riboside.
Pssm-ID: 238982 [Multi-domain] Cd Length: 187 Bit Score: 35.76 E-value: 9.94e-03
10 20 30
....*....|....*....|....*....|....*....
1MT0_A 31 VIGIVGRSGSGKSTLTKLIQR------------FYIPEN 57
Cdd:cd02024 1 IVGISGVTNSGKTTLAKLLQRilpnccvihqddFFKPED 39
|
|
| |
