|
Name |
Accession |
Description |
Interval |
E-value |
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
117-356 |
6.01e-168 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 467.79 E-value: 6.01e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 196
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 IVSQEPMLFDCTIAENIAYGDNSRQVphEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQP 276
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKPDATD--EEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 277 QILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLAEKGIYYSLVNVQ 356
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
10-359 |
1.44e-144 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 421.11 E-value: 1.44e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 10 YRNSVKKAHIFGFCFALSQAMMFFTYAGCFRFGAYLVVNGHMQYKSVFLVFSAVVFGAMALGQSSSFAPDYAKAKTSAAH 89
Cdd:COG1132 234 RRANLRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 90 LFLLFERVPSIDSySEEGEKPETFGGSIMIKDVAFNYPnrPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFY 169
Cdd:COG1132 314 IFELLDEPPEIPD-PPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFY 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 170 DPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPMLFDCTIAENIAYGDNsrQVPHEEIVNAAKEANIHSFIDSLPDKYNT 249
Cdd:COG1132 391 DPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRP--DATDEEVEEAAKAAQAHEFIEALPDGYDT 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 250 RVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQ 329
Cdd:COG1132 469 VVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLD 548
|
330 340 350
....*....|....*....|....*....|
gi 1708878085 330 NGKVVEQGTHQQLLAEKGIYYSLVNVQSGS 359
Cdd:COG1132 549 DGRIVEQGTHEELLARGGLYARLYRLQFGE 578
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
11-356 |
1.64e-125 |
|
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: 376.87 E-value: 1.64e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 11 RNSVKKAHIFGFCFALSQAMMFFTYAGCFRFGAYLVVNGHMqykSV--FLVFSAVVFGAMA-LGQSSSFAPDYAKAKTSA 87
Cdd:COG2274 369 NARFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQL---TLgqLIAFNILSGRFLApVAQLIGLLQRFQDAKIAL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 88 AHLFLLFERVPSIDSYSEEGEKPEtFGGSIMIKDVAFNYPNRpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLER 167
Cdd:COG2274 446 ERLDDILDLPPEREEGRSKLSLPR-LKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLG 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 168 FYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPMLFDCTIAENIAYGDnsRQVPHEEIVNAAKEANIHSFIDSLPDKY 247
Cdd:COG2274 524 LYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGD--PDATDEEIIEAARLAGLHDFIEALPMGY 601
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 248 NTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAV 327
Cdd:COG2274 602 DTVVGEGGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIV 681
|
330 340
....*....|....*....|....*....
gi 1708878085 328 VQNGKVVEQGTHQQLLAEKGIYYSLVNVQ 356
Cdd:COG2274 682 LDKGRIVEDGTHEELLARKGLYAELVQQQ 710
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
117-352 |
1.82e-118 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 342.29 E-value: 1.82e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRPEvKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 196
Cdd:cd03251 1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 IVSQEPMLFDCTIAENIAYGDnsRQVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQP 276
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGR--PGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1708878085 277 QILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLAEKGIYYSL 352
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
89-357 |
5.97e-114 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 343.73 E-value: 5.97e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 89 HLFLLFERVPSI-DSyseEGEKPETF-GGSIMIKDVAFNY-PNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL 165
Cdd:COG5265 331 RMFDLLDQPPEVaDA---PDAPPLVVgGGEVRFENVSFGYdPERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 166 ERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPMLFDCTIAENIAYG--DNSRqvphEEIVNAAKEANIHSFIDSL 243
Cdd:COG5265 405 FRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGrpDASE----EEVEAAARAAQIHDFIESL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 244 PDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNAD 323
Cdd:COG5265 481 PDGYDTRVGERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDAD 560
|
250 260 270
....*....|....*....|....*....|....
gi 1708878085 324 KIAVVQNGKVVEQGTHQQLLAEKGIYYSLVNVQS 357
Cdd:COG5265 561 EILVLEAGRIVERGTHAELLAQGGLYAQMWARQQ 594
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
117-356 |
1.15e-111 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 324.95 E-value: 1.15e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPnrPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 196
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 IVSQEPMLFDCTIAENIAYGDNSrqVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQP 276
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRPD--ATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 277 QILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLAEKGIYYSLVNVQ 356
Cdd:cd03253 157 PILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
115-347 |
1.16e-107 |
|
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: 314.55 E-value: 1.16e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 115 GSIMIKDVAFNYpnRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQ 194
Cdd:cd03254 1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 195 IGIVSQEPMLFDCTIAENIAYGDNSRQVphEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVR 274
Cdd:cd03254 79 IGVVLQDTFLFSGTIMENIRLGRPNATD--EEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1708878085 275 QPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLAEKG 347
Cdd:cd03254 157 DPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
41-353 |
2.28e-106 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 327.45 E-value: 2.28e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 41 FGAYLVVNGHMQYKSV--FLVFSavvfgaMALGQS----SSFAPDYAKAKTSAAHLFLLFERVPSIdsySEEGE-KPETF 113
Cdd:TIGR00958 405 YGGQLVLTGKVSSGNLvsFLLYQ------EQLGEAvrvlSYVYSGMMQAVGASEKVFEYLDRKPNI---PLTGTlAPLNL 475
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 114 GGSIMIKDVAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRA 193
Cdd:TIGR00958 476 EGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHR 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 194 QIGIVSQEPMLFDCTIAENIAYGdnSRQVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALV 273
Cdd:TIGR00958 556 QVALVGQEPVLFSGSVRENIAYG--LTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALV 633
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 274 RQPQILLLDEATSALDTESEKIVQEalDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLAEKGIYYSLV 353
Cdd:TIGR00958 634 RKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYKHLV 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
10-356 |
2.84e-103 |
|
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: 315.49 E-value: 2.84e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 10 YRNSVKKAHIFGFCFALSQAMMFFTYAGCFRFGAYLVVNGHMQYKSV--FLVFSavVFGAMALGQSSSFAPDYAKAKTSA 87
Cdd:TIGR02204 231 YEAARQRIRTRALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLgqFVFYA--VMVAGSIGTLSEVWGELQRAAGAA 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 88 AHLFLLFERVPSIDSYSEEGEKPETFGGSIMIKDVAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLER 167
Cdd:TIGR02204 309 ERLIELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLR 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 168 FYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPMLFDCTIAENIAYG--DNSRqvphEEIVNAAKEANIHSFIDSLPD 245
Cdd:TIGR02204 389 FYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGrpDATD----EEVEAAARAAHAHEFISALPE 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 246 KYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKI 325
Cdd:TIGR02204 465 GYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRI 544
|
330 340 350
....*....|....*....|....*....|.
gi 1708878085 326 AVVQNGKVVEQGTHQQLLAEKGIYYSLVNVQ 356
Cdd:TIGR02204 545 VVMDQGRIVAQGTHAELIAKGGLYARLARLQ 575
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
85-356 |
6.97e-101 |
|
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: 309.34 E-value: 6.97e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 85 TSAAHLFLLFERVPSIDSYSEEGEKPEtfgGSIMIKDVAFNYPNRpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQL 164
Cdd:TIGR02203 302 AAAESLFTLLDSPPEKDTGTRAIERAR---GDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 165 LERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPMLFDCTIAENIAYGDnSRQVPHEEIVNAAKEANIHSFIDSLP 244
Cdd:TIGR02203 378 IPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFNDTIANNIAYGR-TEQADRAEIERALAAAYAQDFVDKLP 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 245 DKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADK 324
Cdd:TIGR02203 457 LGLDTPIGENGVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADR 536
|
250 260 270
....*....|....*....|....*....|..
gi 1708878085 325 IAVVQNGKVVEQGTHQQLLAEKGIYYSLVNVQ 356
Cdd:TIGR02203 537 IVVMDDGRIVERGTHNELLARNGLYAQLHNMQ 568
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
26-347 |
6.40e-100 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 306.30 E-value: 6.40e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 26 LSQAMM-FFTYAG--------CFRFgaylvVNGHMQYKSVFLVF--SAVVFGAM-ALGQsssfapDY---AKAKTSAAHL 90
Cdd:COG4988 243 LSSAVLeFFASLSialvavyiGFRL-----LGGSLTLFAALFVLllAPEFFLPLrDLGS------FYharANGIAAAEKI 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 91 FLLFERVPSIdsySEEGEKPETFGGSIMI--KDVAFNYPNRPEVkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERF 168
Cdd:COG4988 312 FALLDAPEPA---APAGTAPLPAAGPPSIelEDVSFSYPGGRPA--LDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGF 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 169 YDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPMLFDCTIAENIAYGDnsRQVPHEEIVNAAKEANIHSFIDSLPDKYN 248
Cdd:COG4988 387 LPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGR--PDASDEELEAALEAAGLDEFVAALPDGLD 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 249 TRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVV 328
Cdd:COG4988 465 TPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVL 544
|
330
....*....|....*....
gi 1708878085 329 QNGKVVEQGTHQQLLAEKG 347
Cdd:COG4988 545 DDGRIVEQGTHEELLAKNG 563
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
25-352 |
2.98e-94 |
|
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: 292.06 E-value: 2.98e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 25 ALSQAMMFFTYAGCFRFGAYLVVNGHMQykSVFLVfsAVVFGAMALGQSssFAP------DYAKAKTSAAHLFLLFERVP 98
Cdd:COG4987 244 ALLQLAAGLAVVAVLWLAAPLVAAGALS--GPLLA--LLVLAALALFEA--LAPlpaaaqHLGRVRAAARRLNELLDAPP 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 99 SIDSYSEEGEKPEtfGGSIMIKDVAFNYPNRPEvKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLF 178
Cdd:COG4987 318 AVTEPAEPAPAPG--GPSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITL 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 179 DGKNAKTLNIQWLRAQIGIVSQEPMLFDCTIAENIAYGDNsrQVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQL 258
Cdd:COG4987 395 GGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARP--DATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRL 472
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 259 SGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGT 338
Cdd:COG4987 473 SGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGT 552
|
330
....*....|....
gi 1708878085 339 HQQLLAEKGIYYSL 352
Cdd:COG4987 553 HEELLAQNGRYRQL 566
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
63-358 |
2.47e-93 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 290.00 E-value: 2.47e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 63 VVFGAM-ALGQ--------SSSFAPDYAKAKTsaahLFLLFERVPSIDSYSEEGEKPEtfgGSIMIKDVAFNYPNRpEVK 133
Cdd:PRK11176 286 VVFSSMiALMRplksltnvNAQFQRGMAACQT----LFAILDLEQEKDEGKRVIERAK---GDIEFRNVTFTYPGK-EVP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 134 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPMLFDCTIAENI 213
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNVHLFNDTIANNI 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 214 AYGDNsRQVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESE 293
Cdd:PRK11176 438 AYART-EQYSREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESE 516
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1708878085 294 KIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLAEKGIYYSLVNVQSG 358
Cdd:PRK11176 517 RAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLAQNGVYAQLHKMQFG 581
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
117-356 |
2.01e-91 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 273.59 E-value: 2.01e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNY-PNRPEvkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQI 195
Cdd:cd03252 1 ITFEHVRFRYkPDGPV--ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 196 GIVSQEPMLFDCTIAENIAYGDNSrqVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQ 275
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPG--MSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHN 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 276 PQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLAEKGIYYSLVNV 355
Cdd:cd03252 157 PRILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQL 236
|
.
gi 1708878085 356 Q 356
Cdd:cd03252 237 Q 237
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
25-353 |
3.95e-89 |
|
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: 282.60 E-value: 3.95e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 25 ALSQAMMFFTYAGCFRFGAYLVVNGHMQ------YKSVFLVFSAVVFGAMALGQS-SSFAPDYAKAKTSAAH-LFLLFER 96
Cdd:TIGR03796 381 VLPTLLTSLNSALILVVGGLRVMEGQLTigmlvaFQSLMSSFLEPVNNLVGFGGTlQELEGDLNRLDDVLRNpVDPLLEE 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 97 VPSIDSYSEEGEKPEtfgGSIMIKDVAFNYpNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEM 176
Cdd:TIGR03796 461 PEGSAATSEPPRRLS---GYVELRNITFGY-SPLEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEI 536
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 177 LFDGKNAKTLNIQWLRAQIGIVSQEPMLFDCTIAENIAYGDNSrqVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGT 256
Cdd:TIGR03796 537 LFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTLWDPT--IPDADLVRACKDAAIHDVITSRPGGYDAELAEGGA 614
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 257 QLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALdkAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQ 336
Cdd:TIGR03796 615 NLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNL--RRRGCTCIIVAHRLSTIRDCDEIIVLERGKVVQR 692
|
330
....*....|....*..
gi 1708878085 337 GTHQQLLAEKGIYYSLV 353
Cdd:TIGR03796 693 GTHEELWAVGGAYARLI 709
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
110-333 |
7.98e-89 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 266.64 E-value: 7.98e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 110 PETFGGSIMIKDVAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQ 189
Cdd:cd03248 5 PDHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 190 WLRAQIGIVSQEPMLFDCTIAENIAYGdnSRQVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIA 269
Cdd:cd03248 85 YLHSKVSLVGQEPVLFARSLQDNIAYG--LQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1708878085 270 RALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKV 333
Cdd:cd03248 163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
39-356 |
1.02e-88 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 278.38 E-value: 1.02e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 39 FRFGAYLVVNGHMqykSVFLVFSAVVFGAMALG---QSSSFAPDYAKAKTSAAHLFLLFERVPSIDSySEEGEKPETFGG 115
Cdd:PRK13657 258 LVLGAALVQKGQL---RVGEVVAFVGFATLLIGrldQVVAFINQVFMAAPKLEEFFEVEDAVPDVRD-PPGAIDLGRVKG 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 116 SIMIKDVAFNYPNRPEVkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQI 195
Cdd:PRK13657 334 AVEFDDVSFSYDNSRQG--VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNI 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 196 GIVSQEPMLFDCTIAENIAYG--DNSrqvpHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALV 273
Cdd:PRK13657 412 AVVFQDAGLFNRSIEDNIRVGrpDAT----DEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALL 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 274 RQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLAEKGIYYSLV 353
Cdd:PRK13657 488 KDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVARGGRFAALL 567
|
...
gi 1708878085 354 NVQ 356
Cdd:PRK13657 568 RAQ 570
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
117-332 |
2.95e-88 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 263.09 E-value: 2.95e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRPEvKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 196
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 IVSQEPMLFDCTIAENIaygdnsrqvpheeivnaakeanihsfidslpdkyntrvgdkgtqLSGGQKQRIAIARALVRQP 276
Cdd:cd03228 80 YVPQDPFLFSGTIRENI--------------------------------------------LSGGQRQRIAIARALLRDP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1708878085 277 QILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGK 332
Cdd:cd03228 116 PILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
41-358 |
2.93e-84 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 269.30 E-value: 2.93e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 41 FGAYLVVNGHMQyksvflVFSAVVFGAMAlGQSSSFAPDYAKAKTSAAHLFLLFERVPSI-DSYSEEGEK-----PEtFG 114
Cdd:TIGR01846 382 FGAHLVIGGALS------PGQLVAFNMLA-GRVTQPVLRLAQLWQDFQQTGIALERLGDIlNSPTEPRSAglaalPE-LR 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 115 GSIMIKDVAFNY-PNRPEVkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRA 193
Cdd:TIGR01846 454 GAITFENIRFRYaPDSPEV--LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRR 531
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 194 QIGIVSQEPMLFDCTIAENIAYGDNsrQVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALV 273
Cdd:TIGR01846 532 QMGVVLQENVLFSRSIRDNIALCNP--GAPFEHVIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALV 609
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 274 RQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLAEKGIYYSLV 353
Cdd:TIGR01846 610 GNPRILIFDEATSALDYESEALIMRNMREICRGRTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQGLYARLW 689
|
....*
gi 1708878085 354 NVQSG 358
Cdd:TIGR01846 690 QQQSG 694
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
33-356 |
6.54e-74 |
|
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: 241.78 E-value: 6.54e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 33 FTYAGCFRFGAYLVVNGHMQYKSvFLVFSAvvfgamALGQSSSFAPDYAKAKTSAAHLFLLFERV-PSIDS---YSEEGE 108
Cdd:TIGR03797 371 LTSAALFAAAISLLGGAGLSLGS-FLAFNT------AFGSFSGAVTQLSNTLISILAVIPLWERAkPILEAlpeVDEAKT 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 109 KPETFGGSIMIKDVAFNY-PNRPevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN 187
Cdd:TIGR03797 444 DPGKLSGAIEVDRVTFRYrPDGP--LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLD 521
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 188 IQWLRAQIGIVSQEPMLFDCTIAENIAYGDnsrQVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIA 267
Cdd:TIGR03797 522 VQAVRRQLGVVLQNGRLMSGSIFENIAGGA---PLTLDEAWEAARMAGLAEDIRAMPMGMHTVISEGGGTLSGGQRQRLL 598
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 268 IARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRtcIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLAEKG 347
Cdd:TIGR03797 599 IARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRVVQQGTYDELMAREG 676
|
....*....
gi 1708878085 348 IYYSLVNVQ 356
Cdd:TIGR03797 677 LFAQLARRQ 685
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
115-337 |
6.93e-72 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 223.24 E-value: 6.93e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 115 GSIMIKDVAFNYPNRpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQ 194
Cdd:cd03245 1 GRIEFRNVSFSYPNQ-EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 195 IGIVSQEPMLFDCTIAENIAYGDNSrqVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVR 274
Cdd:cd03245 80 IGYVPQDVTLFYGTLRDNITLGAPL--ADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLN 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1708878085 275 QPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQG 337
Cdd:cd03245 158 DPPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
12-361 |
1.90e-69 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 236.46 E-value: 1.90e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 12 NSVKKAHIfgfcfALSQAMMFFTYAGCFRFGAYLVV--------NGHMQYKSVFLVFSAVVFGAMALGQSSSFAPDYAKA 83
Cdd:PTZ00265 277 NFMESLHI-----GMINGFILASYAFGFWYGTRIIIsdlsnqqpNNDFHGGSVISILLGVLISMFMLTIILPNITEYMKS 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 84 KTSAAHLFLLFERVPSIDSySEEGEKPETFGgSIMIKDVAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQ 163
Cdd:PTZ00265 352 LEATNSLYEIINRKPLVEN-NDDGKKLKDIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILK 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 164 LLERFYDPLDGEMLF-DGKNAKTLNIQWLRAQIGIVSQEPMLFDCTIAENIAY------------------------GDN 218
Cdd:PTZ00265 430 LIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYslyslkdlealsnyynedgndsqeNKN 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 219 SRQ-------------------------------VPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIA 267
Cdd:PTZ00265 510 KRNscrakcagdlndmsnttdsneliemrknyqtIKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQKQRIS 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 268 IARALVRQPQILLLDEATSALDTESEKIVQEALD--KAREGRTCIVIAHRLSTIQNADKIAVVQNGK------------- 332
Cdd:PTZ00265 590 IARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIFVLSNRErgstvdvdiiged 669
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1708878085 333 ----------------------------------VVEQGTHQQLLAEK-GIYYSLVNVQSGSCN 361
Cdd:PTZ00265 670 ptkdnkennnknnkddnnnnnnnnnnkinnagsyIIEQGTHDALMKNKnGIYYTMINNQKVSSK 733
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
115-338 |
1.28e-68 |
|
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: 214.66 E-value: 1.28e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 115 GSIMIKDVAFNY-PNRPEVkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRA 193
Cdd:cd03244 1 GDIEFKNVSLRYrPNLPPV--LKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 194 QIGIVSQEPMLFDCTIAENIaygDNSRQVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALV 273
Cdd:cd03244 79 RISIIPQDPVLFSGTIRSNL---DPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1708878085 274 RQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGT 338
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
11-355 |
2.88e-68 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 233.00 E-value: 2.88e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 11 RNSVKKAHIFGFcfalSQAMMFFTYAGCFRFGAYLVVNGHMQYKSVFLVFSAVVFGAMALGQSSSFAPDYAKAKTSAAHL 90
Cdd:PTZ00265 1061 RKTLVNSMLWGF----SQSAQLFINSFAYWFGSFLIRRGTILVDDFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKY 1136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 91 FLLFERVPSIDSYSEEG---EKPETFGGSIMIKDVAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLER 167
Cdd:PTZ00265 1137 YPLIIRKSNIDVRDNGGiriKNKNDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMR 1216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 168 FYDPLD------------------------------------------------------GEMLFDGKNAKTLNIQWLRA 193
Cdd:PTZ00265 1217 FYDLKNdhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfknsGKILLDGVDICDYNLKDLRN 1296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 194 QIGIVSQEPMLFDCTIAENIAYGdnSRQVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALV 273
Cdd:PTZ00265 1297 LFSIVSQEPMLFNMSIYENIKFG--KEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALL 1374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 274 RQPQILLLDEATSALDTESEKIVQEAL----DKAreGRTCIVIAHRLSTIQNADKIAVVQN----GKVVE-QGTHQQLL- 343
Cdd:PTZ00265 1375 REPKILLLDEATSSLDSNSEKLIEKTIvdikDKA--DKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLs 1452
|
410
....*....|..
gi 1708878085 344 AEKGIYYSLVNV 355
Cdd:PTZ00265 1453 VQDGVYKKYVKL 1464
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
42-345 |
6.66e-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: 223.09 E-value: 6.66e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 42 GAYLVVNGHMqykSVFLVFSAVVFGAMAL-------GQSSSFApdyaKAKTSAAHLFLLFERVPsidsysEEGE-----K 109
Cdd:COG4618 260 GAYLVIQGEI---TPGAMIAASILMGRALapieqaiGGWKQFV----SARQAYRRLNELLAAVP------AEPErmplpR 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 110 PEtfgGSIMIKDVAFNYPNRPEVkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKtlniQ 189
Cdd:COG4618 327 PK---GRLSVENLTVVPPGSKRP-ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLS----Q 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 190 WLRAQ----IGIVSQEPMLFDCTIAENIA-YGDnsrqVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQ 264
Cdd:COG4618 399 WDREElgrhIGYLPQDVELFDGTIAENIArFGD----ADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQ 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 265 RIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKARE-GRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLL 343
Cdd:COG4618 475 RIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKArGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
..
gi 1708878085 344 AE 345
Cdd:COG4618 555 AR 556
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
114-356 |
1.33e-66 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 220.75 E-value: 1.33e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 114 GGSIMIKDVAFNYpnRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRA 193
Cdd:PRK10790 338 SGRIDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 194 QIGIVSQEPMLFDCTIAENIAYGdnsRQVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALV 273
Cdd:PRK10790 416 GVAMVQQDPVVLADTFLANVTLG---RDISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLV 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 274 RQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLAEKGIYYSLV 353
Cdd:PRK10790 493 QTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMY 572
|
...
gi 1708878085 354 NVQ 356
Cdd:PRK10790 573 QLQ 575
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
63-349 |
1.86e-66 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 219.58 E-value: 1.86e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 63 VVFGAMALGQSSSFA--------PDYAKA-------KTSAAH--LFLLFERVPSIDsyseEGEKPETFGGSIMIKDV-AF 124
Cdd:PRK10789 246 VVNGSLTLGQLTSFVmylglmiwPMLALAwmfniveRGSAAYsrIRAMLAEAPVVK----DGSEPVPEGRGELDVNIrQF 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 125 NYPNRpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPML 204
Cdd:PRK10789 322 TYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFL 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 205 FDCTIAENIAYGD-NSRQvphEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDE 283
Cdd:PRK10789 401 FSDTVANNIALGRpDATQ---QEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDD 477
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1708878085 284 ATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLAEKGIY 349
Cdd:PRK10789 478 ALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWY 543
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
46-328 |
2.59e-66 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 218.31 E-value: 2.59e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 46 VVNGHMQYKSVFLVFSAV--VFgaMALGQSSSFAPDYAKAKTSAAHLFLLFERVPSIdsYSEEGEKPETFGGSIMIKDVA 123
Cdd:TIGR02857 253 LLAGDLDLATGLFVLLLApeFY--LPLRQLGAQYHARADGVAAAEALFAVLDAAPRP--LAGKAPVTAAPASSLEFSGVS 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 124 FNYPNRPEVkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPM 203
Cdd:TIGR02857 329 VAYPGRRPA--LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPF 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 204 LFDCTIAENIAYGDnsRQVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDE 283
Cdd:TIGR02857 407 LFAGTIAENIRLAR--PDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDE 484
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1708878085 284 ATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVV 328
Cdd:TIGR02857 485 PTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
63-352 |
3.39e-64 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 213.92 E-value: 3.39e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 63 VVFGAMA--------------LGQSSsfapdyakakTSAAHLFLLFERVPSIDSYSEEGEKPETfgGSIMIKDVAFNYPN 128
Cdd:PRK11160 283 FVFAALAafealmpvagafqhLGQVI----------ASARRINEITEQKPEVTFPTTSTAAADQ--VSLTLNNVSFTYPD 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 129 RPEvKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPMLFDCT 208
Cdd:PRK11160 351 QPQ-PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSAT 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 209 IAENIAYGDNsrQVPHEEIVNAAKEANIHSFIDSlPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSAL 288
Cdd:PRK11160 430 LRDNLLLAAP--NASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGL 506
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1708878085 289 DTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLAEKGIYYSL 352
Cdd:PRK11160 507 DAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQL 570
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
97-355 |
9.94e-62 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 209.98 E-value: 9.94e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 97 VPSIDSYSEEGEKPETFGGSIMIKDVAFNYP-NRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGE 175
Cdd:TIGR01193 454 VDSEFINKKKRTELNNLNGDIVINDVSYSYGyGSN---ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGE 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 176 MLFDGKNAKTLNIQWLRAQIGIVSQEPMLFDCTIAENIAYGdNSRQVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKG 255
Cdd:TIGR01193 531 ILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLG-AKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEG 609
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 256 TQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREgRTCIVIAHRLSTIQNADKIAVVQNGKVVE 335
Cdd:TIGR01193 610 SSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIE 688
|
250 260
....*....|....*....|
gi 1708878085 336 QGTHQQLLAEKGIYYSLVNV 355
Cdd:TIGR01193 689 QGSHDELLDRNGFYASLIHN 708
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
130-360 |
3.13e-60 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 203.54 E-value: 3.13e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 130 PEVKILQG-LNLKVEKGQTLALVGSSGCGKSTVVQLLERFYdPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPMLFDCT 208
Cdd:PRK11174 360 PDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 209 IAENIAYGDNsrQVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSAL 288
Cdd:PRK11174 439 LRDNVLLGNP--DASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1708878085 289 DTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLAEKGIYYSLVNVQSGSC 360
Cdd:PRK11174 517 DAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQEEI 588
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
117-346 |
2.71e-56 |
|
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: 183.30 E-value: 2.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNrpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 196
Cdd:COG1122 1 IELENLSFSYPG--GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 IVSQEP--MLFDCTIAENIAYGDNSRQVPHEEIVNAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIAR 270
Cdd:COG1122 79 LVFQNPddQLFAPTVEEDVAFGPENLGLPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIAG 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1708878085 271 ALVRQPQILLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLSTI-QNADKIAVVQNGKVVEQGTHQQLLAEK 346
Cdd:COG1122 148 VLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
117-342 |
7.17e-56 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 182.38 E-value: 7.17e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYD-----PLDGEMLFDGKNAKTLNIQ-- 189
Cdd:cd03260 1 IELRDLNVYYGDK---HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 190 WLRAQIGIVSQEPMLFDCTIAENIAYGDN-----SRQVPHEEIVNAAKEANihsfidsLPDKYNTRVgdKGTQLSGGQKQ 264
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLRlhgikLKEELDERVEEALRKAA-------LWDEVKDRL--HALGLSGGQQQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1708878085 265 RIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQL 342
Cdd:cd03260 149 RLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
42-345 |
5.64e-55 |
|
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: 188.71 E-value: 5.64e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 42 GAYLVVNGHMqykSVFLVFSAVVFGAMALG---QSSSFAPDYAKAKTSAAHLFLLFERVPSIDSYSEEGEkPEtfgGSIM 118
Cdd:TIGR01842 246 GAYLAIDGEI---TPGMMIAGSILVGRALApidGAIGGWKQFSGARQAYKRLNELLANYPSRDPAMPLPE-PE---GHLS 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKDVAFNYPNrPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIV 198
Cdd:TIGR01842 319 VENVTIVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 199 SQEPMLFDCTIAENIA-YGDNsrqVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQ 277
Cdd:TIGR01842 398 PQDVELFPGTVAENIArFGEN---ADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGDPK 474
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1708878085 278 ILLLDEATSALDTESEKIVQEALDKAR-EGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLAE 345
Cdd:TIGR01842 475 LVVLDEPNSNLDEEGEQALANAIKALKaRGITVVVITHRPSLLGCVDKILVLQDGRIARFGERDEVLAK 543
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
119-332 |
8.12e-55 |
|
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: 178.81 E-value: 8.12e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKDVAFNYPNRPEvKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIV 198
Cdd:cd03225 2 LKNLSFSYPDGAR-PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 199 SQEP--MLFDCTIAENIAYGDNSRQVPHEEIVNAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARAL 272
Cdd:cd03225 81 FQNPddQFFGPTVEEEVAFGLENLGLPEEEIEERVEEAlelvGLEGLRDRSPF-----------TLSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1708878085 273 VRQPQILLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLSTIQN-ADKIAVVQNGK 332
Cdd:cd03225 150 AMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
95-344 |
7.96e-54 |
|
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: 185.11 E-value: 7.96e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 95 ERVPSIDSYSEEGEKPETFGGSIM-IKDVAFNYPNRP--EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDP 171
Cdd:COG1123 238 AAVPRLGAARGRAAPAAAAAEPLLeVRNLSKRYPVRGkgGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRP 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 172 LDGEMLFDGKNAKTLN---IQWLRAQIGIVSQEPML-FDC--TIAENIAYG-DNSRQVPHEEIVNAAKEAnIH------S 238
Cdd:COG1123 318 TSGSILFDGKDLTKLSrrsLRELRRRVQMVFQDPYSsLNPrmTVGDIIAEPlRLHGLLSRAERRERVAEL-LErvglppD 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 239 FIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALD--KAREGRTCIVIAHRL 316
Cdd:COG1123 397 LADRYPH-----------ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDL 465
|
250 260
....*....|....*....|....*....
gi 1708878085 317 STIQN-ADKIAVVQNGKVVEQGTHQQLLA 344
Cdd:COG1123 466 AVVRYiADRVAVMYDGRIVEDGPTEEVFA 494
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
119-333 |
7.12e-53 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 173.85 E-value: 7.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIV 198
Cdd:COG4619 3 LEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 199 SQEPMLFDCTIAENIAYGDNSRQ-VPHEEIVNAAKEAnihsFidSLPDKY-NTRVgdkgTQLSGGQKQRIAIARALVRQP 276
Cdd:COG4619 80 PQEPALWGGTVRDNLPFPFQLRErKFDRERALELLER----L--GLPPDIlDKPV----ERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 277 QILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLSTIQN-ADKIAVVQNGKV 333
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHDPEQIERvADRVLTLEAGRL 209
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
117-337 |
8.56e-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: 170.19 E-value: 8.56e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRPEvKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwLRAQIG 196
Cdd:cd03247 1 LSINNVSFSYPEQEQ-QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 IVSQEPMLFDCTIAENIaygdnsrqvpheeivnaakeanihsfidslpdkyntrvgdkGTQLSGGQKQRIAIARALVRQP 276
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL-----------------------------------------GRRFSGGERQRLALARILLQDA 117
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1708878085 277 QILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQG 337
Cdd:cd03247 118 PIVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
56-316 |
9.78e-52 |
|
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: 179.86 E-value: 9.78e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 56 VFLVFSAV-VFGAM--ALGQsssfapdYAKAKTSAAHLFLLFERVPSIDSYSEEGEKPETFGG-SIMIKDVAFNYPNRPE 131
Cdd:TIGR02868 277 VLLPLAAFeAFAALpaAAQQ-------LTRVRAAAERIVEVLDAAGPVAEGSAPAAGAVGLGKpTLELRDLSAGYPGAPP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 132 VkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPMLFDCTIAE 211
Cdd:TIGR02868 350 V--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRE 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 212 NIAYGdnSRQVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTE 291
Cdd:TIGR02868 428 NLRLA--RPDATDEELWAALERVGLADWLRALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAE 505
|
250 260
....*....|....*....|....*
gi 1708878085 292 SEKIVQEALDKAREGRTCIVIAHRL 316
Cdd:TIGR02868 506 TADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
117-333 |
5.30e-51 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 167.78 E-value: 5.30e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRPEVkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 196
Cdd:cd03246 1 LEVENVSFRYPGAEPP-VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 IVSQEPMLFDCTIAENIaygdnsrqvpheeivnaakeanihsfidslpdkyntrvgdkgtqLSGGQKQRIAIARALVRQP 276
Cdd:cd03246 80 YLPQDDELFSGSIAENI--------------------------------------------LSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1708878085 277 QILLLDEATSALDTESEKIVQEALDKARE-GRTCIVIAHRLSTIQNADKIAVVQNGKV 333
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALKAaGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
119-337 |
7.50e-51 |
|
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: 169.22 E-value: 7.50e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKDVAFNYPNRP-EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWL---RAQ 194
Cdd:cd03257 4 VKNLSVSFPTGGgSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 195 IGIVSQEPM-----LFdcTIAENIA-----YGDNSRQVPHEEIVNAAKEA--NIHSFIDSLPDkyntrvgdkgtQLSGGQ 262
Cdd:cd03257 84 IQMVFQDPMsslnpRM--TIGEQIAeplriHGKLSKKEARKEAVLLLLVGvgLPEEVLNRYPH-----------ELSGGQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1708878085 263 KQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKARE--GRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQG 337
Cdd:cd03257 151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
119-344 |
1.51e-49 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 173.55 E-value: 1.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKDVAFNYPNRpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDP---LDGEMLFDGKNAKTLNIQWLRAQI 195
Cdd:COG1123 7 VRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEALRGRRI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 196 GIVSQEPM--LFDCTIAENIAYGDNSRQVPHEEIVNAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIA 269
Cdd:COG1123 86 GMVFQDPMtqLNPVTVGDQIAEALENLGLSRAEARARVLELleavGLERRLDRYPH-----------QLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1708878085 270 RALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLSTI-QNADKIAVVQNGKVVEQGTHQQLLA 344
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
117-344 |
2.18e-48 |
|
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: 163.44 E-value: 2.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRPE-VKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQI 195
Cdd:COG1124 2 LEVRNLSVSYGQGGRrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 196 GIVSQEPML-------FDCTIAE--NIAYGDNSRqvphEEIVNAAKEANIH-SFIDSLPDkyntrvgdkgtQLSGGQKQR 265
Cdd:COG1124 82 QMVFQDPYAslhprhtVDRILAEplRIHGLPDRE----ERIAELLEQVGLPpSFLDRYPH-----------QLSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 266 IAIARALVRQPQILLLDEATSALDTesekIVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGT 338
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDV----SVQaEILNllkdlREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELT 222
|
....*.
gi 1708878085 339 HQQLLA 344
Cdd:COG1124 223 VADLLA 228
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
117-346 |
1.55e-47 |
|
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: 161.83 E-value: 1.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTL-NIQWLRAQI 195
Cdd:TIGR04520 1 IEVENVSFSYPES-EKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEeNLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 196 GIVSQEPmlfD-----CTIAENIAYGDNSRQVPHEEIV----NAAKEANIHSFIDSLPdkyntrvgdkgTQLSGGQKQRI 266
Cdd:TIGR04520 80 GMVFQNP---DnqfvgATVEDDVAFGLENLGVPREEMRkrvdEALKLVGMEDFRDREP-----------HLLSGGQKQRV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 267 AIARALVRQPQILLLDEATSALDTESEKIVQEALDKAR--EGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLA 344
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNkeEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFS 225
|
..
gi 1708878085 345 EK 346
Cdd:TIGR04520 226 QV 227
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
119-337 |
2.72e-47 |
|
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: 159.61 E-value: 2.72e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKDVAFNYPnrpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwlRAQIGIV 198
Cdd:cd03259 3 LKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 199 SQEPMLFD-CTIAENIAYGDNSRQVPHEEIVNAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALV 273
Cdd:cd03259 78 FQDYALFPhLTVAENIAFGLKLRGVPKAEIRARVRELlelvGLEGLLNRYPH-----------ELSGGQQQRVALARALA 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1708878085 274 RQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLS-TIQNADKIAVVQNGKVVEQG 337
Cdd:cd03259 147 REPSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
110-338 |
5.77e-47 |
|
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: 158.73 E-value: 5.77e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 110 PETfgGSIMIKDVAFNY-PNRPEVkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNI 188
Cdd:cd03369 2 PEH--GEIEVENLSVRYaPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 189 QWLRAQIGIVSQEPMLFDCTIAENIaygDNSRQVPHEEIVNAakeanihsfidslpdkynTRVGDKGTQLSGGQKQRIAI 268
Cdd:cd03369 78 EDLRSSLTIIPQDPTLFSGTIRSNL---DPFDEYSDEEIYGA------------------LRVSEGGLNLSQGQRQLLCL 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 269 ARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGT 338
Cdd:cd03369 137 ARALLKRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
117-336 |
8.93e-47 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 158.67 E-value: 8.93e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPN-RPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQL---LERfydPLDGEMLFDGKNAKTLN---IQ 189
Cdd:COG1136 5 LELRNLTKSYGTgEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNIlggLDR---PTSGEVLIDGQDISSLSereLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 190 WLRAQ-IGIVSQEPMLFDC-TIAENIA----YGDNSRQVPHEEIVNAAKEANIHSFIDSLPDkyntrvgdkgtQLSGGQK 263
Cdd:COG1136 82 RLRRRhIGFVFQFFNLLPElTALENVAlpllLAGVSRKERRERARELLERVGLGDRLDHRPS-----------QLSGGQQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1708878085 264 QRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQ 336
Cdd:COG1136 151 QRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
117-336 |
2.46e-46 |
|
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: 157.25 E-value: 2.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNR-PEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNaktlnIQWLRAQI 195
Cdd:cd03293 1 LEVRNVSKTYGGGgGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEP-----VTGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 196 GIVSQEPMLFD-CTIAENIAYGDNSRQVPHEEIvnaakEANIHSFIDslpdkyntRVGDKGT------QLSGGQKQRIAI 268
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEA-----RERAEELLE--------LVGLSGFenayphQLSGGMRQRVAL 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1708878085 269 ARALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLS-TIQNADKIAVVQN--GKVVEQ 336
Cdd:cd03293 143 ARALAVDPDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
119-343 |
2.67e-46 |
|
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: 158.28 E-value: 2.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIV 198
Cdd:COG1120 4 AENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 199 SQEPML-FDCTIAENIAYGdnsRQvPH-----------EEIVNAA-KEANIHSFIDslpdkynTRVgdkgTQLSGGQKQR 265
Cdd:COG1120 81 PQEPPApFGLTVRELVALG---RY-PHlglfgrpsaedREAVEEAlERTGLEHLAD-------RPV----DELSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 266 IAIARALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLS-TIQNADKIAVVQNGKVVEQGTHQQL 342
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225
|
.
gi 1708878085 343 L 343
Cdd:COG1120 226 L 226
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
117-344 |
2.74e-46 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 157.74 E-value: 2.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRP-EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQ---LLERfydPLDGEMLFDGKNAKTLN---IQ 189
Cdd:cd03258 2 IELKNVSKVFGDTGgKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRcinGLER---PTSGSVLVDGTDLTLLSgkeLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 190 WLRAQIGIVSQEPMLFDC-TIAENIAYgdnsrqvPHEeIVNAAKeANIHSFIDSLPDkyntRVG--DKG----TQLSGGQ 262
Cdd:cd03258 79 KARRRIGMIFQHFNLLSSrTVFENVAL-------PLE-IAGVPK-AEIEERVLELLE----LVGleDKAdaypAQLSGGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 263 KQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTH 339
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTV 225
|
....*
gi 1708878085 340 QQLLA 344
Cdd:cd03258 226 EEVFA 230
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
117-338 |
3.35e-46 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 160.63 E-value: 3.35e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRP-EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQ---LLERfydPLDGEMLFDGKNAKTLNIQWLR 192
Cdd:COG1135 2 IELENLSKTFPTKGgPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRcinLLER---PTSGSVLVDGVDLTALSERELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 193 A---QIGIVSQEPMLFD-CTIAENIAY-----GdnsrqVPHEEIvnAAKeanihsfIDSLPDkyntRVG--DKG----TQ 257
Cdd:COG1135 79 AarrKIGMIFQHFNLLSsRTVAENVALpleiaG-----VPKAEI--RKR-------VAELLE----LVGlsDKAdaypSQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 258 LSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKARE--GRTCIVIAHRLSTIQN-ADKIAVVQNGKVV 334
Cdd:COG1135 141 LSGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIV 220
|
....
gi 1708878085 335 EQGT 338
Cdd:COG1135 221 EQGP 224
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
131-344 |
5.55e-46 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 157.08 E-value: 5.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 131 EVKILQGLNLKVEKGQTLALVGSSGCGKSTV---VQLLERfydPLDGEMLFDGKN--AKTLNIQWLRAQIGIVSQEPMLF 205
Cdd:COG1126 13 DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDltDSKKDINKLRRKVGMVFQQFNLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 206 -DCTIAENIAYGD-NSRQVPHEEIVNAAKEAnihsfidsLpdkynTRVG--DKG----TQLSGGQKQRIAIARALVRQPQ 277
Cdd:COG1126 90 pHLTVLENVTLAPiKVKKMSKAEAEERAMEL--------L-----ERVGlaDKAdaypAQLSGGQQQRVAIARALAMEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1708878085 278 ILLLDEATSALDTEsekIVQEALD--K--AREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQLLA 344
Cdd:COG1126 157 VMLFDEPTSALDPE---LVGEVLDvmRdlAKEGMTMVVVTHEMGFAREvADRVVFMDGGRIVEEGPPEEFFE 225
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
117-345 |
7.20e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 156.76 E-value: 7.20e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNrpeVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWlRAQIG 196
Cdd:COG1131 1 IEVRGLTKRYGD---KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV-RRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 IVSQEPMLF-DCTIAENIAYGDNSRQVPHEEIVNAAKEAnIHSFidSLPDKYNTRVGdkgtQLSGGQKQRIAIARALVRQ 275
Cdd:COG1131 77 YVPQEPALYpDLTVRENLRFFARLYGLPRKEARERIDEL-LELF--GLTDAADRKVG----TLSGGMKQRLGLALALLHD 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1708878085 276 PQILLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQLLAE 345
Cdd:COG1131 150 PELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
135-286 |
7.98e-46 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 153.57 E-value: 7.98e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 135 LQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPMLF-DCTIAENI 213
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1708878085 214 AYGdnsrqVPHEEIVNAAKEANIHSFID--SLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATS 286
Cdd:pfam00005 81 RLG-----LLLKGLSKREKDARAEEALEklGLGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
105-352 |
8.34e-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: 167.82 E-value: 8.34e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 105 EEGEKPETF--GGSIMIKDVAFNYpnRPEVK-ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGK 181
Cdd:TIGR00957 1271 QETAPPSGWppRGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGL 1348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 182 NAKTLNIQWLRAQIGIVSQEPMLFDCTIAENIaygDNSRQVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGG 261
Cdd:TIGR00957 1349 NIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL---DPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVG 1425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 262 QKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQ 341
Cdd:TIGR00957 1426 QRQLVCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSN 1505
|
250
....*....|.
gi 1708878085 342 LLAEKGIYYSL 352
Cdd:TIGR00957 1506 LLQQRGIFYSM 1516
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
117-347 |
1.09e-45 |
|
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: 156.56 E-value: 1.09e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNrpeVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIqWLRAQIG 196
Cdd:COG4555 2 IEVENLSKKYGK---VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQIG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 IVSQEPMLFD-CTIAENIAYGDNSRQVPHEEIVNAAKEAnIHSFIdsLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQ 275
Cdd:COG4555 78 VLPDERGLYDrLTVRENIRYFAELYGLFDEELKKRIEEL-IELLG--LEEFLDRRVGE----LSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1708878085 276 PQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIA-HRLSTIQN-ADKIAVVQNGKVVEQGTHQQLLAEKG 347
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSsHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
119-338 |
1.35e-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: 159.49 E-value: 1.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKDVAFNYPnrpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwlRAQIGIV 198
Cdd:COG3842 8 LENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 199 SQEPMLF-DCTIAENIAYGDNSRQVPHEEIVNAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALV 273
Cdd:COG3842 83 FQDYALFpHLTVAENVAFGLRMRGVPKAEIRARVAELlelvGLEGLADRYPH-----------QLSGGQQQRVALARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 274 RQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLS---TIqnADKIAVVQNGKVVEQGT 338
Cdd:COG3842 152 PEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVGT 219
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
117-344 |
2.58e-45 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 154.97 E-value: 2.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN---IQWLRA 193
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSeaeLYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 194 QIGIVSQEPMLFDC-TIAENIAYGDNS-RQVPHEEIVNAAKE----ANIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIA 267
Cdd:cd03261 78 RMGMLFQSGALFDSlTVFENVAFPLREhTRLSEEEIREIVLEkleaVGLRGAEDLYPA-----------ELSGGMKKRVA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 268 IARALVRQPQILLLDEATSALD-TESEKIVQEALD-KAREGRTCIVIAHRLSTI-QNADKIAVVQNGKVVEQGTHQQLLA 344
Cdd:cd03261 147 LARALALDPELLLYDEPTAGLDpIASGVIDDLIRSlKKELGLTSIMVTHDLDTAfAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
119-332 |
1.24e-44 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 150.86 E-value: 1.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIV 198
Cdd:cd00267 2 IENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 199 SQepmlfdctiaeniaygdnsrqvpheeivnaakeanihsfidslpdkyntrvgdkgtqLSGGQKQRIAIARALVRQPQI 278
Cdd:cd00267 79 PQ---------------------------------------------------------LSGGQRQRVALARALLLNPDL 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1708878085 279 LLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLSTIQNA-DKIAVVQNGK 332
Cdd:cd00267 102 LLLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
117-342 |
4.91e-44 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 152.50 E-value: 4.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYD--P---LDGEMLFDGKN--AKTLNIQ 189
Cdd:COG1117 12 IEVRNLNVYYGDK---QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPgarVEGEILLDGEDiyDPDVDVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 190 WLRAQIGIVSQEPMLFDCTIAENIAYG-----DNSRQVpHEEIV-NAAKEANihsfidsLPDKYNTRVGDKGTQLSGGQK 263
Cdd:COG1117 89 ELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgIKSKSE-LDEIVeESLRKAA-------LWDEVKDRLKKSALGLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 264 QRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREgRTCIVI-------AHRLStiqnaDKIAVVQNGKVVEQ 336
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIVIvthnmqqAARVS-----DYTAFFYLGELVEF 234
|
....*.
gi 1708878085 337 GTHQQL 342
Cdd:COG1117 235 GPTEQI 240
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
117-344 |
9.97e-44 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 151.29 E-value: 9.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN---IQWLRA 193
Cdd:COG1127 6 IEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 194 QIGIVSQEPMLFDC-TIAENIAYG-DNSRQVPHEEIVNAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIA 267
Cdd:COG1127 83 RIGMLFQGGALFDSlTVFENVAFPlREHTDLSEAEIRELVLEKlelvGLPGAADKMPS-----------ELSGGMRKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 268 IARALVRQPQILLLDEATSALDTESEKIVQEALDKARE--GRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQLLA 344
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
117-344 |
1.50e-43 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 150.91 E-value: 1.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRPevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 196
Cdd:cd03295 1 IEFENVTKRYGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 IVSQEPMLF-DCTIAENIAYGDNSRQVPHEEIVNAAKEanIHSFIDSLPDKYNTRVGDkgtQLSGGQKQRIAIARALVRQ 275
Cdd:cd03295 79 YVIQQIGLFpHMTVEENIALVPKLLKWPKEKIRERADE--LLALVGLDPAEFADRYPH---ELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1708878085 276 PQILLLDEATSALDTESEKIVQEALDKARE--GRTCIVIAHRL-STIQNADKIAVVQNGKVVEQGTHQQLLA 344
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQelGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
117-348 |
1.82e-43 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 151.30 E-value: 1.82e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 196
Cdd:PRK13632 8 IKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 IVSQEP--MLFDCTIAENIAYGDNSRQVPHEE----IVNAAKEANIHSFIDSLPDKyntrvgdkgtqLSGGQKQRIAIAR 270
Cdd:PRK13632 87 IIFQNPdnQFIGATVEDDIAFGLENKKVPPKKmkdiIDDLAKKVGMEDYLDKEPQN-----------LSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 271 ALVRQPQILLLDEATSALDTESEKIVQEALDKAREGR--TCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLAEKGI 348
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEILNNKEI 235
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
117-332 |
2.31e-43 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 148.10 E-value: 2.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPnrpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQW--LRAQ 194
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 195 IGIVSQEPMLF-DCTIAENIAYGdnsrqvpheeivnaakeanihsfidslpdkyntrvgdkgtqLSGGQKQRIAIARALV 273
Cdd:cd03229 78 IGMVFQDFALFpHLTVLENIALG-----------------------------------------LSGGQQQRVALARALA 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1708878085 274 RQPQILLLDEATSALDTESEKIVQEALD--KAREGRTCIVIAHRLSTIQN-ADKIAVVQNGK 332
Cdd:cd03229 117 MDPDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
117-335 |
6.85e-43 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 149.47 E-value: 6.85e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRP-EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNaktlnIQWLRAQI 195
Cdd:COG1116 8 LELRGVSKRFPTGGgGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKP-----VTGPGPDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 196 GIVSQEPMLFD-CTIAENIAYGDNSRQVPHEEIVNAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIAR 270
Cdd:COG1116 83 GVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERARELlelvGLAGFEDAYPH-----------QLSGGMRQRVAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1708878085 271 ALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAH------RLstiqnADKIAVVQN--GKVVE 335
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFL-----ADRVVVLSArpGRIVE 221
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
117-333 |
1.01e-42 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 148.02 E-value: 1.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYP-NRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN----IQWL 191
Cdd:cd03255 1 IELKNLSKTYGgGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSekelAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 192 RAQIGIVSQE----PMLfdcTIAENIAYGDNSRQVPHEEIVNAAKEAnihsfIDS--LPDKYNTRVGdkgtQLSGGQKQR 265
Cdd:cd03255 81 RRHIGFVFQSfnllPDL---TALENVELPLLLAGVPKKERRERAEEL-----LERvgLGDRLNHYPS----ELSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 266 IAIARALVRQPQILLLDEATSALDTESEKIVQEAL-DKAREGRTCIVIA-HRLSTIQNADKIAVVQNGKV 333
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLrELNKEAGTTIVVVtHDPELAEYADRIIELRDGKI 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
117-344 |
7.60e-42 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 147.47 E-value: 7.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKnakTLNIQ--W-LRA 193
Cdd:PRK13635 6 IRVEHISFRYPDA-ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEEtvWdVRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 194 QIGIVSQEP--MLFDCTIAENIAYGDNSRQVPHEEIVN----AAKEANIHSFIDSLPdkyntrvgdkgTQLSGGQKQRIA 267
Cdd:PRK13635 82 QVGMVFQNPdnQFVGATVQDDVAFGLENIGVPREEMVErvdqALRQVGMEDFLNREP-----------HRLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 268 IARALVRQPQILLLDEATSALDTESEkivQEALD-----KAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQL 342
Cdd:PRK13635 151 IAGVLALQPDIIILDEATSMLDPRGR---REVLEtvrqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
|
..
gi 1708878085 343 LA 344
Cdd:PRK13635 228 FK 229
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
116-343 |
2.28e-41 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 147.99 E-value: 2.28e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 116 SIMIKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQL---LERfydPLDGEMLFDGKNAKTlniqWLR 192
Cdd:COG1118 2 SIEVRNISKRFGSF---TLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDLFT----NLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 193 AQ---IGIVSQEPMLF-DCTIAENIAYGDNSRQVPHEEIVNAAKE----ANIHSFIDSLPdkyntrvgdkgTQLSGGQKQ 264
Cdd:COG1118 72 PRerrVGFVFQHYALFpHMTVAENIAFGLRVRPPSKAEIRARVEEllelVQLEGLADRYP-----------SQLSGGQRQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 265 RIAIARALVRQPQILLLDEATSALDT----ESEKIVQEALDkaREGRTCIVIAH------RLstiqnADKIAVVQNGKVV 334
Cdd:COG1118 141 RVALARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHD--ELGGTTVFVTHdqeealEL-----ADRVVVMNQGRIE 213
|
....*....
gi 1708878085 335 EQGTHQQLL 343
Cdd:COG1118 214 QVGTPDEVY 222
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
117-332 |
2.43e-41 |
|
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: 143.76 E-value: 2.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRPEV--KILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL--ErfYDPLDGEMLFDGKnaktlniqwlr 192
Cdd:cd03250 1 ISVEDASFTWDSGEQEtsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPGS----------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 193 aqIGIVSQEPMLFDCTIAENIAYG---DNSRqvpHEEIVNA-AKEANIhsfiDSLPDKYNTRVGDKGTQLSGGQKQRIAI 268
Cdd:cd03250 68 --IAYVSQEPWIQNGTIRENILFGkpfDEER---YEKVIKAcALEPDL----EILPDGDLTEIGEKGINLSGGQKQRISL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1708878085 269 ARALVRQPQILLLDEATSALDTE-SEKIVQEALDKA-REGRTCIVIAHRLSTIQNADKIAVVQNGK 332
Cdd:cd03250 139 ARAVYSDADIYLLDDPLSAVDAHvGRHIFENCILGLlLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
119-345 |
2.32e-40 |
|
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: 144.81 E-value: 2.32e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKD--VAFNYPNRPeVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPL---DGEMLFDGKNAKTLN---IQW 190
Cdd:COG0444 4 VRNlkVYFPTRRGV-VKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSekeLRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 191 LR-AQIGIVSQEPM-----LFdcTIAENIA-----YGDNSRQVPHEEIVNAAKEANIH---SFIDSLPdkyntrvgdkgT 256
Cdd:COG0444 83 IRgREIQMIFQDPMtslnpVM--TVGDQIAeplriHGGLSKAEARERAIELLERVGLPdpeRRLDRYP-----------H 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 257 QLSGGQKQRIAIARALVRQPQILLLDEATSALDTesekIVQ-EALD-----KAREGRTCIVIAHRLSTI-QNADKIAVVQ 329
Cdd:COG0444 150 ELSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQaQILNllkdlQRELGLAILFITHDLGVVaEIADRVAVMY 225
|
250
....*....|....*.
gi 1708878085 330 NGKVVEQGTHQQLLAE 345
Cdd:COG0444 226 AGRIVEEGPVEELFEN 241
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
135-343 |
2.68e-40 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 142.09 E-value: 2.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 135 LQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwlRAQIGIVSQEPMLF-DCTIAENI 213
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 214 AYGDNSRQVPHEEIvnAAKEANIHSF--IDSLPDKYNTRvgdkgtqLSGGQKQRIAIARALVRQPQILLLDEATSALDTE 291
Cdd:cd03299 93 AYGLKKRKVDKKEI--ERKVLEIAEMlgIDHLLNRKPET-------LSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1708878085 292 SEKIVQEALDKARE--GRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQLL 343
Cdd:cd03299 164 TKEKLREELKKIRKefGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVF 218
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
113-353 |
6.50e-40 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 141.97 E-value: 6.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 113 FGGSIMIKDVAFNYPN--RPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQW 190
Cdd:cd03288 16 LGGEIKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 191 LRAQIGIVSQEPMLFDCTIAENIaygDNSRQVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIAR 270
Cdd:cd03288 93 LRSRLSIILQDPILFSGSIRFNL---DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLAR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 271 ALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLAEK-GIY 349
Cdd:cd03288 170 AFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEdGVF 249
|
....
gi 1708878085 350 YSLV 353
Cdd:cd03288 250 ASLV 253
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
139-345 |
6.92e-40 |
|
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: 142.01 E-value: 6.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 139 NLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRA----QIGIVSQEPMLF-DCTIAENI 213
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 214 AYGDNSRQVPHEEIVNAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPQILLLDEATSALD 289
Cdd:cd03294 124 AFGLEVQGVPRAEREERAAEAlelvGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1708878085 290 TESEKIVQEALDK--AREGRTCIVIAHRLS-TIQNADKIAVVQNGKVVEQGTHQQLLAE 345
Cdd:cd03294 193 PLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
118-335 |
8.90e-40 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 140.19 E-value: 8.90e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 118 MIK--DVAFNYPNRPEVkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN---IQWLR 192
Cdd:COG2884 1 MIRfeNVSKRYPGGREA--LSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKrreIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 193 AQIGIVSQE-PMLFDCTIAENIAY-----GdnsrqVPHEEIVNAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQ 262
Cdd:COG2884 79 RRIGVVFQDfRLLPDRTVYENVALplrvtG-----KSRKEIRRRVREVldlvGLSDKAKALPH-----------ELSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1708878085 263 KQRIAIARALVRQPQILLLDEATSALDTE-SEKIVqEALDKAREGRTCIVIA-HRLSTIQNADK-IAVVQNGKVVE 335
Cdd:COG2884 143 QQRVAIARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRRGTTVLIAtHDLELVDRMPKrVLELEDGRLVR 217
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
117-342 |
1.51e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 140.58 E-value: 1.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRpeVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN---IQWLRA 193
Cdd:COG3638 3 LELRNLSKRYPGG--TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgraLRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 194 QIGIVSQEPMLFD-CTIAENI---AYGDNS------RQVPHEEIvNAAKEAnihsfIDS--LPDKYNTRVGdkgtQLSGG 261
Cdd:COG3638 81 RIGMIFQQFNLVPrLSVLTNVlagRLGRTStwrsllGLFPPEDR-ERALEA-----LERvgLADKAYQRAD----QLSGG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 262 QKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEAL-DKARE-GRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGT 338
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrRIAREdGITVVVNLHQVDLARRyADRIIGLRDGRVVFDGP 230
|
....
gi 1708878085 339 HQQL 342
Cdd:COG3638 231 PAEL 234
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
119-337 |
4.88e-39 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 136.80 E-value: 4.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIV 198
Cdd:cd03214 2 VENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 199 SQepmlfdctiaeniaygdnsrqvpheeivnAAKEANIHSFIDSLpdkYNTrvgdkgtqLSGGQKQRIAIARALVRQPQI 278
Cdd:cd03214 79 PQ-----------------------------ALELLGLAHLADRP---FNE--------LSGGERQRVLLARALAQEPPI 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1708878085 279 LLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLS-TIQNADKIAVVQNGKVVEQG 337
Cdd:cd03214 119 LLLDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
115-342 |
6.89e-39 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 141.36 E-value: 6.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 115 GSIMIKDVAFNYPNrpeVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNaktlnIQWLRAQ 194
Cdd:COG3839 2 ASLELENVSKSYGG---VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRD-----VTDLPPK 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 195 ---IGIVSQEPMLFD-CTIAENIAYGDNSRQVPHEEIVNAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQKQRI 266
Cdd:COG3839 74 drnIAMVFQSYALYPhMTVYENIAFPLKLRKVPKAEIDRRVREAaellGLEDLLDRKPK-----------QLSGGQRQRV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 267 AIARALVRQPQILLLDEATSALD------TESE-KIVQEALdkareGRTCIVIAHRLS---TIqnADKIAVVQNGKVVEQ 336
Cdd:COG3839 143 ALGRALVREPKVFLLDEPLSNLDaklrveMRAEiKRLHRRL-----GTTTIYVTHDQVeamTL--ADRIAVMNDGRIQQV 215
|
....*.
gi 1708878085 337 GTHQQL 342
Cdd:COG3839 216 GTPEEL 221
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
1-100 |
7.61e-39 |
|
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350022 [Multi-domain] Cd Length: 317 Bit Score: 140.66 E-value: 7.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 1 MYREHLHVPYRNSVKKAHIFGFCFALSQAMMFFTYAGCFRFGAYLVVNGHMQYKSVFLVFSAVVFGAMALGQSSSFAPDY 80
Cdd:cd18578 218 KYEEALEEPLKKGLRRALISGLGFGLSQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDI 297
|
90 100
....*....|....*....|
gi 1708878085 81 AKAKTSAAHLFLLFERVPSI 100
Cdd:cd18578 298 AKAKAAAARIFRLLDRKPEI 317
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
117-346 |
3.30e-38 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 136.93 E-value: 3.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNrpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGK---NAKTLNIQWLRA 193
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTdinKLKGKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 194 QIGIVSQEPMLFD-CTIAENI---AYGDNS------RQVPHEEIVNAAkeanihSFIDS--LPDKYNTRVGdkgtQLSGG 261
Cdd:cd03256 79 QIGMIFQQFNLIErLSVLENVlsgRLGRRStwrslfGLFPKEEKQRAL------AALERvgLLDKAYQRAD----QLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 262 QKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEAL-DKARE-GRTCIVIAHRLSTI-QNADKIAVVQNGKVVEQGT 338
Cdd:cd03256 149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLkRINREeGITVIVSLHQVDLArEYADRIVGLKDGRIVFDGP 228
|
....*...
gi 1708878085 339 HQQLLAEK 346
Cdd:cd03256 229 PAELTDEV 236
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
117-345 |
6.37e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 135.99 E-value: 6.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLniqwlRAQIG 196
Cdd:COG1121 7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 IVSQE-------PMlfdcTIAENIAYGdNSRQVP--------HEEIVNAA-KEANIHSFIDslpdkynTRVGdkgtQLSG 260
Cdd:COG1121 79 YVPQRaevdwdfPI----TVRDVVLMG-RYGRRGlfrrpsraDREAVDEAlERVGLEDLAD-------RPIG----ELSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 261 GQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLSTI-QNADKIAVVqNGKVVEQGT 338
Cdd:COG1121 143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVrEYFDRVLLL-NRGLVAHGP 221
|
....*..
gi 1708878085 339 HQQLLAE 345
Cdd:COG1121 222 PEEVLTP 228
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
117-338 |
1.13e-37 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 138.01 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYP-NRPEVKILQGLNLKVEKGQTLALVGSSGCGKST---VVQLLERfydPLDGEMLFDGKNAKTLNIQWLR 192
Cdd:PRK11153 2 IELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 193 A---QIGIVSQE-PMLFDCTIAENIAYgdnsrqvPHEeIVNAAKeANIHSFIDSLPDkyntRVG--DKG----TQLSGGQ 262
Cdd:PRK11153 79 KarrQIGMIFQHfNLLSSRTVFDNVAL-------PLE-LAGTPK-AEIKARVTELLE----LVGlsDKAdrypAQLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1708878085 263 KQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKA-RE-GRTCIVIAHRLSTI-QNADKIAVVQNGKVVEQGT 338
Cdd:PRK11153 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRElGLTIVLITHEMDVVkRICDRVAVIDAGRLVEQGT 224
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
119-333 |
1.36e-37 |
|
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: 132.91 E-value: 1.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwLRAQIGIV 198
Cdd:cd03230 3 VRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-VKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 199 SQEPMLF-DCTIAENIaygdnsrqvpheeivnaakeanihsfidslpdkyntrvgdkgtQLSGGQKQRIAIARALVRQPQ 277
Cdd:cd03230 79 PEEPSLYeNLTVRENL-------------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1708878085 278 ILLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLSTIQN-ADKIAVVQNGKV 333
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
131-344 |
2.58e-37 |
|
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: 140.59 E-value: 2.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 131 EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFyDPLDGEMLFDGKNAKTLN---IQWLRAQIGIVSQEP----- 202
Cdd:COG4172 298 HVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDPfgsls 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 203 --MlfdcTIAENIAYG------DNSRQvPHEEIVNAAKEanihsfidslpdkyntRVG-DKGT------QLSGGQKQRIA 267
Cdd:COG4172 377 prM----TVGQIIAEGlrvhgpGLSAA-ERRARVAEALE----------------EVGlDPAArhryphEFSGGQRQRIA 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 268 IARALVRQPQILLLDEATSALDteseKIVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQ 340
Cdd:COG4172 436 IARALILEPKLLVLDEPTSALD----VSVQaQILDllrdlQREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQGPTE 511
|
....
gi 1708878085 341 QLLA 344
Cdd:COG4172 512 QVFD 515
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
95-361 |
3.40e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 142.81 E-value: 3.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 95 ERVPS-IDSYSE-----EGEKPET---FGGSIMIKDVAFNYpnRPEVK-ILQGLNLKVEKGQTLALVGSSGCGKSTVVQL 164
Cdd:PLN03232 1204 ERVGNyIDLPSEataiiENNRPVSgwpSRGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNA 1281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 165 LERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPMLFDCTIAENIaygDNSRQVPHEEIVNAAKEANIHSFIDSLP 244
Cdd:PLN03232 1282 LFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNI---DPFSEHNDADLWEALERAHIKDVIDRNP 1358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 245 DKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADK 324
Cdd:PLN03232 1359 FGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDK 1438
|
250 260 270
....*....|....*....|....*....|....*..
gi 1708878085 325 IAVVQNGKVVEQGTHQQLLAEKGIYYSLVNVQSGSCN 361
Cdd:PLN03232 1439 ILVLSSGQVLEYDSPQELLSRDTSAFFRMVHSTGPAN 1475
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
119-337 |
6.38e-37 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 132.66 E-value: 6.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLniqwlRAQIGIV 198
Cdd:cd03235 2 VEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 199 SQEPmLFDC----TIAENIAYGDNSRQVPHEEIVNAAKEAnihsfIDSLPDkyntRVGDKG------TQLSGGQKQRIAI 268
Cdd:cd03235 74 PQRR-SIDRdfpiSVRDVVLMGLYGHKGLFRRLSKADKAK-----VDEALE----RVGLSEladrqiGELSGGQQQRVLL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1708878085 269 ARALVRQPQILLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLSTIQN-ADKIAVVqNGKVVEQG 337
Cdd:cd03235 144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL-NRTVVASG 213
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
134-342 |
6.56e-37 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 133.13 E-value: 6.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 134 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNakTLNIQWLRAQIGIVSQEPMLF-DCTIAEN 212
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKD--ITNLPPHKRPVNTVFQNYALFpHLTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 213 IAYGDNSRQVPHEEIVNAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPQILLLDEATSAL 288
Cdd:cd03300 93 IAFGLRLKKLPKAEIKERVAEAldlvQLEGYANRKPS-----------QLSGGQQQRVAIARALVNEPKVLLLDEPLGAL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1708878085 289 DTESEKIVQEALDK--AREGRTCIVIAHRLS-TIQNADKIAVVQNGKVVEQGTHQQL 342
Cdd:cd03300 162 DLKLRKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
128-345 |
1.69e-36 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 134.47 E-value: 1.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 128 NRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN---IQWLRAQIGIVSQEP-- 202
Cdd:COG4608 27 TVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSgreLRPLRRRMQMVFQDPya 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 203 -----MlfdcTIAENIAYG-DNSRQVPHEEivnaaKEANIHSFIDslpdkyntRVGDKGT-------QLSGGQKQRIAIA 269
Cdd:COG4608 107 slnprM----TVGDIIAEPlRIHGLASKAE-----RRERVAELLE--------LVGLRPEhadryphEFSGGQRQRIGIA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 270 RALVRQPQILLLDEATSALDteseKIVQ-------EALdKAREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQ 341
Cdd:COG4608 170 RALALNPKLIVCDEPVSALD----VSIQaqvlnllEDL-QDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDE 244
|
....
gi 1708878085 342 LLAE 345
Cdd:COG4608 245 LYAR 248
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
117-333 |
2.26e-36 |
|
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: 131.11 E-value: 2.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGK--NAKTLNIQWLRAQ 194
Cdd:cd03262 1 IEIKNLHKSFGDF---HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLklTDDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 195 IGIVSQEPMLF-DCTIAENIAYGD-NSRQVPHEEIVNAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAI 268
Cdd:cd03262 78 VGMVFQQFNLFpHLTVLENITLAPiKVKGMSKAEAEERALELlekvGLADKADAYPA-----------QLSGGQQQRVAI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 269 ARALVRQPQILLLDEATSALDTEsekIVQEALDK----AREGRTCIVIAHRLSTIQN-ADKIAVVQNGKV 333
Cdd:cd03262 147 ARALAMNPKVMLFDEPTSALDPE---LVGEVLDVmkdlAEEGMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
117-344 |
3.53e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 132.55 E-value: 3.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 196
Cdd:PRK13650 5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 IVSQEP--MLFDCTIAENIAYGDNSRQVPHEEIVNAAKEA----NIHSFIDSLPdkyntrvgdkgTQLSGGQKQRIAIAR 270
Cdd:PRK13650 85 MVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEAlelvGMQDFKEREP-----------ARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1708878085 271 ALVRQPQILLLDEATSALDTESEKIVQEALDKARE--GRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLA 344
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
115-361 |
4.06e-36 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 139.49 E-value: 4.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 115 GSIMIKDVAFNYpnRPEVK-ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRA 193
Cdd:PLN03130 1236 GSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRK 1313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 194 QIGIVSQEPMLFDCTIAENIaygDNSRQVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALV 273
Cdd:PLN03130 1314 VLGIIPQAPVLFSGTVRFNL---DPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALL 1390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 274 RQPQILLLDEATSALDTESEKIVQEALDKarEGRTC--IVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLAEKGIYYS 351
Cdd:PLN03130 1391 RRSKILVLDEATAAVDVRTDALIQKTIRE--EFKSCtmLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGSAFS 1468
|
250
....*....|.
gi 1708878085 352 LVnVQS-GSCN 361
Cdd:PLN03130 1469 KM-VQStGAAN 1478
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
117-344 |
2.23e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 129.10 E-value: 2.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRPevkiLQgLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIqwlrAQ-- 194
Cdd:COG3840 2 LRLDDLTYRYGDFP----LR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP----AErp 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 195 IGIVSQEPMLFD-CTIAENIAYGD------NSRQvpHEEIVNAAKEANIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIA 267
Cdd:COG3840 73 VSMLFQENNLFPhLTVAQNIGLGLrpglklTAEQ--RAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 268 IARALVRQPQILLLDEATSALD----TESEKIVQEALDkaREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQL 342
Cdd:COG3840 140 LARCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCR--ERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAAL 217
|
..
gi 1708878085 343 LA 344
Cdd:COG3840 218 LD 219
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
134-338 |
3.08e-35 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 132.38 E-value: 3.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 134 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwlRAQIGIVSQEPMLF-DCTIAEN 212
Cdd:PRK09452 29 VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVFQSYALFpHMTVFEN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 213 IAYGDNSRQVPHEEIVNAAKEA----NIHSFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPQILLLDEATSAL 288
Cdd:PRK09452 107 VAFGLRMQKTPAAEITPRVMEAlrmvQLEEFAQRKP-----------HQLSGGQQQRVAIARAVVNKPKVLLLDESLSAL 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1708878085 289 DTESEKIVQEALdKA--RE-GRTCIVIAH-RLSTIQNADKIAVVQNGKVVEQGT 338
Cdd:PRK09452 176 DYKLRKQMQNEL-KAlqRKlGITFVFVTHdQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
119-334 |
3.87e-35 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 127.76 E-value: 3.87e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKDVAFNYPNRPEvkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKtlniQWLRAQ-IGI 197
Cdd:cd03226 2 IENISFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK----AKERRKsIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 198 VSQEP--MLFDCTIAENIAYGDNSRQVPHEEIVNAAKEANIHSFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQ 275
Cdd:cd03226 76 VMQDVdyQLFTDSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSG 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1708878085 276 PQILLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVV 334
Cdd:cd03226 145 KDLLIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
130-337 |
5.64e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 133.61 E-value: 5.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 130 PEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNI-QWLRAQIGIVSQEPMLF-DC 207
Cdd:COG1129 15 GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrDAQAAGIAIIHQELNLVpNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 208 TIAENIAYGDNSRQ---VPHEEIVNAAKEA----NIHsfIDslPDkynTRVGDkgtqLSGGQKQRIAIARALVRQPQILL 280
Cdd:COG1129 95 SVAENIFLGREPRRgglIDWRAMRRRARELlarlGLD--ID--PD---TPVGD----LSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1708878085 281 LDEATSAL-DTESE---KIVQEaLdkAREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQG 337
Cdd:COG1129 164 LDEPTASLtEREVErlfRIIRR-L--KAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTG 222
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
120-346 |
1.47e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 128.27 E-value: 1.47e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 120 KDVAFNYPNRPEVkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWL--RAQIGI 197
Cdd:PRK13639 5 RDLKYSYPDGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLevRKTVGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 198 VSQEP--MLFDCTIAENIAYGDNSRQVPHEEIVNAAKEANihsfidslpdkynTRVGDKGTQ------LSGGQKQRIAIA 269
Cdd:PRK13639 83 VFQNPddQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEAL-------------KAVGMEGFEnkpphhLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1708878085 270 RALVRQPQILLLDEATSALDTE-SEKIVQEALDKAREGRTCIVIAHRLSTIQ-NADKIAVVQNGKVVEQGTHQQLLAEK 346
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMgASQIMKLLYDLNKEGITIIISTHDVDLVPvYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
117-346 |
2.62e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 127.66 E-value: 2.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRPEVkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGK--NAKTLNIQWLRAQ 194
Cdd:PRK13636 6 LKVEELNYNYSDGTHA--LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRES 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 195 IGIVSQEP--MLFDCTIAENIAYGDNSRQVPHEEIVNAAKEANIHSFIDSLPDKyntrvgdKGTQLSGGQKQRIAIARAL 272
Cdd:PRK13636 84 VGMVFQDPdnQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDK-------PTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1708878085 273 VRQPQILLLDEATSALD----TESEKIVQEALDKAreGRTCIVIAHRLSTIQ-NADKIAVVQNGKVVEQGTHQQLLAEK 346
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKEL--GLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
117-338 |
3.85e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 127.22 E-value: 3.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRPEvKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGE---MLFDGKNAKTLNIQWLRA 193
Cdd:PRK13640 6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 194 QIGIVSQEP--MLFDCTIAENIAYGDNSRQVPHEEIV----NAAKEANIHSFIDSLPdkyntrvgdkgTQLSGGQKQRIA 267
Cdd:PRK13640 85 KVGIVFQNPdnQFVGATVGDDVAFGLENRAVPRPEMIkivrDVLADVGMLDYIDSEP-----------ANLSGGQKQRVA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1708878085 268 IARALVRQPQILLLDEATSALDTESE----KIVQEALDKarEGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGT 338
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKeqilKLIRKLKKK--NNLTVISITHDIDEANMADQVLVLDDGKLLAQGS 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
117-337 |
4.41e-34 |
|
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) proteins function from bacteria to human, mediating the translocation of substances into and out of cells or organelles. ABC transporters contain two transmembrane-spanning domains (TMDs) or subunits and two nucleotide binding domains (NBDs) or subunits that couple transport to the hydrolysis of ATP. In the maltose transport system, the periplasmic maltose binding protein (MBP) stimulates the ATPase activity of the membrane-associated transporter, which consists of two transmembrane subunits, MalF and MalG, and two copies of the ATP binding subunit, MalK, and becomes tightly bound to the transporter in the catalytic transition state, ensuring that maltose is passed to the transporter as ATP is hydrolyzed.
Pssm-ID: 213268 [Multi-domain] Cd Length: 213 Bit Score: 125.06 E-value: 4.41e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNrpeVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKN-----AKTLNIqwl 191
Cdd:cd03301 1 VELENVTKRFGN---VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDvtdlpPKDRDI--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 192 raqiGIVSQEPMLF-DCTIAENIAYGDNSRQVPHEEIVNAAKEANIHSFIDSLPDKyntrvgdKGTQLSGGQKQRIAIAR 270
Cdd:cd03301 75 ----AMVFQNYALYpHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDR-------KPKQLSGGQRQRVALGR 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 271 ALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAH-RLSTIQNADKIAVVQNGKVVEQG 337
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
117-342 |
6.24e-34 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 125.66 E-value: 6.24e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYD-----PLDGEMLFDGKN---AKTLNI 188
Cdd:PRK14239 6 LQVSDLSVYYNKK---KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnpevTITGSIVYNGHNiysPRTDTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 189 QwLRAQIGIVSQEPMLFDCTIAENIAYGDNSRQVPHEEIVNAAKEANIHSfiDSLPDKYNTRVGDKGTQLSGGQKQRIAI 268
Cdd:PRK14239 83 D-LRKEIGMVFQQPNPFPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKG--ASIWDEVKDRLHDSALGLSGGQQQRVCI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1708878085 269 ARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRL---STIqnADKIAVVQNGKVVEQGTHQQL 342
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMqqaSRI--SDRTGFFLDGDLIEYNDTKQM 234
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
131-345 |
1.21e-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: 124.08 E-value: 1.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 131 EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNiQWLRAQIGI--VSQEPMLF-DC 207
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLP-PHERARAGIgyVPEGRRIFpEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 208 TIAENIAYGDNSRQvpheeivNAAKEANIHSFIDSLPDKYnTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSA 287
Cdd:cd03224 91 TVEENLLLGAYARR-------RAKRKARLERVYELFPRLK-ERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1708878085 288 LdteSEKIVQE---ALDK-AREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQLLAE 345
Cdd:cd03224 163 L---APKIVEEifeAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLAD 222
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
116-345 |
1.62e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 125.55 E-value: 1.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 116 SIMIKDVAFNY-PNRP-EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKN--AKTLNIQWL 191
Cdd:PRK13637 2 SIKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDitDKKVKLSDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 192 RAQIGIVSQEP--MLFDCTIAENIAYGDNSRQVPHEEIVNAAKEAnihsfIDSLPDKYNTrVGDKGT-QLSGGQKQRIAI 268
Cdd:PRK13637 82 RKKVGLVFQYPeyQLFEETIEKDIAFGPINLGLSEEEIENRVKRA-----MNIVGLDYED-YKDKSPfELSGGQKRRVAI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 269 ARALVRQPQILLLDEATSALDTeseKIVQEALDKARE-----GRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQL 342
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDP---KGRDEILNKIKElhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGTPREV 232
|
...
gi 1708878085 343 LAE 345
Cdd:PRK13637 233 FKE 235
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
117-348 |
2.97e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 124.48 E-value: 2.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYpNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 196
Cdd:PRK13648 8 IVFKNVSFQY-QSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 IVSQEP--MLFDCTIAENIAYGDNSRQVPHEE---IVNAA-KEANIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIAR 270
Cdd:PRK13648 87 IVFQNPdnQFVGSIVKYDVAFGLENHAVPYDEmhrRVSEAlKQVDMLERADYEPN-----------ALSGGQKQRVAIAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 271 ALVRQPQILLLDEATSALDTESEKIVQEALDKAREGR--TCIVIAHRLSTIQNADKIAVVQNGKVVEQGT------HQQL 342
Cdd:PRK13648 156 VLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTpteifdHAEE 235
|
....*.
gi 1708878085 343 LAEKGI 348
Cdd:PRK13648 236 LTRIGL 241
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
119-344 |
4.40e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 124.43 E-value: 4.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKDVAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIV 198
Cdd:PRK13642 7 VENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 199 SQEP--MLFDCTIAENIAYGDNSRQVPHEEIVNAAKEANIH-SFIDslpdkYNTRvgdKGTQLSGGQKQRIAIARALVRQ 275
Cdd:PRK13642 87 FQNPdnQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAvNMLD-----FKTR---EPARLSGGQKQRVAVAGIIALR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1708878085 276 PQILLLDEATSALD----TESEKIVQEALDKARegRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLA 344
Cdd:PRK13642 159 PEIIILDESTSMLDptgrQEIMRVIHEIKEKYQ--LTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFA 229
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
133-337 |
5.16e-33 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 122.40 E-value: 5.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 133 KILQGLNLKVE---KGQTLALVGSSGCGKSTVVQLLERFYDP------LDGEMLFDGKnaKTLNIQWLRAQIGIVSQEPM 203
Cdd:cd03297 8 KRLPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPdggtivLNGTVLFDSR--KKINLPPQQRKIGLVFQQYA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 204 LF-DCTIAENIAYG-----DNSRQVPHEEIVNAAKeanihsfIDSLPDKYNTrvgdkgtQLSGGQKQRIAIARALVRQPQ 277
Cdd:cd03297 86 LFpHLNVRENLAFGlkrkrNREDRISVDELLDLLG-------LDHLLNRYPA-------QLSGGEKQRVALARALAAQPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1708878085 278 ILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQG 337
Cdd:cd03297 152 LLLLDEPFSALDRALRLQLLPELKQikKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
117-333 |
5.41e-33 |
|
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: 122.13 E-value: 5.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNrpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN---IQWLRA 193
Cdd:cd03292 1 IEFINVTKTYPN--GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 194 QIGIVSQE-PMLFDCTIAENIAYGDNSRQVPHEEIVNAAKEA----NIHSFIDSLPdkyntrvgdkgTQLSGGQKQRIAI 268
Cdd:cd03292 79 KIGVVFQDfRLLPDRNVYENVAFALEVTGVPPREIRKRVPAAlelvGLSHKHRALP-----------AELSGGEQQRVAI 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1708878085 269 ARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADK--IAVVQNGKV 333
Cdd:cd03292 148 ARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRhrVIALERGKL 214
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
117-353 |
5.43e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 124.08 E-value: 5.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNrpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 196
Cdd:PRK13647 5 IEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 IVSQEP--MLFDCTIAENIAYGDNSRQVPHEEIVNAAKEA----NIHSFIDSLPdkyntrvgdkgTQLSGGQKQRIAIAR 270
Cdd:PRK13647 83 LVFQDPddQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEAlkavRMWDFRDKPP-----------YHLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 271 ALVRQPQILLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLS-TIQNADKIAVVQNGKVVEQG-----THQQLL 343
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGdksllTDEDIV 231
|
250
....*....|
gi 1708878085 344 AEKGIYYSLV 353
Cdd:PRK13647 232 EQAGLRLPLV 241
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
119-327 |
5.62e-33 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 121.82 E-value: 5.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWlRAQIGIV 198
Cdd:COG4133 5 AENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 199 SQEPMLF-DCTIAENIA-----YGdnsRQVPHEEIVNAAKEANIHSFIDslpdkynTRVGdkgtQLSGGQKQRIAIARAL 272
Cdd:COG4133 81 GHADGLKpELTVRENLRfwaalYG---LRADREAIDEALEAVGLAGLAD-------LPVR----QLSAGQKRRVALARLL 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1708878085 273 VRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIA-HRLSTIQNADKIAV 327
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTtHQPLELAAARVLDL 202
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
114-325 |
1.11e-32 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 128.00 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 114 GGSIMIKDVAFNYPN-RPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL-----------ERfydPLDGEMLFdgk 181
Cdd:COG4178 360 DGALALEDLTLRTPDgRP---LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIaglwpygsgriAR---PAGARVLF--- 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 182 naktlniqwlraqigiVSQEPMLFDCTIAENIAYGDNSRQVPHEEIVNAAKEANIHSFIDSLpdkynTRVGDKGTQLSGG 261
Cdd:COG4178 431 ----------------LPQRPYLPLGTLREALLYPATAEAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLG 489
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1708878085 262 QKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKI 325
Cdd:COG4178 490 EQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRV 553
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
116-342 |
1.32e-32 |
|
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: 122.06 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 116 SIMIKDVAFNYPNRPEvkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwlRAQI 195
Cdd:cd03296 2 SIEVRNVSKRFGDFVA---LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 196 GIVSQEPMLF-DCTIAENIAYG----DNSRQVPHEEIvnAAKEANIHSFI--DSLPDKYNTrvgdkgtQLSGGQKQRIAI 268
Cdd:cd03296 77 GFVFQHYALFrHMTVFDNVAFGlrvkPRSERPPEAEI--RAKVHELLKLVqlDWLADRYPA-------QLSGGQRQRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1708878085 269 ARALVRQPQILLLDEATSALDTESEKIVQEALDKARE--GRTCIVIAHRLS-TIQNADKIAVVQNGKVVEQGTHQQL 342
Cdd:cd03296 148 ARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDelHVTTVFVTHDQEeALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
135-345 |
2.51e-32 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 121.81 E-value: 2.51e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 135 LQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPL-----DGEMLFDGKN--AKTLNIQWLRAQIGIVSQEPMLFDC 207
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLIpgfrvEGKVTFHGKNlyAPDVDPVEVRRRIGMVFQKPNPFPK 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 208 TIAENIAYGD--NSRQVPHEEIVNAA-KEAnihSFIDSLPDKYNtrvgDKGTQLSGGQKQRIAIARALVRQPQILLLDEA 284
Cdd:PRK14243 106 SIYDNIAYGAriNGYKGDMDELVERSlRQA---ALWDEVKDKLK----QSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1708878085 285 TSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLAE 345
Cdd:PRK14243 179 CSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEGGGRYGYLVE 239
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
119-344 |
2.67e-32 |
|
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: 126.72 E-value: 2.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKD--VAFNYPNRpEVKILQGLNLKVEKGQTLALVGSSGCGKS----TVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLR 192
Cdd:COG4172 9 VEDlsVAFGQGGG-TVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 193 A----QIGIVSQEPM-----LFdcTIAENIA-----YGDNSRQVPHEEIVNAAKEANIhsfidslPDKyNTRVGDKGTQL 258
Cdd:COG4172 88 RirgnRIAMIFQEPMtslnpLH--TIGKQIAevlrlHRGLSGAAARARALELLERVGI-------PDP-ERRLDAYPHQL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 259 SGGQKQRIAIARALVRQPQILLLDEATSALDTesekIVQ-EALD-----KAREGRTCIVIAHRLSTIQN-ADKIAVVQNG 331
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALDV----TVQaQILDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQG 233
|
250
....*....|...
gi 1708878085 332 KVVEQGTHQQLLA 344
Cdd:COG4172 234 EIVEQGPTAELFA 246
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
116-291 |
2.14e-31 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 117.97 E-value: 2.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 116 SIMIKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDP---LDGEMLFDGKNAKTLNIQwlR 192
Cdd:COG4136 1 MLSLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--Q 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 193 AQIGIVSQEPMLFD-CTIAENIAYG---DNSRQVPHEEIVNAAKEANIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAI 268
Cdd:COG4136 76 RRIGILFQDDLLFPhLSVGENLAFAlppTIGRAQRRARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVAL 144
|
170 180
....*....|....*....|...
gi 1708878085 269 ARALVRQPQILLLDEATSALDTE 291
Cdd:COG4136 145 LRALLAEPRALLLDEPFSKLDAA 167
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
117-342 |
3.78e-31 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 117.61 E-value: 3.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRPeVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTlNIQWLRAQIG 196
Cdd:cd03263 1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 IVSQEPMLFD-CTIAENIAYGDNSRQVPHEEIvnaakEANIHSFID--SLPDKYNTRVGDkgtqLSGGQKQRIAIARALV 273
Cdd:cd03263 79 YCPQFDALFDeLTVREHLRFYARLKGLPKSEI-----KEEVELLLRvlGLTDKANKRART----LSGGMKRKLSLAIALI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 274 RQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQL 342
Cdd:cd03263 150 GGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
130-334 |
4.61e-31 |
|
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: 115.60 E-value: 4.61e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 130 PEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN-IQWLRAQIGIVSQepmlfdct 208
Cdd:cd03216 11 GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAMVYQ-------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 209 iaeniaygdnsrqvpheeivnaakeanihsfidslpdkyntrvgdkgtqLSGGQKQRIAIARALVRQPQILLLDEATSAL 288
Cdd:cd03216 83 -------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAAL 113
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1708878085 289 -DTESEKIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVV 334
Cdd:cd03216 114 tPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
117-350 |
5.92e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 118.55 E-value: 5.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNrpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN-IQWLRAQI 195
Cdd:PRK13644 2 IRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 196 GIVSQEP--MLFDCTIAENIAYGDNSRQVPHEEIVNAAKEAnihsFIDSLPDKYNTRvgdKGTQLSGGQKQRIAIARALV 273
Cdd:PRK13644 80 GIVFQNPetQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRA----LAEIGLEKYRHR---SPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1708878085 274 RQPQILLLDEATSALDTESEKIVQEALDKA-REGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLAEKGIYY 350
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVSLQT 230
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
131-343 |
9.92e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 117.12 E-value: 9.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 131 EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGK--NAKTLNIQWLRAQIGIVSQEPMLF-DC 207
Cdd:PRK09493 13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLkvNDPKVDERLIRQEAGMVFQQFYLFpHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 208 TIAENIAYGdnSRQVpheeivNAAKEANIHSFIDSLPDKYN--TRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEAT 285
Cdd:PRK09493 93 TALENVMFG--PLRV------RGASKEEAEKQARELLAKVGlaERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1708878085 286 SALDTEsekIVQEAL----DKAREGRTCIVIAHRlstIQNADKIA----VVQNGKVVEQGTHQQLL 343
Cdd:PRK09493 165 SALDPE---LRHEVLkvmqDLAEEGMTMVIVTHE---IGFAEKVAsrliFIDKGRIAEDGDPQVLI 224
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
115-349 |
1.65e-30 |
|
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: 117.26 E-value: 1.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 115 GSIMIKDVAFNYPNRPEVkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDpLDGEMLFDGKNAKTLNIQWLRAQ 194
Cdd:cd03289 1 GQMTVKDLTAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 195 IGIVSQEPMLFDCTIAENIaygDNSRQVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVR 274
Cdd:cd03289 79 FGVIPQKVFIFSGTFRKNL---DPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1708878085 275 QPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLAEKGIY 349
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHF 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
134-345 |
3.07e-30 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 116.00 E-value: 3.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 134 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDG-----EMLFDGknAKTLN-----IQWLRAQIGIVSQEPM 203
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIDT--ARSLSqqkglIRQLRQHVGFVFQNFN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 204 LFDC-TIAENIAYGDN-SRQVPHEEIVNAAKEANIHSFIDSLPDKYNTRvgdkgtqLSGGQKQRIAIARALVRQPQILLL 281
Cdd:PRK11264 96 LFPHrTVLENIIEGPViVKGEPKEEATARARELLAKVGLAGKETSYPRR-------LSGGQQQRVAIARALAMRPEVILF 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1708878085 282 DEATSALDTEsekIVQEALDK----AREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQLLAE 345
Cdd:PRK11264 169 DEPTSALDPE---LVGEVLNTirqlAQEKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
115-345 |
6.01e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 115.96 E-value: 6.01e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 115 GSIMI--KDVAFNYPNRPEVK---ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQ 189
Cdd:PRK13633 1 MNEMIkcKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 190 W-LRAQIGIVSQEP--MLFDCTIAENIAYGDNSRQVPHEEIV----NAAKEANIHSFIDSLPDkyntrvgdkgtQLSGGQ 262
Cdd:PRK13633 81 WdIRNKAGMVFQNPdnQIVATIVEEDVAFGPENLGIPPEEIRervdESLKKVGMYEYRRHAPH-----------LLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 263 KQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQ 340
Cdd:PRK13633 150 KQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPK 229
|
....*
gi 1708878085 341 QLLAE 345
Cdd:PRK13633 230 EIFKE 234
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
117-346 |
6.33e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 115.89 E-value: 6.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNY-PNRP-EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDG------EMLFDGKNAKtlNI 188
Cdd:PRK13634 3 ITFQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGtvtigeRVITAGKKNK--KL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 189 QWLRAQIGIVSQ--EPMLFDCTIAENIAYGDNSRQVPHEEIVNAAKEAnihsfID--SLPDKYNTRvgdKGTQLSGGQKQ 264
Cdd:PRK13634 81 KPLRKKVGIVFQfpEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREM-----IElvGLPEELLAR---SPFELSGGQMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 265 RIAIARALVRQPQILLLDEATSALDTESEKIVQE---ALDKaREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQ 340
Cdd:PRK13634 153 RVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEmfyKLHK-EKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPR 231
|
....*.
gi 1708878085 341 QLLAEK 346
Cdd:PRK13634 232 EIFADP 237
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
117-337 |
8.94e-30 |
|
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: 113.44 E-value: 8.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRpevKILQGLNLKVEKGQTlALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTlNIQWLRAQIG 196
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 IVSQEPMLFD-CTIAENIAY-----GDNSRQVpHEEIVNAAKEANihsfidsLPDKYNTRVGdkgtQLSGGQKQRIAIAR 270
Cdd:cd03264 76 YLPQEFGVYPnFTVREFLDYiawlkGIPSKEV-KARVDEVLELVN-------LGDRAKKKIG----SLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1708878085 271 ALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQG 337
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
116-343 |
1.12e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 114.75 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 116 SIMIKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDpLDGEMLFDGK--------NAKTLN 187
Cdd:PRK14258 7 AIKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGRveffnqniYERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 188 IQWLRAQIGIVSQEPMLFDCTIAENIAYGDN----SRQVPHEEIVNAAKEANihsfidSLPDKYNTRVGDKGTQLSGGQK 263
Cdd:PRK14258 83 LNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKivgwRPKLEIDDIVESALKDA------DLWDEIKHKIHKSALDLSGGQQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 264 QRIAIARALVRQPQILLLDEATSALDTESEKIVQEALD--KAREGRTCIVIAHRLSTIQN-ADKIAVVQN-----GKVVE 335
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQVSRlSDFTAFFKGnenriGQLVE 236
|
....*...
gi 1708878085 336 QGTHQQLL 343
Cdd:PRK14258 237 FGLTKKIF 244
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
134-342 |
1.23e-29 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 116.74 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 134 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwlRAQIGIVSQEPMLF-DCTIAEN 212
Cdd:PRK11432 21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRDICMVFQSYALFpHMSLGEN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 213 IAYGDNSRQVPHEEIVNAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPQILLLDEATSAL 288
Cdd:PRK11432 99 VGYGLKMLGVPKEERKQRVKEAlelvDLAGFEDRYVD-----------QISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 289 DTESEKIVQEaldKARE-----GRTCIVIAHRLS-TIQNADKIAVVQNGKVVEQGTHQQL 342
Cdd:PRK11432 168 DANLRRSMRE---KIRElqqqfNITSLYVTHDQSeAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
130-334 |
1.31e-29 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 118.98 E-value: 1.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 130 PEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKnakTLNI----QWLRAQIGIVSQEPMLF 205
Cdd:COG3845 16 GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGK---PVRIrsprDAIALGIGMVHQHFMLV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 206 DC-TIAENIAYGDNSRQVPHEEIVNAAKEanihsfIDSLPDKY------NTRVGDkgtqLSGGQKQRIAIARALVRQPQI 278
Cdd:COG3845 93 PNlTVAENIVLGLEPTKGGRLDRKAARAR------IRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1708878085 279 LLLDEATSALdTESEkiVQE---ALDK-AREGRTCIVIAHRLSTI-QNADKIAVVQNGKVV 334
Cdd:COG3845 163 LILDEPTAVL-TPQE--ADElfeILRRlAAEGKSIIFITHKLREVmAIADRVTVLRRGKVV 220
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
114-349 |
1.52e-29 |
|
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: 120.40 E-value: 1.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 114 GGSIMIKDVAFNYPNRPEvKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPlDGEMLFDGKNAKTLNIQWLRA 193
Cdd:TIGR01271 1215 GGQMDVQGLTAKYTEAGR-AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVSWNSVTLQTWRK 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 194 QIGIVSQEPMLFDCTIAENIaygDNSRQVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALV 273
Cdd:TIGR01271 1293 AFGVIPQKVFIFSGTFRKNL---DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSIL 1369
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1708878085 274 RQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLAEKGIY 349
Cdd:TIGR01271 1370 SKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLF 1445
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
116-340 |
4.24e-29 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 112.80 E-value: 4.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 116 SIMIKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEM-----LFD-GKNAKTLNIQ 189
Cdd:PRK11124 2 SIQLNGINCFYGAH---QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnHFDfSKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 190 WLRAQIGIVSQE----PMLfdcTIAEN-IAYGDNSRQVPHEEIVNAAKEA----NIHSFIDSLPdkyntrvgdkgTQLSG 260
Cdd:PRK11124 79 ELRRNVGMVFQQynlwPHL---TVQQNlIEAPCRVLGLSKDQALARAEKLlerlRLKPYADRFP-----------LHLSG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 261 GQKQRIAIARALVRQPQILLLDEATSALDTE-SEKIVQEALDKAREGRTCIVIAHRLSTiqnADKIA--VV--QNGKVVE 335
Cdd:PRK11124 145 GQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEV---ARKTAsrVVymENGHIVE 221
|
....*
gi 1708878085 336 QGTHQ 340
Cdd:PRK11124 222 QGDAS 226
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
138-362 |
4.66e-29 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 115.70 E-value: 4.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 138 LNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKtlNIQWLRAQIGIVSQEPMLF-DCTIAENIAYG 216
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS--HVPPYQRPINMMFQSYALFpHMTVEQNIAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 217 DNSRQVPHEEIVNAAKE--ANIHSfidslpDKYNTRvgdKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTE-SE 293
Cdd:PRK11607 116 LKQDKLPKAEIASRVNEmlGLVHM------QEFAKR---KPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlRD 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1708878085 294 KIVQEALD-KAREGRTCIVIAH-RLSTIQNADKIAVVQNGKVVEQGTHQQLLAEKGIYYSLVNVqsGSCNM 362
Cdd:PRK11607 187 RMQLEVVDiLERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFI--GSVNV 255
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
130-331 |
1.02e-28 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 110.88 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 130 PEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQ----IGIVSQEPMLF 205
Cdd:cd03290 12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPWLL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 206 DCTIAENIAYGDNSRQVPHEEIVNAAkeaNIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEAT 285
Cdd:cd03290 92 NATVEENITFGSPFNKQRYKAVTDAC---SLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1708878085 286 SALDTE-SEKIVQEALDK--AREGRTCIVIAHRLSTIQNADKIAVVQNG 331
Cdd:cd03290 169 SALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
114-349 |
1.30e-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: 117.35 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 114 GGSIMIKDVAFNYPnRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGknaktlniqwlra 193
Cdd:TIGR00957 634 GNSITVHNATFTWA-RDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG------------- 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 194 QIGIVSQEPMLFDCTIAENIAYGDNSRQVPHEEIVNAAKeanIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALV 273
Cdd:TIGR00957 700 SVAYVPQQAWIQNDSLRENILFGKALNEKYYQQVLEACA---LLPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVY 776
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1708878085 274 RQPQILLLDEATSALDTESEKIVQEAL---DKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLAEKGIY 349
Cdd:TIGR00957 777 SNADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAF 855
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
130-332 |
1.54e-28 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 115.80 E-value: 1.54e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 130 PEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYdP---LDGEMLFDGKNAKTLNIQWL-RAQIGIVSQEPMLF 205
Cdd:PRK13549 16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PhgtYEGEIIFEGEELQASNIRDTeRAGIAIIHQELALV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 206 -DCTIAENIAYGdnSRQVPH-----EEIVNAAKE--ANIHSFIDSlpdkyNTRVGDkgtqLSGGQKQRIAIARALVRQPQ 277
Cdd:PRK13549 95 kELSVLENIFLG--NEITPGgimdyDAMYLRAQKllAQLKLDINP-----ATPVGN----LGLGQQQLVEIAKALNKQAR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1708878085 278 ILLLDEATSALdTESE-----KIVQealDKAREGRTCIVIAHRLSTIQN-ADKIAVVQNGK 332
Cdd:PRK13549 164 LLILDEPTASL-TESEtavllDIIR---DLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
132-338 |
1.58e-28 |
|
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: 110.99 E-value: 1.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 132 VKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwLRAQIGIVS--QEPMLF-DCT 208
Cdd:cd03219 13 LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPH-EIARLGIGRtfQIPRLFpELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 209 IAENI----------AYGDNSRQVPHEEIVNAAKEAnihsfIDS--LPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQP 276
Cdd:cd03219 92 VLENVmvaaqartgsGLLLARARREEREARERAEEL-----LERvgLADLADRPAGE----LSYGQQRRLEIARALATDP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1708878085 277 QILLLDEATSAL-DTESEKIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGT 338
Cdd:cd03219 163 KLLLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
117-343 |
1.79e-28 |
|
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: 110.94 E-value: 1.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGE--MLFDGKNAKTlNIQWLRAQ 194
Cdd:COG1119 4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdvRLFGERRGGE-DVWELRKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 195 IGIVSQEpmlfdctIAENIAYGDNSRQV--------------PHEEIVNAAKEAnIHSF-IDSLPDK-YNTrvgdkgtqL 258
Cdd:COG1119 80 IGLVSPA-------LQLRFPRDETVLDVvlsgffdsiglyrePTDEQRERAREL-LELLgLAHLADRpFGT--------L 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 259 SGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDK-AREGRTCIV-IAHRLSTIQNA-DKIAVVQNGKVVE 335
Cdd:COG1119 144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVEEIPPGiTHVLLLKDGRVVA 223
|
....*...
gi 1708878085 336 QGTHQQLL 343
Cdd:COG1119 224 AGPKEEVL 231
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
117-329 |
2.00e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 110.19 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 196
Cdd:PRK10247 8 LQLQNVGYLAGDA---KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 IVSQEPMLFDCTIAENIAYgdnSRQVPHEEIVNAAKEANIHSFidSLPDKyntrVGDKG-TQLSGGQKQRIAIARALVRQ 275
Cdd:PRK10247 85 YCAQTPTLFGDTVYDNLIF---PWQIRNQQPDPAIFLDDLERF--ALPDT----ILTKNiAELSGGEKQRISLIRNLQFM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1708878085 276 PQILLLDEATSALDTESEKIVQEALDK-AREGRTCIV-IAHRLSTIQNADKIAVVQ 329
Cdd:PRK10247 156 PKVLLLDEITSALDESNKHNVNEIIHRyVREQNIAVLwVTHDKDEINHADKVITLQ 211
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
149-344 |
3.52e-28 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 112.89 E-value: 3.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 149 ALVGSSGCGKSTVVQL---LERfydP------LDGEMLFDGKNAktlniQWL---RAQIGIVSQEPMLFD-CTIAENIAY 215
Cdd:COG4148 29 ALFGPSGSGKTTLLRAiagLER---PdsgrirLGGEVLQDSARG-----IFLpphRRRIGYVFQEARLFPhLSVRGNLLY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 216 G-----DNSRQVPHEEIVNAAkeaNIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPQILLLDEATSALDT 290
Cdd:COG4148 101 GrkrapRAERRISFDEVVELL---GIGHLLDRRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1708878085 291 ES-EKIVQ--EALdkAREGRTCIV-IAH------RLstiqnADKIAVVQNGKVVEQGTHQQLLA 344
Cdd:COG4148 167 ARkAEILPylERL--RDELDIPILyVSHsldevaRL-----ADHVVLLEQGRVVASGPLAEVLS 223
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
117-337 |
4.46e-28 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 108.84 E-value: 4.46e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWlrAQIG 196
Cdd:cd03268 1 LKTNDLTKTYGKKR---VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL--RRIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 IVSQEPMLFD-CTIAENIAYGDNSRQVPHEEIVNAAKEANIHsfidslpdkynTRVGDKGTQLSGGQKQRIAIARALVRQ 275
Cdd:cd03268 76 ALIEAPGFYPnLTARENLRLLARLLGIRKKRIDEVLDVVGLK-----------DSAKKKVKGFSLGMKQRLGIALALLGN 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1708878085 276 PQILLLDEATSALDTESEKIVQEAL-DKAREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQG 337
Cdd:cd03268 145 PDLLILDEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
131-337 |
5.51e-28 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 108.91 E-value: 5.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 131 EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwlraQIGIVSQEPMLF-DCTI 209
Cdd:cd03269 12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARN----RIGYLPEERGLYpKMKV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 210 AENIAYGDNSRQVPHEEIvnaakEANIHSFIDS--LPDKYNTRVgdkgTQLSGGQKQRIAIARALVRQPQILLLDEATSA 287
Cdd:cd03269 88 IDQLVYLAQLKGLKKEEA-----RRRIDEWLERleLSEYANKRV----EELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1708878085 288 LDTESEKIVQEAL-DKAREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQG 337
Cdd:cd03269 159 LDPVNVELLKDVIrELARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
116-339 |
5.81e-28 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 109.72 E-value: 5.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 116 SIMIKDVAFNYPNrpeVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEML-----FD---GKNAKTln 187
Cdd:COG4161 2 SIQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNiaghqFDfsqKPSEKA-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 188 IQWLRAQIGIVSQE----PMLfdcTIAENIAYG-----DNSRQVPHEEIVNAAKEANIHSFIDSLPdkyntrvgdkgTQL 258
Cdd:COG4161 77 IRLLRQKVGMVFQQynlwPHL---TVMENLIEApckvlGLSKEQAREKAMKLLARLRLTDKADRFP-----------LHL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 259 SGGQKQRIAIARALVRQPQILLLDEATSALDTE-SEKIVQEALDKAREGRTCIVIAHRLSTiqnADKIA--VV--QNGKV 333
Cdd:COG4161 143 SGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEF---ARKVAsqVVymEKGRI 219
|
....*.
gi 1708878085 334 VEQGTH 339
Cdd:COG4161 220 IEQGDA 225
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
139-343 |
6.13e-28 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 112.82 E-value: 6.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 139 NLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLR----AQIGIVSQE-PMLFDCTIAENI 213
Cdd:PRK10070 48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSfALMPHMTVLDNT 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 214 AYGDNSRQVPHEE----IVNAAKEANIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPQILLLDEATSALD 289
Cdd:PRK10070 128 AFGMELAGINAEErrekALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAFSALD 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1708878085 290 TESEKIVQEALDK--AREGRTCIVIAHRL-STIQNADKIAVVQNGKVVEQGTHQQLL 343
Cdd:PRK10070 197 PLIRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
134-343 |
6.60e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 109.75 E-value: 6.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 134 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERF---YDP---LDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPMLF-D 206
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSkikVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFpH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 207 CTIAENIAYGDNSRQVPHEEIVNAAKEANIHSFidSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATS 286
Cdd:PRK14246 105 LSIYDNIAYPLKSHGIKEKREIKKIVEECLRKV--GLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1708878085 287 ALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQLL 343
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGSSNEIF 240
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
132-344 |
6.85e-28 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 111.21 E-value: 6.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 132 VKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN---IQWLRAQIGIVSQEPmlfdct 208
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQNP------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 209 iaeniaYGD-NSRQ----------VPHEEIVNAAKEANIHSFIdslpdkynTRVGDKGTQ-------LSGGQKQRIAIAR 270
Cdd:PRK11308 102 ------YGSlNPRKkvgqileeplLINTSLSAAERREKALAMM--------AKVGLRPEHydryphmFSGGQRQRIAIAR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1708878085 271 ALVRQPQILLLDEATSALDTESEKIVQEAL-DKAREGRTCIV-IAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQLLA 344
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDVSVQAQVLNLMmDLQQELGLSYVfISHDLSVVEHiADEVMVMYLGRCVEKGTKEQIFN 244
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
133-337 |
7.19e-28 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 108.02 E-value: 7.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 133 KILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL--ERFYDPLDGEMLFDGKNaktLNIQWLRAQIGIVSQEPMLFDC-TI 209
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRP---LDKRSFRKIIGYVPQDDILHPTlTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 210 AENIAYgdnsrqvpheeivnAAKeanihsfidsLpdkyntrvgdKGtqLSGGQKQRIAIARALVRQPQILLLDEATSALD 289
Cdd:cd03213 100 RETLMF--------------AAK----------L----------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1708878085 290 TESEKIVQEALDK-AREGRTCIVIAHRLST--IQNADKIAVVQNGKVVEQG 337
Cdd:cd03213 144 SSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
139-344 |
8.47e-28 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 108.90 E-value: 8.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 139 NLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwlRAQIGIVSQEPMLFD-CTIAENIAYGD 217
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS--RRPVSMLFQENNLFShLTVAQNIGLGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 218 ------NSRQvpHEEIVNAAKEANIHSFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPQILLLDEATSALD-- 289
Cdd:PRK10771 97 npglklNAAQ--REKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVALARCLVREQPILLLDEPFSALDpa 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1708878085 290 --TESEKIVQEALDkaREGRTCIVIAHRLstiQNADKIA----VVQNGKVVEQGTHQQLLA 344
Cdd:PRK10771 164 lrQEMLTLVSQVCQ--ERQLTLLMVSHSL---EDAARIAprslVVADGRIAWDGPTDELLS 219
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
119-344 |
8.74e-28 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 108.92 E-value: 8.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKDVAFNYPnrpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNaktlnIQWLRAQ---- 194
Cdd:COG0410 6 VENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGED-----ITGLPPHriar 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 195 --IGIVSQEPMLF-DCTIAENI---AYGDNSRQVPHEEIvnaakeANIHSFIDSLPDKYNTRvgdkGTQLSGGQKQRIAI 268
Cdd:COG0410 78 lgIGYVPEGRRIFpSLTVEENLllgAYARRDRAEVRADL------ERVYELFPRLKERRRQR----AGTLSGGEQQMLAI 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 269 ARALVRQPQILLLDEATSALdteSEKIVQEALDK----AREGRTCIVI---AHRLSTIqnADKIAVVQNGKVVEQGTHQQ 341
Cdd:COG0410 148 GRALMSRPKLLLLDEPSLGL---APLIVEEIFEIirrlNREGVTILLVeqnARFALEI--ADRAYVLERGRIVLEGTAAE 222
|
...
gi 1708878085 342 LLA 344
Cdd:COG0410 223 LLA 225
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
134-353 |
1.22e-27 |
|
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: 114.62 E-value: 1.22e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 134 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKnaktlniqwlraqIGIVSQEPMLFDCTIAENI 213
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIKDNI 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 214 AYGDNSRQVPHEEIVNAAKeanIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESE 293
Cdd:TIGR01271 508 IFGLSYDEYRYTSVIKACQ---LEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1708878085 294 K-IVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLAEKGIYYSLV 353
Cdd:TIGR01271 585 KeIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLL 645
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
138-346 |
1.40e-27 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 110.97 E-value: 1.40e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 138 LNLKVEKGQTLALVGSSGCGKSTVVQL---LERFYDP---LDGEMLFDGKNAKTLNIQwlRAQIGIVSQEPMLF-DCTIA 210
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLiagLTRPDEGeivLNGRTLFDSRKGIFLPPE--KRRIGYVFQEARLFpHLSVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 211 ENIAYG-----DNSRQVPHEEIVNAAkeaNIHSFIDSLPDKyntrvgdkgtqLSGGQKQRIAIARALVRQPQILLLDEAT 285
Cdd:TIGR02142 94 GNLRYGmkrarPSERRISFERVIELL---GIGHLLGRLPGR-----------LSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1708878085 286 SALDTESEKIVQEALDKARE--GRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQLLAEK 346
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAefGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASP 223
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
116-345 |
1.69e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 109.45 E-value: 1.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 116 SIMIKDVAFNY-PNRP-EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGK----NAKTLNIQ 189
Cdd:PRK13649 2 GINLQNVSYTYqAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTlitsTSKNKDIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 190 WLRAQIGIVSQ--EPMLFDCTIAENIAYGDNSRQVPHEEIVNAAKEA-NIHSFIDSLPDKyntrvgdKGTQLSGGQKQRI 266
Cdd:PRK13649 82 QIRKKVGLVFQfpESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKlALVGISESLFEK-------NPFELSGGQMRRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 267 AIARALVRQPQILLLDEATSALDTESEKIVQEALDKARE-GRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQLLA 344
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSGKPKDIFQ 234
|
.
gi 1708878085 345 E 345
Cdd:PRK13649 235 D 235
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
138-337 |
1.74e-27 |
|
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: 107.58 E-value: 1.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 138 LNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwlRAQIGIVSQEPMLF-DCTIAENIAYG 216
Cdd:cd03298 17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFaHLTVEQNVGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 217 DNSR----QVPHEEIVNAAKEANIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPQILLLDEATSALD-TE 291
Cdd:cd03298 95 LSPGlkltAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALARVLVRDKPVLLLDEPFAALDpAL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1708878085 292 SEKIVQEALDKARE-GRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQG 337
Cdd:cd03298 164 RAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
134-346 |
1.98e-27 |
|
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: 108.74 E-value: 1.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 134 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRA---QIGIVSQepmlfDCTIA 210
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrDVQLVFQ-----DSPSA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 211 ENIAygDNSRQVPHEEIVN------AAKEANIHSFID--SLPDKYNTRVGdkgTQLSGGQKQRIAIARALVRQPQILLLD 282
Cdd:TIGR02769 101 VNPR--MTVRQIIGEPLRHltsldeSEQKARIAELLDmvGLRSEDADKLP---RQLSGGQLQRINIARALAVKPKLIVLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1708878085 283 EATSALDTESEKIVQEALDK--AREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQLLAEK 346
Cdd:TIGR02769 176 EAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEECDVAQLLSFK 242
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
129-337 |
2.67e-27 |
|
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: 107.36 E-value: 2.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 129 RPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLD---GEMLFDGKnakTLNIQWLRAQIGIVSQEPMLF 205
Cdd:cd03234 17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQ---PRKPDQFQKCVAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 206 DC-TIAENIAYGDNSRQvpHEEIVNAAKEANIHSFidSLPDKYNTRVGDKG-TQLSGGQKQRIAIARALVRQPQILLLDE 283
Cdd:cd03234 94 PGlTVRETLTYTAILRL--PRKSSDAIRKKRVEDV--LLRDLALTRIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1708878085 284 ATSALDTESE-KIVQEALDKAREGRTCIVIAH--RLSTIQNADKIAVVQNGKVVEQG 337
Cdd:cd03234 170 PTSGLDSFTAlNLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
116-346 |
3.30e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 108.76 E-value: 3.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 116 SIMIKDVAFNY-PNRP-EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGK----NAKTLNIQ 189
Cdd:PRK13641 2 SIKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYhitpETGNKNLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 190 WLRAQIGIVSQ--EPMLFDCTIAENIAYGDNSRQVPHEEivnaAKEANIhsfidslpdKYNTRVG------DKGT-QLSG 260
Cdd:PRK13641 82 KLRKKVSLVFQfpEAQLFENTVLKDVEFGPKNFGFSEDE----AKEKAL---------KWLKKVGlsedliSKSPfELSG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 261 GQKQRIAIARALVRQPQILLLDEATSALDTESEK-IVQEALDKAREGRTCIVIAHRLSTI-QNADKIAVVQNGKVVEQGT 338
Cdd:PRK13641 149 GQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHAS 228
|
....*...
gi 1708878085 339 HQQLLAEK 346
Cdd:PRK13641 229 PKEIFSDK 236
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
124-349 |
3.37e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 109.55 E-value: 3.37e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 124 FNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQ----LL---------ERFY--DPLDGEMLFDGKNAKTL-N 187
Cdd:PRK13631 31 FDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVThfngLIkskygtiqvGDIYigDKKNNHELITNPYSKKIkN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 188 IQWLRAQIGIVSQEP--MLFDCTIAENIAYGDNSRQVPHEEivnAAKEANIHSFIDSLPDKYNTRvgdKGTQLSGGQKQR 265
Cdd:PRK13631 111 FKELRRRVSMVFQFPeyQLFKDTIEKDIMFGPVALGVKKSE---AKKLAKFYLNKMGLDDSYLER---SPFGLSGGQKRR 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 266 IAIARALVRQPQILLLDEATSALDTESEK-IVQEALDKAREGRTCIVIAHRLSTI-QNADKIAVVQNGKVVEQGTHQQLL 343
Cdd:PRK13631 185 VAIAGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEIF 264
|
....*.
gi 1708878085 344 AEKGIY 349
Cdd:PRK13631 265 TDQHII 270
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
134-337 |
4.36e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 107.62 E-value: 4.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 134 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYD-----PLDGEMLFDGKNAKTLNIQWL--RAQIGIVSQEPMLF- 205
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneeaRVEGEVRLFGRNIYSPDVDPIevRREVGMVFQYPNPFp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 206 DCTIAENIAYG------DNSRQVPHEEIVNAAKEAnihsfidSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQIL 279
Cdd:PRK14267 99 HLTIYDNVAIGvklnglVKSKKELDERVEWALKKA-------ALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1708878085 280 LLDEATSALDTESEKIVQEALDKAREGRTCIVIAHrlSTIQNA---DKIAVVQNGKVVEQG 337
Cdd:PRK14267 172 LMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTH--SPAQAArvsDYVAFLYLGKLIEVG 230
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
117-337 |
5.24e-27 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 107.31 E-value: 5.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNrpeVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYD-----PLDGEMLFDGKNAKTLNIQWL 191
Cdd:PRK14247 4 IEIRDLKVSFGQ---VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 192 RAQIGIVSQEPM-LFDCTIAENIAYG------DNSRQVPHEEIVNAAKEANihsfidsLPDKYNTRVGDKGTQLSGGQKQ 264
Cdd:PRK14247 81 RRRVQMVFQIPNpIPNLSIFENVALGlklnrlVKSKKELQERVRWALEKAQ-------LWDEVKDRLDAPAGKLSGGQQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1708878085 265 RIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAH------RLStiqnaDKIAVVQNGKVVEQG 337
Cdd:PRK14247 154 RLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfpqqaaRIS-----DYVAFLYKGQIVEWG 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
133-346 |
5.67e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 107.41 E-value: 5.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 133 KILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPML-FDCTIAE 211
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITVRE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 212 NIAYGDNsrqvPH-----------EEIVNAAKEAnihSFIDSLPDKyntRVgdkgTQLSGGQKQRIAIARALVRQPQILL 280
Cdd:PRK11231 96 LVAYGRS----PWlslwgrlsaedNARVNQAMEQ---TRINHLADR---RL----TDLSGGQRQRAFLAMVLAQDTPVVL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1708878085 281 LDEATSALD----TESEKIVQEAldkAREGRTCIVIAHRLS-TIQNADKIAVVQNGKVVEQGTHQQLLAEK 346
Cdd:PRK11231 162 LDEPTTYLDinhqVELMRLMREL---NTQGKTVVTVLHDLNqASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
127-337 |
7.96e-27 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 105.91 E-value: 7.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 127 PNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTlNIQWLRAQIGIVSQEPMLFD 206
Cdd:cd03266 13 DVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 207 -CTIAENIAY-GDnsrqvpheeiVNAAKEANIHSFIDSLPDKY------NTRVGDkgtqLSGGQKQRIAIARALVRQPQI 278
Cdd:cd03266 92 rLTARENLEYfAG----------LYGLKGDELTARLEELADRLgmeellDRRVGG----FSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1708878085 279 LLLDEATSALDTESEKIVQEALDKAREGRTCIVIA-HRLSTIQN-ADKIAVVQNGKVVEQG 337
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQLRALGKCILFStHIMQEVERlCDRVVVLHRGRVVYEG 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
117-346 |
8.78e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 107.86 E-value: 8.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNY-PNRP-EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTL-------- 186
Cdd:PRK13651 3 IKVKNIVKIFnKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKkktkekek 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 187 ----------------NIQWLRAQIGIVSQ--EPMLFDCTIAENIAYGDNSRQVPHEEivnAAKEANIHSFIDSLPDKYN 248
Cdd:PRK13651 83 vleklviqktrfkkikKIKEIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEE---AKKRAAKYIELVGLDESYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 249 TRvgdKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKA-REGRTCIVIAHRL-STIQNADKIA 326
Cdd:PRK13651 160 QR---SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLdNVLEWTKRTI 236
|
250 260
....*....|....*....|.
gi 1708878085 327 VVQNGKVVEQG-THQQLLAEK 346
Cdd:PRK13651 237 FFKDGKIIKDGdTYDILSDNK 257
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
115-354 |
9.97e-27 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 111.79 E-value: 9.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 115 GSIMIKDVAFNY-PNRPEVkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRA 193
Cdd:PTZ00243 1307 GSLVFEGVQMRYrEGLPLV--LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRR 1384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 194 QIGIVSQEPMLFDCTIAENIaygDNSRQVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALV 273
Cdd:PTZ00243 1385 QFSMIPQDPVLFDGTVRQNV---DPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALL 1461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 274 -RQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQL-LAEKGIYYS 351
Cdd:PTZ00243 1462 kKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELvMNRQSIFHS 1541
|
...
gi 1708878085 352 LVN 354
Cdd:PTZ00243 1542 MVE 1544
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
134-338 |
1.35e-26 |
|
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: 105.68 E-value: 1.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 134 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWL-RAQIGIVSQEPMLF-DCTIAE 211
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVPQGREIFpRLTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 212 NI-----AYGDNSRQVPHEeivnaakeanIHSFIDSLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQPQILLLDEATS 286
Cdd:TIGR03410 95 NLltglaALPRRSRKIPDE----------IYELFPVLKEMLGRRGGD----LSGGQQQQLAIARALVTRPKLLLLDEPTE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1708878085 287 ALDTESEKIVQEALDK--AREGRTCIVIAHRLS-TIQNADKIAVVQNGKVVEQGT 338
Cdd:TIGR03410 161 GIQPSIIKDIGRVIRRlrAEGGMAILLVEQYLDfARELADRYYVMERGRVVASGA 215
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
132-338 |
3.63e-26 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 105.12 E-value: 3.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 132 VKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNiQWLRAQIGIVS--QEPMLF-DCT 208
Cdd:COG0411 17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP-PHRIARLGIARtfQNPRLFpELT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 209 IAEN--IAYGDNSRQVPHEEIVN----AAKEANIHSFIDS------LPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQP 276
Cdd:COG0411 96 VLENvlVAAHARLGRGLLAALLRlpraRREEREARERAEEllervgLADRADEPAGN----LSYGQQRRLEIARALATEP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1708878085 277 QILLLDEATSAL-DTESEKIVqEALDKARE--GRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGT 338
Cdd:COG0411 172 KLLLLDEPAAGLnPEETEELA-ELIRRLRDerGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
119-344 |
5.91e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 108.64 E-value: 5.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKDVAFNYPNRPEVK-ILQGLNLKVEKGQTLALVGSSGCGKS-TVVQLLERFYDP----LDGEMLFDGKNAKTLNIQWLR 192
Cdd:PRK15134 8 IENLSVAFRQQQTVRtVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 193 A----QIGIVSQEPML-------FDCTIAENIAYGDNSRQVP-HEEIVNAAKEANIHsfidslpdKYNTRVGDKGTQLSG 260
Cdd:PRK15134 88 GvrgnKIAMIFQEPMVslnplhtLEKQLYEVLSLHRGMRREAaRGEILNCLDRVGIR--------QAAKRLTDYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 261 GQKQRIAIARALVRQPQILLLDEATSALD-TESEKIVQEALDKARE-GRTCIVIAHRLSTI-QNADKIAVVQNGKVVEQG 337
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDvSVQAQILQLLRELQQElNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQN 239
|
....*..
gi 1708878085 338 THQQLLA 344
Cdd:PRK15134 240 RAATLFS 246
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
133-342 |
6.04e-26 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 106.71 E-value: 6.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 133 KILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwlRAQIGIVSQEPMLF-DCTIAE 211
Cdd:PRK10851 16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHAR--DRKVGFVFQHYALFrHMTVFD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 212 NIAYGdnSRQVPHEEIVNAA----KEANIHSFI--DSLPDKYNTrvgdkgtQLSGGQKQRIAIARALVRQPQILLLDEAT 285
Cdd:PRK10851 94 NIAFG--LTVLPRRERPNAAaikaKVTQLLEMVqlAHLADRYPA-------QLSGGQKQRVALARALAVEPQILLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 286 SALDTESEKIVQEALDKARE--GRTCIVIAH-RLSTIQNADKIAVVQNGKVVEQGTHQQL 342
Cdd:PRK10851 165 GALDAQVRKELRRWLRQLHEelKFTSVFVTHdQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
134-353 |
8.48e-26 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 104.55 E-value: 8.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 134 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKnaktlniqwlraqIGIVSQEPMLFDCTIAENI 213
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIKENI 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 214 AYGDNSRQVPHEEIVNAAK-EANIHSFidslPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTES 292
Cdd:cd03291 119 IFGVSYDEYRYKSVVKACQlEEDITKF----PEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1708878085 293 EK-IVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLAEKGIYYSLV 353
Cdd:cd03291 195 EKeIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQSLRPDFSSKL 256
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
131-335 |
1.53e-25 |
|
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: 102.90 E-value: 1.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 131 EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQL---LERfydPLDGEMLFDGKNAKTLN----IQWLRAQIGIVSQE-- 201
Cdd:COG4181 24 ELTILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDedarARLRARHVGFVFQSfq 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 202 --PMLfdcTIAENIAygdnsrqVPHEE--IVNAAKEAnihsfIDSLpdkynTRVGDKG------TQLSGGQKQRIAIARA 271
Cdd:COG4181 101 llPTL---TALENVM-------LPLELagRRDARARA-----RALL-----ERVGLGHrldhypAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1708878085 272 LVRQPQILLLDEATSALDTE-SEKIVQEALDKARE-GRTCIVIAHRLSTIQNADKIAVVQNGKVVE 335
Cdd:COG4181 161 FATEPAILFADEPTGNLDAAtGEQIIDLLFELNRErGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
116-338 |
2.02e-25 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 104.93 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 116 SIMIKDVAFNYPNRPEVkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQL---LERFydpLDGEMLFDGKNAKTLniqwlr 192
Cdd:PRK11650 3 GLKLQAVRKSYDGKTQV--IKGIDLDVADGEFIVLVGPSGCGKSTLLRMvagLERI---TSGEIWIGGRVVNEL------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 193 aqigivsqEP------MLFD-------CTIAENIAYGDNSRQVPHEEI----VNAAKEANIHSFIDSLPdkyntrvgdkg 255
Cdd:PRK11650 72 --------EPadrdiaMVFQnyalyphMSVRENMAYGLKIRGMPKAEIeervAEAARILELEPLLDRKP----------- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 256 TQLSGGQKQRIAIARALVRQPQILLLDEATSALDTeseKI-VQEALD----KAREGRTCIVIAH-RLSTIQNADKIaVVQ 329
Cdd:PRK11650 133 RELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDA---KLrVQMRLEiqrlHRRLKTTSLYVTHdQVEAMTLADRV-VVM 208
|
250
....*....|
gi 1708878085 330 NGKVVEQ-GT 338
Cdd:PRK11650 209 NGGVAEQiGT 218
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
134-343 |
2.05e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 102.93 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 134 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPML-FDCTIAEN 212
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLsFPFTVEEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 213 IAYG---DNSRQVPHEEIVNAA-KEANIHSFIDSLpdkYntrvgdkgTQLSGGQKQRIAIARALVR------QPQILLLD 282
Cdd:PRK13548 97 VAMGrapHGLSRAEDDALVAAAlAQVDLAHLAGRD---Y--------PQLSGGEQQRVQLARVLAQlwepdgPPRWLLLD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1708878085 283 EATSALD-TESEKIVQEALDKARE-GRTCIVIAHRLS-TIQNADKIAVVQNGKVVEQGTHQQLL 343
Cdd:PRK13548 166 EPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVL 229
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
131-347 |
2.57e-25 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 102.45 E-value: 2.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 131 EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL---ERfYDPLDGEMLFDGKNAKTLNIQwLRAQIGI-VS-QEP--- 202
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDILELSPD-ERARAGIfLAfQYPvei 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 203 -----MLFDCTIAENIAYGDNSRQVPHEEIVNAAKEANihsfidsLPDKYNTR---VGdkgtqLSGGQKQRIAIARALVR 274
Cdd:COG0396 90 pgvsvSNFLRTALNARRGEELSAREFLKLLKEKMKELG-------LDEDFLDRyvnEG-----FSGGEKKRNEILQMLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1708878085 275 QPQILLLDEATSALDTESEKIVQEALDKAR-EGRTCIVIAH--RLSTIQNADKIAVVQNGKVVEQGTHQ--QLLAEKG 347
Cdd:COG0396 158 EPKLAILDETDSGLDIDALRIVAEGVNKLRsPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKElaLELEEEG 235
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
129-344 |
3.13e-25 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 102.61 E-value: 3.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 129 RPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWlRAQ-IGIVSQEPmlfdc 207
Cdd:COG4167 23 RQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY-RCKhIRMIFQDP----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 208 tiaeNIAYgdNSRQvpheeivnaakeaNIHSFIDsLPDKYNT----------------RVG-------DKGTQLSGGQKQ 264
Cdd:COG4167 97 ----NTSL--NPRL-------------NIGQILE-EPLRLNTdltaeereerifatlrLVGllpehanFYPHMLSSGQKQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 265 RIAIARALVRQPQILLLDEATSALD-TESEKIVQEALD-KAREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQ 341
Cdd:COG4167 157 RVALARALILQPKIIIADEALAALDmSVRSQIINLMLElQEKLGISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGKTAE 236
|
...
gi 1708878085 342 LLA 344
Cdd:COG4167 237 VFA 239
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
118-334 |
4.86e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 102.09 E-value: 4.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 118 MIK----DVAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNiQWLRA 193
Cdd:COG1101 1 MLElknlSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP-EYKRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 194 Q-IGIVSQEPMLFDC---TIAEN--IAYGDNSRQvpheEIVNAAKEANIHSFIDS-------LPDKYNTRVGdkgtQLSG 260
Cdd:COG1101 80 KyIGRVFQDPMMGTApsmTIEENlaLAYRRGKRR----GLRRGLTKKRRELFRELlatlglgLENRLDTKVG----LLSG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1708878085 261 GQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLS-TIQNADKIAVVQNGKVV 334
Cdd:COG1101 152 GQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNMEqALDYGNRLIMMHEGRII 228
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
119-314 |
5.17e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 101.86 E-value: 5.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKDVAFNYPN-RPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNaktlnIQWLRAQIGI 197
Cdd:COG4525 6 VRHVSVRYPGgGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVP-----VTGPGADRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 198 VSQEPMLFD-CTIAENIAYGDNSRQVPHEEIVNAAKEanihsfidslpdkYNTRVGDKGT------QLSGGQKQRIAIAR 270
Cdd:COG4525 81 VFQKDALLPwLNVLDNVAFGLRLRGVPKAERRARAEE-------------LLALVGLADFarrriwQLSGGMRQRVGIAR 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1708878085 271 ALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAH 314
Cdd:COG4525 148 ALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
135-331 |
6.41e-25 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 101.00 E-value: 6.41e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 135 LQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNaktlnIQWLRAQIGIVSQEPMLFD-CTIAENI 213
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQ-----ITEPGPDRMVVFQNYSLLPwLTVRENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 214 AYGDNS--RQVPHEEivnaaKEANIHSFIDSLPdkyNTRVGDKG-TQLSGGQKQRIAIARALVRQPQILLLDEATSALDT 290
Cdd:TIGR01184 76 ALAVDRvlPDLSKSE-----RRAIVEEHIALVG---LTEAADKRpGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1708878085 291 ESEKIVQEALDKARE--GRTCIVIAHRL-STIQNADKIAVVQNG 331
Cdd:TIGR01184 148 LTRGNLQEELMQIWEehRVTVLMVTHDVdEALLLSDRVVMLTNG 191
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
132-334 |
6.96e-25 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 105.29 E-value: 6.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 132 VKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFY--DPLDGEMLFDGKNAKTLNIQWL-RAQIGIVSQEPMLF-DC 207
Cdd:TIGR02633 14 VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphGTWDGEIYWSGSPLKASNIRDTeRAGIVIIHQELTLVpEL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 208 TIAENIAYGD----NSRQVPHEEIVNAAKEANIHSFIDSLPdkyNTR-VGDKGtqlsGGQKQRIAIARALVRQPQILLLD 282
Cdd:TIGR02633 94 SVAENIFLGNeitlPGGRMAYNAMYLRAKNLLRELQLDADN---VTRpVGDYG----GGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1708878085 283 EATSAL-DTESEKIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVV 334
Cdd:TIGR02633 167 EPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQHV 220
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
121-344 |
1.34e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 101.24 E-value: 1.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 121 DVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGK--NAKTLNIQWLRAQIGIV 198
Cdd:PRK13638 6 DLWFRYQDEP---VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 199 SQEP--MLFDCTIAENIAYGDNSRQVPHEEIVNAAKEANihsfidSLPDKYNTRvgDKGTQ-LSGGQKQRIAIARALVRQ 275
Cdd:PRK13638 83 FQDPeqQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEAL------TLVDAQHFR--HQPIQcLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1708878085 276 PQILLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLSTI-QNADKIAVVQNGKVVEQGTHQQLLA 344
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
134-344 |
2.33e-24 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 104.02 E-value: 2.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 134 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYdPLDGEMLFDGKNAKTLNIQWL---RAQIGIVSQEP---MLFDC 207
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPnssLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 208 TIAENIAYGdnsRQVPHEEIVNAAKEANIHSFIDSLPDKYNTRvGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSA 287
Cdd:PRK15134 380 NVLQIIEEG---LRVHQPTLSAAQREQQVIAVMEEVGLDPETR-HRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1708878085 288 LDteseKIVQE---ALDKAREGR---TCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQLLA 344
Cdd:PRK15134 456 LD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
117-335 |
2.95e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.61 E-value: 2.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFdGKNAKtlniqwlraqIG 196
Cdd:COG0488 316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK----------IG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 IVSQEPMLFDC--TIAENIAygdnsrqvpheEIVNAAKEANIHSFIDSL---PDKYNTRVGDkgtqLSGGQKQRIAIARA 271
Cdd:COG0488 382 YFDQHQEELDPdkTVLDELR-----------DGAPGGTEQEVRGYLGRFlfsGDDAFKPVGV----LSGGEKARLALAKL 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1708878085 272 LVRQPQILLLDEATSALDTESEKIVQEALDkAREGrTCIVIAH-R--LSTIqnADKIAVVQNGKVVE 335
Cdd:COG0488 447 LLSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVRE 509
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
117-345 |
4.61e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 99.88 E-value: 4.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYpnRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 196
Cdd:PRK13652 4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 IVSQEP--MLFDCTIAENIAYGDNSRQVPHEEIVNAAKEA----NIHSFIDSLPDkyntrvgdkgtQLSGGQKQRIAIAR 270
Cdd:PRK13652 82 LVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSAlhmlGLEELRDRVPH-----------HLSGGEKKRVAIAG 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1708878085 271 ALVRQPQILLLDEATSALDTESEKIVQEALDKARE--GRTCIVIAHRLSTI-QNADKIAVVQNGKVVEQGTHQQLLAE 345
Cdd:PRK13652 151 VIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIFLQ 228
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
119-358 |
8.28e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 102.88 E-value: 8.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKDVAFNYPNRPE-VKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWL----RA 193
Cdd:PRK10535 7 LKDIRRSYPSGEEqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaqlrRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 194 QIGIVSQE-PMLFDCTIAENIaygdnsrQVP--HEEIVNAAKEANIHSFIDSLpdKYNTRVGDKGTQLSGGQKQRIAIAR 270
Cdd:PRK10535 87 HFGFIFQRyHLLSHLTAAQNV-------EVPavYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 271 ALVRQPQILLLDEATSALDTESEKIVQEALDKARE-GRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLAEKGIY 349
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQEKVNVAGGT 237
|
....*....
gi 1708878085 350 YSLVNVQSG 358
Cdd:PRK10535 238 EPVVNTASG 246
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
129-335 |
9.06e-24 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 98.99 E-value: 9.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 129 RPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN----------IQWL------- 191
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkafrrdIQMVfqdsisa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 192 ---RAQIGIVSQEPM--LFDCTIAEniaygdnsRQVPHEEIVNAAKEANihSFIDSLPdkyntrvgdkgTQLSGGQKQRI 266
Cdd:PRK10419 102 vnpRKTVREIIREPLrhLLSLDKAE--------RLARASEMLRAVDLDD--SVLDKRP-----------PQLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1708878085 267 AIARALVRQPQILLLDEATSALDTESEKIVQEALDKARE--GRTCIVIAHRLSTIQN-ADKIAVVQNGKVVE 335
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqfGTACLFITHDLRLVERfCQRVMVMDNGQIVE 232
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
130-335 |
1.39e-23 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 101.40 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 130 PEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYdP---LDGEMLFDGKNAKTLNI-QWLRAQIGIVSQE---- 201
Cdd:NF040905 12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PhgsYEGEILFDGEVCRFKDIrDSEALGIVIIHQElali 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 202 PMLfdcTIAENIAYGdNSRqvpheeivnaAKeaniHSFID---------------SLPDKYNTRVGDKGTqlsgGQKQRI 266
Cdd:NF040905 91 PYL---SIAENIFLG-NER----------AK----RGVIDwnetnrrarellakvGLDESPDTLVTDIGV----GKQQLV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1708878085 267 AIARALVRQPQILLLDEATSAL-DTESEKIVQEALDKAREGRTCIVIAHRLSTI-QNADKIAVVQNGKVVE 335
Cdd:NF040905 149 EIAKALSKDVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIrRVADSITVLRDGRTIE 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
116-346 |
1.86e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 98.31 E-value: 1.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 116 SIMIKDVAFNYPN-RP-EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDG----KNAKTLNIQ 189
Cdd:PRK13646 2 TIRFDNVSYTYQKgTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDititHKTKDKYIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 190 WLRAQIGIVSQ--EPMLFDCTIAENIAYGDNSRQVPHEEIVNAAkeaniHSFIDSLPDKYNTrVGDKGTQLSGGQKQRIA 267
Cdd:PRK13646 82 PVRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYA-----HRLLMDLGFSRDV-MSQSPFQMSGGQMRKIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 268 IARALVRQPQILLLDEATSALDTESEKIVQEALDKAR--EGRTCIVIAHRLSTI-QNADKIAVVQNGKVVEQGTHQQLLA 344
Cdd:PRK13646 156 IVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFK 235
|
..
gi 1708878085 345 EK 346
Cdd:PRK13646 236 DK 237
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
131-336 |
2.15e-23 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 96.77 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 131 EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQW---LRAQ-IGIVSQEPMLFD 206
Cdd:PRK10584 22 ELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEArakLRAKhVGFVFQSFMLIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 207 CTIA-ENIAY-----GDNSRQvPHEEIVNAAKEANIHSFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARALVRQPQILL 280
Cdd:PRK10584 102 TLNAlENVELpallrGESSRQ-SRNGAKALLEQLGLGKRLDHLP-----------AQLSGGEQQRVALARAFNGRPDVLF 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1708878085 281 LDEATSALDTES-EKIVQEALDKARE-GRTCIVIAHRLSTIQNADKIAVVQNGKVVEQ 336
Cdd:PRK10584 170 ADEPTGNLDRQTgDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
126-314 |
3.23e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 97.08 E-value: 3.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 126 YPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNaktlnIQWLRAQIGIVSQ-EPML 204
Cdd:PRK11248 11 YGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKP-----VEGPGAERGVVFQnEGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 205 FDCTIAENIAYGDNSRQVPHEEIVNAAKEANIhsfidslpdkyntRVGDKGT------QLSGGQKQRIAIARALVRQPQI 278
Cdd:PRK11248 83 PWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLK-------------KVGLEGAekryiwQLSGGQRQRVGIARALAANPQL 149
|
170 180 190
....*....|....*....|....*....|....*...
gi 1708878085 279 LLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAH 314
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
90-344 |
3.36e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 101.35 E-value: 3.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 90 LFLLFERV----PSIDSyseegEKPetfggSIMIKDVAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL 165
Cdd:PLN03130 594 LLLAEERVllpnPPLEP-----GLP-----AISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAM 663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 166 ErfydpldGEMlfdgkNAKTLNIQWLRAQIGIVSQEPMLFDCTIAENIAYGDNSRQVPHEEIVNAAKeanIHSFIDSLPD 245
Cdd:PLN03130 664 L-------GEL-----PPRSDASVVIRGTVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTA---LQHDLDLLPG 728
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 246 KYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTE-SEKIVQEALDKAREGRTCIVIAHRLSTIQNADK 324
Cdd:PLN03130 729 GDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHvGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDR 808
|
250 260
....*....|....*....|
gi 1708878085 325 IAVVQNGKVVEQGTHQQLLA 344
Cdd:PLN03130 809 IILVHEGMIKEEGTYEELSN 828
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
1-90 |
3.78e-23 |
|
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 98.12 E-value: 3.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 1 MYREHLHVPYRNSVKKAHIFGFCFALSQAMMFFTYAGCFRFGAYLVVNGHMQ-YKSVFLVFSAVVFGAMALGQSSSFAPd 79
Cdd:cd18558 223 RYAQNLEIAKRNGIKKAITFNISMGAAFLLIYASYALAFWYGTYLVTQQEYSiGEVLTVFFSVLIGAFSAGQQVPSIEA- 301
|
90
....*....|.
gi 1708878085 80 YAKAKTSAAHL 90
Cdd:cd18558 302 FANARGAAYHI 312
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
112-345 |
4.12e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 97.39 E-value: 4.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 112 TFGGSIMIKDVAFNYPNRP--EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQL-----LERFYDPLDGEMLFDGKNAK 184
Cdd:PRK13645 2 DFSKDIILDNVSYTYAKKTpfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLtngliISETGQTIVGDYAIPANLKK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 185 TLNIQWLRAQIGIVSQEP--MLFDCTIAENIAYGDNSRQVPHEEIVNAAKEanihsFID--SLPDKYNTRvgdKGTQLSG 260
Cdd:PRK13645 82 IKEVKRLRKEIGLVFQFPeyQLFQETIEKDIAFGPVNLGENKQEAYKKVPE-----LLKlvQLPEDYVKR---SPFELSG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 261 GQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQ---EALDKaREGRTCIVIAHRLSTI-QNADKIAVVQNGKVVEQ 336
Cdd:PRK13645 154 GQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFInlfERLNK-EYKKRIIMVTHNMDQVlRIADEVIVMHEGKVISI 232
|
250
....*....|....*
gi 1708878085 337 G------THQQLLAE 345
Cdd:PRK13645 233 GspfeifSNQELLTK 247
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
116-353 |
4.14e-23 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 101.21 E-value: 4.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 116 SIMIKDVAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQllerfydpldgEMLFDGKNAKTLNIQwLRAQI 195
Cdd:PLN03232 614 AISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLIS-----------AMLGELSHAETSSVV-IRGSV 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 196 GIVSQEPMLFDCTIAENIAYGDNSRQVPHEEIVNAAKeanIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQ 275
Cdd:PLN03232 682 AYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTA---LQHDLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSN 758
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1708878085 276 PQILLLDEATSALDTE-SEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQGTHQQLLAEKGIYYSLV 353
Cdd:PLN03232 759 SDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLM 837
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
114-333 |
7.42e-23 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 95.90 E-value: 7.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 114 GGSIMIKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLfdgknAKTLNIQWLRA 193
Cdd:PRK11247 10 GTPLLLNAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL-----AGTAPLAEARE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 194 QIGIVSQEPMLFDC-TIAENIAYG--DNSRQVPHE--EIVNAAKEANihsfidslpdkyntrvgDKGTQLSGGQKQRIAI 268
Cdd:PRK11247 82 DTRLMFQDARLLPWkKVIDNVGLGlkGQWRDAALQalAAVGLADRAN-----------------EWPAALSGGQKQRVAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1708878085 269 ARALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLS-TIQNADKIAVVQNGKV 333
Cdd:PRK11247 145 ARALIHRPGLLLLDEPLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
131-337 |
8.87e-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: 94.52 E-value: 8.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 131 EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERF--YDPLDGEMLFDGKNAKTLNIQwLRAQIGIVsqepMLFdct 208
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPE-ERARLGIF----LAF--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 209 iaeniaygdnsrQVPhEEIvnaaKEANIHSFIDSLpdkyntrvgDKGtqLSGGQKQRIAIARALVRQPQILLLDEATSAL 288
Cdd:cd03217 84 ------------QYP-PEI----PGVKNADFLRYV---------NEG--FSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1708878085 289 DTESEKIVQEALDKAR-EGRTCIVIAH--RLSTIQNADKIAVVQNGKVVEQG 337
Cdd:cd03217 136 DIDALRLVAEVINKLReEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
113-344 |
9.09e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 96.32 E-value: 9.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 113 FGGSIMIKDVAFNYPNRPevkilqglnlkvekgqTLALVGSSGCGKSTVVQLLERFYDPLDG-----EMLFDGKNA-KTL 186
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARA----------------VTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfNYR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 187 NIQWLRAQIGIVSQEPMLFDCTIAENIAYGDNSRQ-VPHEEIVNAAkEANIHSFidSLPDKYNTRVGDKGTQLSGGQKQR 265
Cdd:PRK14271 95 DVLEFRRRVGMLFQRPNPFPMSIMDNVLAGVRAHKlVPRKEFRGVA-QARLTEV--GLWDAVKDRLSDSPFRLSGGQQQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 266 IAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQLLA 344
Cdd:PRK14271 172 LCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQLFS 251
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
118-345 |
9.39e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 96.34 E-value: 9.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 118 MIKDVAFNY---PNRP-EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEM----LFDGKNAKTLNIQ 189
Cdd:PRK13643 1 MIKFEKVNYtyqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdIVVSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 190 WLRAQIGIVSQEP--MLFDCTIAENIAYGDNSRQVPHEEIVN-AAKEANIHSFIDSLPDKyntrvgdKGTQLSGGQKQRI 266
Cdd:PRK13643 81 PVRKKVGVVFQFPesQLFEETVLKDVAFGPQNFGIPKEKAEKiAAEKLEMVGLADEFWEK-------SPFELSGGQMRRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 267 AIARALVRQPQILLLDEATSALDTESEKIVQEALDKARE-GRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQLLA 344
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQ 233
|
.
gi 1708878085 345 E 345
Cdd:PRK13643 234 E 234
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
131-344 |
1.14e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 95.42 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 131 EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTL-------------NIQWLRAQIGI 197
Cdd:PRK10619 17 EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvadknQLRLLRTRLTM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 198 VSQEPMLFD-CTIAENIAygdnsrQVPHEEIVNAAKEANIHSFidslpdKYNTRVG-DKGTQ------LSGGQKQRIAIA 269
Cdd:PRK10619 97 VFQHFNLWShMTVLENVM------EAPIQVLGLSKQEARERAV------KYLAKVGiDERAQgkypvhLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1708878085 270 RALVRQPQILLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQLLA 344
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
133-342 |
1.44e-22 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 96.70 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 133 KILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN-IQWL--RAQIGIVSQEP------- 202
Cdd:PRK15079 35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKdDEWRavRSDIQMIFQDPlaslnpr 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 203 MlfdcTIAENIA------YGDNSRQVPHEEIVNA-AKEANIHSFIDSLPDKYntrvgdkgtqlSGGQKQRIAIARALVRQ 275
Cdd:PRK15079 115 M----TIGEIIAeplrtyHPKLSRQEVKDRVKAMmLKVGLLPNLINRYPHEF-----------SGGQCQRIGIARALILE 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 276 PQILLLDEATSALDTESEKIVQEALDK-ARE-GRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQL 342
Cdd:PRK15079 180 PKLIICDEPVSALDVSIQAQVVNLLQQlQREmGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
119-314 |
2.61e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.83 E-value: 2.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGknaktlniqwlRAQIGIV 198
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 199 SQEPMLFD-CTIAENIAYGDNSR-----------QVPHEEIVNAAKEANIHSFIDSL-------------------PDKY 247
Cdd:COG0488 67 PQEPPLDDdLTVLDTVLDGDAELraleaeleeleAKLAEPDEDLERLAELQEEFEALggweaearaeeilsglgfpEEDL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1708878085 248 NTRVGDkgtqLSGGQKQRIAIARALVRQPQILLLDEATSALDTESekiVQ--EALDKAREGrTCIVIAH 314
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwlEEFLKNYPG-TVLVVSH 207
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
131-331 |
3.01e-22 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 93.65 E-value: 3.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 131 EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKN-----AKTLNIQWL---RAQIGIVSQ-- 200
Cdd:COG4778 23 RLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdlAQASPREILalrRRTIGYVSQfl 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 201 -------------EPMLfdctiaeniaygdnSRQVPHEEIVNAAKEA----NIHSFIDSLPDkyNTrvgdkgtqLSGGQK 263
Cdd:COG4778 103 rviprvsaldvvaEPLL--------------ERGVDREEARARARELlarlNLPERLWDLPP--AT--------FSGGEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 264 QRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIV-IAHRLSTIQN-ADKIAVVQNG 331
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVREAvADRVVDVTPF 228
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
116-337 |
3.18e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 96.25 E-value: 3.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 116 SIMIKDVAFNYPnrpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKtlNIQWLRAQI 195
Cdd:PRK11000 3 SVTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN--DVPPAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 196 GIVSQEPMLF-DCTIAENIAYGDNSRQVPHEEI---VNAAKEA-NIHSFIDSLPdkyntrvgdkgTQLSGGQKQRIAIAR 270
Cdd:PRK11000 78 GMVFQSYALYpHLSVAENMSFGLKLAGAKKEEInqrVNQVAEVlQLAHLLDRKP-----------KALSGGQRQRVAIGR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1708878085 271 ALVRQPQILLLDEATSALDTE---SEKIVQEALDKaREGRTCIVIAH-RLSTIQNADKIAVVQNGKVVEQG 337
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLDAAlrvQMRIEISRLHK-RLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
63-337 |
3.96e-22 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 98.31 E-value: 3.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 63 VVFGAMALGQSSSFAPDYAKAKTSAAHlfllfervpsidsysEEGEKPETFGGSIMIKDVAFnYPNRPEVkILQGLNLKV 142
Cdd:PTZ00243 621 VVVEDTDYGSPSSASRHIVEGGTGGGH---------------EATPTSERSAKTPKMKTDDF-FELEPKV-LLRDVSVSV 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 143 EKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMlfdgknaktlniqWLRAQIGIVSQEPMLFDCTIAENIAYGDNSRQv 222
Cdd:PTZ00243 684 PRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAERSIAYVPQQAWIMNATVRGNILFFDEEDA- 749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 223 phEEIVNAAKEANIHSFIDSLPDKYNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTE-SEKIVQEALD 301
Cdd:PTZ00243 750 --ARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGERVVEECFL 827
|
250 260 270
....*....|....*....|....*....|....*.
gi 1708878085 302 KAREGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQG 337
Cdd:PTZ00243 828 GALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSG 863
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
117-343 |
4.06e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 96.45 E-value: 4.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNypnRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 196
Cdd:PRK09536 4 IDVSDLSVE---FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 IVSQEPML-FDCTIAENIAYGdnsrQVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGDKG-TQLSGGQKQRIAIARALVR 274
Cdd:PRK09536 81 SVPQDTSLsFEFDVRQVVEMG----RTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPvTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1708878085 275 QPQILLLDEATSALDTESE-KIVQEALDKAREGRTCIVIAHRLS-TIQNADKIAVVQNGKVVEQGTHQQLL 343
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVL 227
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
135-342 |
5.04e-22 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 92.82 E-value: 5.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 135 LQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDG----KNAKTLniqwlRAQIGIVSQEPMLFD-CTI 209
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGhdvvREPREV-----RRRIGIVFQDLSVDDeLTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 210 AENIA-----YGdnsrqVPHEEIVNAAKEAniHSFIDsLPDKYNTRVGdkgtQLSGGQKQRIAIARALVRQPQILLLDEA 284
Cdd:cd03265 91 WENLYiharlYG-----VPGAERRERIDEL--LDFVG-LLEAADRLVK----TYSGGMRRRLEIARSLVHRPEVLFLDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1708878085 285 TSALDTESEKIVQEALDK--AREGRTCIVIAHRLSTI-QNADKIAVVQNGKVVEQGTHQQL 342
Cdd:cd03265 159 TIGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
135-319 |
5.18e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 93.02 E-value: 5.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 135 LQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNA---KTLNIQWLRAQIGIVSQEP-MLFDCTIA 210
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlKNREVPFLRRQIGMIFQDHhLLMDRTVY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 211 ENIAygdnsrqVPHeeIVNAAKEANIHSFIDSLPDKyntrVG--DKG----TQLSGGQKQRIAIARALVRQPQILLLDEA 284
Cdd:PRK10908 98 DNVA-------IPL--IIAGASGDDIRRRVSAALDK----VGllDKAknfpIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190
....*....|....*....|....*....|....*.
gi 1708878085 285 TSALDTE-SEKIVQEALDKAREGRTCIVIAHRLSTI 319
Cdd:PRK10908 165 TGNLDDAlSEGILRLFEEFNRVGVTVLMATHDIGLI 200
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
117-342 |
1.85e-21 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 92.52 E-value: 1.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWL---RA 193
Cdd:PRK11831 8 VDMRGVSFTRGNRC---IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 194 QIGIVSQEPMLF-DCTIAENIAYgdnsrqvPHEEIVNAAkEANIHSFIDSLPDKyntrVGDKG------TQLSGGQKQRI 266
Cdd:PRK11831 85 RMSMLFQSGALFtDMNVFDNVAY-------PLREHTQLP-APLLHSTVMMKLEA----VGLRGaaklmpSELSGGMARRA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1708878085 267 AIARALVRQPQILLLDEATSALDTESEKIVQEALDKARE--GRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQL 342
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQAL 231
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
116-346 |
1.95e-21 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 93.74 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 116 SIMIKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTlNIQWLRAQI 195
Cdd:PRK13536 41 AIDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARI 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 196 GIVSQepmlFD-----CTIAENIA-----YGDNSRQVpheeivnaakEANIHSFID--SLPDKYNTRVGDkgtqLSGGQK 263
Cdd:PRK13536 117 GVVPQ----FDnldleFTVRENLLvfgryFGMSTREI----------EAVIPSLLEfaRLESKADARVSD----LSGGMK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 264 QRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDK--AReGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQ 340
Cdd:PRK13536 179 RRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVLEAGRKIAEGRPH 257
|
....*.
gi 1708878085 341 QLLAEK 346
Cdd:PRK13536 258 ALIDEH 263
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
126-323 |
2.21e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 90.37 E-value: 2.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 126 YPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKnaktlniqwlrAQIGIVSQ---EP 202
Cdd:NF040873 2 YGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-----------ARVAYVPQrseVP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 203 MLFDCTIAENIAYGDNSRQVPHEEIvNAAKEANIhsfIDSLpdkynTRVGDKG------TQLSGGQKQRIAIARALVRQP 276
Cdd:NF040873 68 DSLPLTVRDLVAMGRWARRGLWRRL-TRDDRAAV---DDAL-----ERVGLADlagrqlGELSGGQRQRALLAQGLAQEA 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1708878085 277 QILLLDEATSALDTESEKIVQEAL-DKAREGRTCIVIAHRLSTIQNAD 323
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRAD 186
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
130-345 |
2.23e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 94.98 E-value: 2.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 130 PEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQ-WLRAQIGIVSQEPMLF-DC 207
Cdd:PRK11288 15 PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTaALAAGVAIIYQELHLVpEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 208 TIAENIAYGdnsrQVPH-------EEIVNAAKEANIHSFIDSLPDkynTRVGDkgtqLSGGQKQRIAIARALVRQPQILL 280
Cdd:PRK11288 95 TVAENLYLG----QLPHkggivnrRLLNYEAREQLEHLGVDIDPD---TPLKY----LSIGQRQMVEIAKALARNARVIA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1708878085 281 LDEATSALDT-ESE---KIVQEALDkarEGRTCIVIAHRLSTI-QNADKIAVVQNGKVVE------QGTHQQLLAE 345
Cdd:PRK11288 164 FDEPTSSLSArEIEqlfRVIRELRA---EGRVILYVSHRMEEIfALCDAITVFKDGRYVAtfddmaQVDRDQLVQA 236
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
133-344 |
1.08e-20 |
|
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: 89.52 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 133 KILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIqWLRAQIGI--VSQEPMLF-DCTI 209
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPM-HKRARLGIgyLPQEASIFrKLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 210 AENIAYGDNSRQVPHEEIVNAAkEANIHSF-IDSLPDKyntrvgdKGTQLSGGQKQRIAIARALVRQPQILLLDEATSAL 288
Cdd:cd03218 93 EENILAVLEIRGLSKKEREEKL-EELLEEFhITHLRKS-------KASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1708878085 289 DTESEKIVQEALDKAREGRTCIVIA-HRLS-TIQNADKIAVVQNGKVVEQGTHQQLLA 344
Cdd:cd03218 165 DPIAVQDIQKIIKILKDRGIGVLITdHNVReTLSITDRAYIIYEGKVLAEGTPEEIAA 222
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
134-315 |
1.98e-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: 86.82 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 134 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL--------ERFYDPLDGEMLFdgknaktlniqwlraqigiVSQEPMLF 205
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALaglwpwgsGRIGMPEGEDLLF-------------------LPQRPYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 206 DCTIAENIAYgdnsrqvPHEEIvnaakeanihsfidslpdkyntrvgdkgtqLSGGQKQRIAIARALVRQPQILLLDEAT 285
Cdd:cd03223 77 LGTLREQLIY-------PWDDV------------------------------LSGGEQQRLAFARLLLHKPKFVFLDEAT 119
|
170 180 190
....*....|....*....|....*....|
gi 1708878085 286 SALDTESEKIVQEALDKarEGRTCIVIAHR 315
Cdd:cd03223 120 SALDEESEDRLYQLLKE--LGITVISVGHR 147
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
131-338 |
3.57e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 89.40 E-value: 3.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 131 EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGK--NAKTlniqwlRAQIGIVSQEPMLF-DC 207
Cdd:COG4152 13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEplDPED------RRRIGYLPEERGLYpKM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 208 TIAENIAY-----GdnsrqVPHEEIVNAAKEanihsFID--SLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQPQILL 280
Cdd:COG4152 87 KVGEQLVYlarlkG-----LSKAEAKRRADE-----WLErlGLGDRANKKVEE----LSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 281 LDEATSALDTES-EKIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGT 338
Cdd:COG4152 153 LDEPFSGLDPVNvELLKDVIRELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGS 212
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
124-337 |
4.35e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 91.46 E-value: 4.35e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 124 FNYPNRpEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN---IQWLRAQIGIVSQ 200
Cdd:PRK10261 330 LNRVTR-EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSpgkLQALRRDIQFIFQ 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 201 EPmlfdctiaeniaYGD-NSRQVPHEEIVNAAKeanIHSFIDSLPDKYNT-----RVGDKGT-------QLSGGQKQRIA 267
Cdd:PRK10261 409 DP------------YASlDPRQTVGDSIMEPLR---VHGLLPGKAAAARVawlleRVGLLPEhawryphEFSGGQRQRIC 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1708878085 268 IARALVRQPQILLLDEATSALDTE-SEKIVQEALDKARE-GRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQG 337
Cdd:PRK10261 474 IARALALNPKVIIADEAVSALDVSiRGQIINLLLDLQRDfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
117-345 |
6.44e-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: 91.02 E-value: 6.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNY--PNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLF-------DGKNAKTLN 187
Cdd:TIGR03269 280 IKVRNVSKRYisVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdewvDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 188 IQWLRAQIGIVSQEPMLF-DCTIAENIAYGDnSRQVPHEEIVNAA---------KEANIHSFIDSLPDkyntrvgdkgtQ 257
Cdd:TIGR03269 360 RGRAKRYIGILHQEYDLYpHRTVLDNLTEAI-GLELPDELARMKAvitlkmvgfDEEKAEEILDKYPD-----------E 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 258 LSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKARE--GRTCIVIAHRLSTIQN-ADKIAVVQNGKVV 334
Cdd:TIGR03269 428 LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIV 507
|
250
....*....|.
gi 1708878085 335 EQGTHQQLLAE 345
Cdd:TIGR03269 508 KIGDPEEIVEE 518
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
117-332 |
6.66e-20 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 84.81 E-value: 6.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLErfydpldGEMlfdgknaktlniqwlraqig 196
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIA-------GEL-------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 ivsqepmlfdctiaeniaygdnsrqVPHEEIVNAAKEANIHSFidslpdkyntrvgdkgTQLSGGQKQRIAIARALVRQP 276
Cdd:cd03221 51 -------------------------EPDEGIVTWGSTVKIGYF----------------EQLSGGEKMRLALAKLLLENP 89
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1708878085 277 QILLLDEATSALDTESEKIVQEALdKAREGrTCIVIAHRLSTIQN-ADKIAVVQNGK 332
Cdd:cd03221 90 NLLLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSHDRYFLDQvATKIIELEDGK 144
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
129-344 |
7.19e-20 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 87.92 E-value: 7.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 129 RPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPmlfdct 208
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDP------ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 209 iaeniAYGDNSRQ-------VP---HEEIVNAAKEANIHSFIDS---LPDKYNTRvgdkGTQLSGGQKQRIAIARALVRQ 275
Cdd:PRK15112 97 -----STSLNPRQrisqildFPlrlNTDLEPEQREKQIIETLRQvglLPDHASYY----PHMLAPGQKQRLGLARALILR 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1708878085 276 PQILLLDEATSALD-TESEKIVQEALD-KAREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQLLA 344
Cdd:PRK15112 168 PKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADVLA 239
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
134-343 |
7.69e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 87.73 E-value: 7.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 134 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPML-FDCTIAEN 212
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNATTpGDITVQEL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 213 IAYGdnsrQVPH-----------EEIVNAAKEAnihsfidslpdkynTRVGDKGTQ----LSGGQKQRIAIARALVRQPQ 277
Cdd:PRK10253 102 VARG----RYPHqplftrwrkedEEAVTKAMQA--------------TGITHLADQsvdtLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1708878085 278 ILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLS-TIQNADKIAVVQNGKVVEQGTHQQLL 343
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLSElnREKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIV 232
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
133-359 |
9.10e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 87.76 E-value: 9.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 133 KILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL----------ERFYDPLDGEMLFDGKNAKtlNIQWLRAQIGIVSQEP 202
Cdd:PRK09984 18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLsglitgdksaGSHIELLGRTVQREGRLAR--DIRKSRANTGYIFQQF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 203 MLFD-CTIAENIAYGDNSRQVPHEEIVNAAKEANIHSFIDSLpdkynTRVG------DKGTQLSGGQKQRIAIARALVRQ 275
Cdd:PRK09984 96 NLVNrLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQAL-----TRVGmvhfahQRVSTLSGGQQQRVAIARALMQQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 276 PQILLLDEATSALDTESEKIVQEALD--KAREGRTCIVIAHRLS-TIQNADKIAVVQNGKVVEQGTHQQLLAEK--GIYY 350
Cdd:PRK09984 171 AKVILADEPIASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQFDNERfdHLYR 250
|
....*....
gi 1708878085 351 SLVNVQSGS 359
Cdd:PRK09984 251 SINRVEENA 259
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
132-337 |
2.39e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.95 E-value: 2.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 132 VKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwLRAQIGI--VSQEPMLF-DCT 208
Cdd:PRK15439 24 VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQLGIylVPQEPLLFpNLS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 209 IAENIAYGDNSRQVPHEEIVNAAKEANIHSFIDSlpdkyntrvgdKGTQLSGGQKQRIAIARALVRQPQILLLDEATSAL 288
Cdd:PRK15439 103 VKENILFGLPKRQASMQKMKQLLAALGCQLDLDS-----------SAGSLEVADRQIVEILRGLMRDSRILILDEPTASL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1708878085 289 D-TESEKI---VQEALDKareGRTCIVIAHRLSTI-QNADKIAVVQNGKVVEQG 337
Cdd:PRK15439 172 TpAETERLfsrIRELLAQ---GVGIVFISHKLPEIrQLADRISVMRDGTIALSG 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
131-348 |
2.59e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 85.70 E-value: 2.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 131 EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKtlniQW-----LRAQIGIVSQEPMLF 205
Cdd:PRK11614 17 KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT----DWqtakiMREAVAIVPEGRRVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 206 D-CTIAENIAYGD--NSRQVPHEEIVNAakeanihsfIDSLPDKYNTRVGDKGTqLSGGQKQRIAIARALVRQPQILLLD 282
Cdd:PRK11614 93 SrMTVEENLAMGGffAERDQFQERIKWV---------YELFPRLHERRIQRAGT-MSGGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1708878085 283 EATSALdteSEKIVQEALDKAR----EGRTCIVIAHRLS-TIQNADKIAVVQNGKVVEQGTHQQLLAEKGI 348
Cdd:PRK11614 163 EPSLGL---APIIIQQIFDTIEqlreQGMTIFLVEQNANqALKLADRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
131-354 |
2.72e-19 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 85.85 E-value: 2.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 131 EVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERF--YDPLDGEMLFDGKNAKTLNIQwLRAQIGI----------- 197
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIflafqypieip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 198 -VSQEPMLfdctiaeNIAYgdNSRQvpheeIVNAAKEANIHSFIDSLPDKYNTrVGDKGTQL--------SGGQKQRIAI 268
Cdd:CHL00131 98 gVSNADFL-------RLAY--NSKR-----KFQGLPELDPLEFLEIINEKLKL-VGMDPSFLsrnvnegfSGGEKKRNEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 269 ARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIV-IAH--RLSTIQNADKIAVVQNGKVVEQGTHQ--QLL 343
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIIlITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElaKEL 242
|
250
....*....|.
gi 1708878085 344 AEKGiyYSLVN 354
Cdd:CHL00131 243 EKKG--YDWLK 251
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
58-357 |
2.77e-19 |
|
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: 89.69 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 58 LVFSAVVFGAMALGQSSSFAPDYAkakTSAAHLFLL------------------FERVPSIDSYSEEGEKPETFGGS--- 116
Cdd:TIGR01257 843 MLLDAALYGLLAWYLDQVFPGDYG---TPLPWYFLLqesywlggegcstreeraLEKTEPLTEEMEDPEHPEGINDSffe 919
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 ---------IMIKDVA--FNYPNRPEVkilQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKT 185
Cdd:TIGR01257 920 relpglvpgVCVKNLVkiFEPSGRPAV---DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET 996
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 186 lNIQWLRAQIGIVSQEPMLFD-CTIAENIAYGDNSRQVPHEEiVNAAKEANIHSfiDSLPDKYNTRVGDkgtqLSGGQKQ 264
Cdd:TIGR01257 997 -NLDAVRQSLGMCPQHNILFHhLTVAEHILFYAQLKGRSWEE-AQLEMEAMLED--TGLHHKRNEEAQD----LSGGMQR 1068
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 265 RIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQL- 342
Cdd:TIGR01257 1069 KLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGTPLFLk 1148
|
330 340
....*....|....*....|
gi 1708878085 343 -LAEKGIYYSLV----NVQS 357
Cdd:TIGR01257 1149 nCFGTGFYLTLVrkmkNIQS 1168
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
134-317 |
3.62e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 85.25 E-value: 3.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 134 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQW---LRAQ-IGIVSQ-EPMLFDCT 208
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQkLGFIYQfHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 209 IAENIAYGDNSRQVPHEEIVNAAKEANIHSFIDSlpdkyntRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSAL 288
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRALEMLAAVGLEH-------RANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176
|
170 180 190
....*....|....*....|....*....|.
gi 1708878085 289 DTESEKIVQEALDK--AREGRTCIVIAHRLS 317
Cdd:PRK11629 177 DARNADSIFQLLGElnRLQGTAFLVVTHDLQ 207
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
130-332 |
3.65e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 88.52 E-value: 3.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 130 PEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAkTLN--IQWLRAQIGIVSQE----PM 203
Cdd:PRK10762 15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEV-TFNgpKSSQEAGIGIIHQElnliPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 204 LfdcTIAENIAYGdnsrqvphEEIVNAAKEAN---IHSFIDSLPDKYN------TRVGDkgtqLSGGQKQRIAIARALVR 274
Cdd:PRK10762 94 L---TIAENIFLG--------REFVNRFGRIDwkkMYAEADKLLARLNlrfssdKLVGE----LSIGEQQMVEIAKVLSF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1708878085 275 QPQILLLDEATSAL-DTESE---KIVQEALDkarEGRTCIVIAHRLSTI-QNADKIAVVQNGK 332
Cdd:PRK10762 159 ESKVIIMDEPTDALtDTETEslfRVIRELKS---QGRGIVYISHRLKEIfEICDDVTVFRDGQ 218
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
132-344 |
5.91e-19 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 87.94 E-value: 5.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 132 VKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERF--YDPLDGEML----------------FDGKNAK----TLNIQ 189
Cdd:TIGR03269 13 KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsKVGEPCPvcggTLEPE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 190 ----W---------LRAQIGIVSQEPMLF--DCTIAENIAYGDNSRQVPHEEIVNAAKEanihsFIDSLpdKYNTRVGDK 254
Cdd:TIGR03269 93 evdfWnlsdklrrrIRKRIAIMLQRTFALygDDTVLDNVLEALEEIGYEGKEAVGRAVD-----LIEMV--QLSHRITHI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 255 GTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKA--REGRTCIVIAHRLSTIQN-ADKIAVVQNG 331
Cdd:TIGR03269 166 ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvkASGISMVLTSHWPEVIEDlSDKAIWLENG 245
|
250
....*....|...
gi 1708878085 332 KVVEQGTHQQLLA 344
Cdd:TIGR03269 246 EIKEEGTPDEVVA 258
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
117-349 |
1.39e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 83.98 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIG 196
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 IVSQEPML-FDCTIAENIAYGdnsrQVPH---------EEIVNAAkeanIHSF-IDSLPDKYNTrvgdkgtQLSGGQKQR 265
Cdd:COG4604 79 ILRQENHInSRLTVRELVAFG----RFPYskgrltaedREIIDEA----IAYLdLEDLADRYLD-------ELSGGQRQR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 266 IAIARALVRQPQILLLDEATSALD----TESEKIVQEAldkARE-GRTCIVIAHRLstiqN-----ADKIAVVQNGKVVE 335
Cdd:COG4604 144 AFIAMVLAQDTDYVLLDEPLNNLDmkhsVQMMKLLRRL---ADElGKTVVIVLHDI----NfascyADHIVAMKDGRVVA 216
|
250
....*....|....*..
gi 1708878085 336 QGTHQQLLAE---KGIY 349
Cdd:COG4604 217 QGTPEEIITPevlSDIY 233
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
135-333 |
1.92e-18 |
|
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: 82.09 E-value: 1.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 135 LQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNI-QWLRAQIGIVSQEPM---LF-DCTI 209
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIAYVPEDRKregLVlDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 210 AENIAygdnsrqvpheeivnaakeanihsfidsLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPQILLLDEATSALD 289
Cdd:cd03215 96 AENIA----------------------------LSS-----------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1708878085 290 TES-EKIVQEALDKAREGRTCIVIahrlST-----IQNADKIAVVQNGKV 333
Cdd:cd03215 137 VGAkAEIYRLIRELADAGKAVLLI----SSeldelLGLCDRILVMYEGRI 182
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
103-335 |
3.12e-18 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 85.79 E-value: 3.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 103 YSEEGEKPETFGG--SIMIKDVAFNYPNRP-EVKilqGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFD 179
Cdd:PRK10522 307 YKAEFPRPQAFPDwqTLELRNVTFAYQDNGfSVG---PINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLD 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 180 GKNAKTLNIQWLRAQIGIVSQEPMLFDCTIaeniayGDNSRQvpheeivnaAKEANIHSFIDSLPDKYNTRVGD---KGT 256
Cdd:PRK10522 384 GKPVTAEQPEDYRKLFSAVFTDFHLFDQLL------GPEGKP---------ANPALVEKWLERLKMAHKLELEDgriSNL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 257 QLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIV-QEALDKARE-GRTCIVIAHRLSTIQNADKIAVVQNGKVV 334
Cdd:PRK10522 449 KLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLS 528
|
.
gi 1708878085 335 E 335
Cdd:PRK10522 529 E 529
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
124-337 |
5.21e-18 |
|
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: 81.81 E-value: 5.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 124 FNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKnaktlnIQW-LRAQIGIvsqEP 202
Cdd:cd03220 27 GRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR------VSSlLGLGGGF---NP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 203 MLfdcTIAENI-----AYGdnsrqVPHEEIvnAAKEANIHSFIDsLPDKYNTRVGdkgtQLSGGQKQRIAIARALVRQPQ 277
Cdd:cd03220 98 EL---TGRENIylngrLLG-----LSRKEI--DEKIDEIIEFSE-LGDFIDLPVK----TYSSGMKARLAFAIATALEPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1708878085 278 ILLLDEATSALDTE-SEKIVQEALDKAREGRTCIVIAHRLSTI-QNADKIAVVQNGKVVEQG 337
Cdd:cd03220 163 ILLIDEVLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIkRLCDRALVLEKGKIRFDG 224
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
2-90 |
8.01e-18 |
|
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1 (ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.
Pssm-ID: 350021 [Multi-domain] Cd Length: 300 Bit Score: 82.91 E-value: 8.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 2 YREHLHVPYRNSVKKAHIFGFCFALSQAMMFFTYAGCFRFGAYLVVNGHMQYKSVFLVFSAVVFGAMALGQSSSFAPDYA 81
Cdd:cd18577 212 YSKALEKARKAGIKKGLVSGLGLGLLFFIIFAMYALAFWYGSRLVRDGEISPGDVLTVFFAVLIGAFSLGQIAPNLQAFA 291
|
....*....
gi 1708878085 82 KAKTSAAHL 90
Cdd:cd18577 292 KARAAAAKI 300
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
125-338 |
1.05e-17 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 81.28 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 125 NYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKnaktlnIQWLraqIGI-VSQEPM 203
Cdd:COG1134 32 RRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR------VSAL---LELgAGFHPE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 204 LfdcTIAENI-----AYGDNSRQVphEEIVNAAKE-ANIHSFIDsLPDKYntrvgdkgtqLSGGQKQRIAIARALVRQPQ 277
Cdd:COG1134 103 L---TGRENIylngrLLGLSRKEI--DEKFDEIVEfAELGDFID-QPVKT----------YSSGMRARLAFAVATAVDPD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1708878085 278 ILLLDEATSALDTE-SEKIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGT 338
Cdd:COG1134 167 ILLVDEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
129-343 |
1.11e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 84.33 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 129 RPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLErFYDPLDGEMLFDGK-NAKTLNIQWLRAQIGIVSQEPMLF-D 206
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKGVKGSGSVLlNGMPIDAKEMRAISAYVQQDDLFIpT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 207 CTIAENIAYGDN---SRQVPHEEIVNAAKEanihsFID--SLPDKYNTRVGDKGTQ--LSGGQKQRIAIARALVRQPQIL 279
Cdd:TIGR00955 114 LTVREHLMFQAHlrmPRRVTKKEKRERVDE-----VLQalGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1708878085 280 LLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLST--IQNADKIAVVQNGKVVEQGTHQQLL 343
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAV 255
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
121-342 |
1.26e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.14 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 121 DVAFNYpNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGE-----MLFDGKNAKTLNI------- 188
Cdd:PRK10261 19 NIAFMQ-EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLvqcdkMLLRRRSRQVIELseqsaaq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 189 -QWLR-AQIGIVSQEPM-----LFdcTIAENIAYGDNSRQ-VPHEEIVNAAKEanihsFIDS--LPDKyNTRVGDKGTQL 258
Cdd:PRK10261 98 mRHVRgADMAMIFQEPMtslnpVF--TVGEQIAESIRLHQgASREEAMVEAKR-----MLDQvrIPEA-QTILSRYPHQL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 259 SGGQKQRIAIARALVRQPQILLLDEATSALDTESE-------KIVQEALDKAregrtCIVIAHRLSTIQN-ADKIAVVQN 330
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMSMG-----VIFITHDMGVVAEiADRVLVMYQ 244
|
250
....*....|..
gi 1708878085 331 GKVVEQGTHQQL 342
Cdd:PRK10261 245 GEAVETGSVEQI 256
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
137-342 |
6.19e-17 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 79.26 E-value: 6.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 137 GLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLrAQIGIVS--QEPMLF-DCTIAENI 213
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI-ARMGVVRtfQHVRLFrEMTVIENL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 214 --------------------AYgdnsRQVPHEEIVNAAkeanihSFID--SLPDKYNTRVGDkgtqLSGGQKQRIAIARA 271
Cdd:PRK11300 102 lvaqhqqlktglfsgllktpAF----RRAESEALDRAA------TWLErvGLLEHANRQAGN----LAYGQQRRLEIARC 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1708878085 272 LVRQPQILLLDEATSALDTESEKIVQEALDKARE--GRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQL 342
Cdd:PRK11300 168 MVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
134-344 |
7.36e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 80.23 E-value: 7.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 134 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTlNIQWLRAQIGIVSQ----EPmlfDCTI 209
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGVVPQfdnlDP---DFTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 210 AENIA-----YGDNSRQVphEEIVNAAKEanihsfIDSLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQPQILLLDEA 284
Cdd:PRK13537 98 RENLLvfgryFGLSAAAA--RALVPPLLE------FAKLENKADAKVGE----LSGGMKRRLTLARALVNDPDVLVLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1708878085 285 TSALDTESEKIVQEALDK--AReGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQLLA 344
Cdd:PRK13537 166 TTGLDPQARHLMWERLRSllAR-GKTILLTTHFMEEAERlCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
108-343 |
1.19e-16 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 78.68 E-value: 1.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 108 EKPETFGGSIMIKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN 187
Cdd:PRK10575 3 EYTNHSDTTFALRNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 188 IQWLRAQIGIVSQE-PMLFDCTIAENIA------------YGDNSRQVPHEEIVNAAKEANIHSFIDSLpdkyntrvgdk 254
Cdd:PRK10575 80 SKAFARKVAYLPQQlPAAEGMTVRELVAigrypwhgalgrFGAADREKVEEAISLVGLKPLAHRLVDSL----------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 255 gtqlSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAhRLSTIQNA----DKIAVVQN 330
Cdd:PRK10575 149 ----SGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIA-VLHDINMAarycDYLVALRG 223
|
250
....*....|...
gi 1708878085 331 GKVVEQGTHQQLL 343
Cdd:PRK10575 224 GEMIAQGTPAELM 236
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
108-337 |
2.24e-16 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 77.37 E-value: 2.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 108 EKPETFGGSIMikdvAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGknaktlN 187
Cdd:cd03267 14 SKEPGLIGSLK----SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG------L 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 188 IQW-----LRAQIGIV--SQEPMLFDCTIAENIAYGDNSRQVPHEEivnaAKEAnihsfIDSLPDKYN-TRVGDKGT-QL 258
Cdd:cd03267 84 VPWkrrkkFLRRIGVVfgQKTQLWWDLPVIDSFYLLAAIYDLPPAR----FKKR-----LDELSELLDlEELLDTPVrQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 259 SGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAREGR--TCIVIAHRLSTIQN-ADKIAVVQNGKVVE 335
Cdd:cd03267 155 SLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRLLY 234
|
..
gi 1708878085 336 QG 337
Cdd:cd03267 235 DG 236
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
130-337 |
2.27e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.21 E-value: 2.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 130 PEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQwLRAQ--IGIVSQEPMLFD- 206
Cdd:PRK09700 16 GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAAQlgIGIIYQELSVIDe 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 207 CTIAENIAYGDN-SRQVPHEEIVNAAK---EANIHSFIDSLPDKYNTRVGDkgtqLSGGQKQRIAIARALVRQPQILLLD 282
Cdd:PRK09700 95 LTVLENLYIGRHlTKKVCGVNIIDWREmrvRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1708878085 283 EATSAL-DTESEKIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQG 337
Cdd:PRK09700 171 EPTSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
118-334 |
2.52e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 80.06 E-value: 2.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 118 MI-KDVAFNYPNRP--------EVK------ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLerF-YDPLD-GEMLFDG 180
Cdd:COG1129 236 MVgRELEDLFPKRAaapgevvlEVEglsvggVVRDVSFSVRAGEILGIAGLVGAGRTELARAL--FgADPADsGEIRLDG 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 181 KNAKTLNI-QWLRAQIGIVS----QEPMLFDCTIAENIAYGdNSRQVPHEEIVNAAKEANI-HSFIDSLpdkyNTRVGDK 254
Cdd:COG1129 314 KPVRIRSPrDAIRAGIAYVPedrkGEGLVLDLSIRENITLA-SLDRLSRGGLLDRRRERALaEEYIKRL----RIKTPSP 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 255 GT---QLSGGQKQRIAIARALVRQPQILLLDEATSALD--TESE--KIVQEAldkAREGRTCIVIahrlST-----IQNA 322
Cdd:COG1129 389 EQpvgNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDvgAKAEiyRLIREL---AAEGKAVIVI----SSelpelLGLS 461
|
250
....*....|..
gi 1708878085 323 DKIAVVQNGKVV 334
Cdd:COG1129 462 DRILVMREGRIV 473
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
113-343 |
6.26e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 76.50 E-value: 6.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 113 FGGSIMIKDVAFN-YPnrpevkilqglnlkvekGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWL 191
Cdd:PRK11701 16 YGPRKGCRDVSFDlYP-----------------GEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 192 ---------RAQIGIVSQEPM---LFDCTIAENI-----AYGDNSrqvpHEEIVNAAKEANIHSFIDSlpdkynTRVGDK 254
Cdd:PRK11701 79 seaerrrllRTEWGFVHQHPRdglRMQVSAGGNIgerlmAVGARH----YGDIRATAGDWLERVEIDA------ARIDDL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 255 GTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTEsekiVQ-EALDKARE-----GRTCIVIAHRLSTIQN-ADKIAV 327
Cdd:PRK11701 149 PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVS----VQaRLLDLLRGlvrelGLAVVIVTHDLAVARLlAHRLLV 224
|
250
....*....|....*.
gi 1708878085 328 VQNGKVVEQGTHQQLL 343
Cdd:PRK11701 225 MKQGRVVESGLTDQVL 240
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
126-344 |
7.36e-16 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 75.84 E-value: 7.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 126 YPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVvqllerFY------DPLDGEMLFDGKNAKTLNIqWLRAQIGI-- 197
Cdd:COG1137 13 YGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRARLGIgy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 198 VSQEPMLF-DCTIAENIA----YGDNSRQVPHEEIVNAAKEANIHSFIDSlpdkyntrvgdKGTQLSGGQKQRIAIARAL 272
Cdd:COG1137 83 LPQEASIFrKLTVEDNILavleLRKLSKKEREERLEELLEEFGITHLRKS-----------KAYSLSGGERRRVEIARAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 273 VRQPQILLLDEATSALD----TESEKIVQEALDK----------AREgrtciviahrlsTIQNADKIAVVQNGKVVEQGT 338
Cdd:COG1137 152 ATNPKFILLDEPFAGVDpiavADIQKIIRHLKERgigvlitdhnVRE------------TLGICDRAYIISEGKVLAEGT 219
|
....*.
gi 1708878085 339 HQQLLA 344
Cdd:COG1137 220 PEEILN 225
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
130-334 |
7.44e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 78.62 E-value: 7.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 130 PEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGK--NAKTLNiQWLRAQIGIVSQE-PMLFD 206
Cdd:PRK10982 9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeiDFKSSK-EALENGISMVHQElNLVLQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 207 CTIAENIAYGDNSRQ---VPHEEIVNAAKeanihSFIDSLPDKYNTRvgDKGTQLSGGQKQRIAIARALVRQPQILLLDE 283
Cdd:PRK10982 88 RSVMDNMWLGRYPTKgmfVDQDKMYRDTK-----AIFDELDIDIDPR--AKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1708878085 284 ATSALdTESE-----KIVQEALDKareGRTCIVIAHRLSTI-QNADKIAVVQNGKVV 334
Cdd:PRK10982 161 PTSSL-TEKEvnhlfTIIRKLKER---GCGIVYISHKMEEIfQLCDEITILRDGQWI 213
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
129-328 |
1.34e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 74.45 E-value: 1.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 129 RPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPMLFDCT 208
Cdd:cd03231 10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 209 IAENIAY--GDNSRqvphEEIVNAAKEANIHSFIDsLPdkyntrvgdkGTQLSGGQKQRIAIARALVRQPQILLLDEATS 286
Cdd:cd03231 90 VLENLRFwhADHSD----EQVEEALARVGLNGFED-RP----------VAQLSAGQQRRVALARLLLSGRPLWILDEPTT 154
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1708878085 287 ALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKIAVV 328
Cdd:cd03231 155 ALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGAREL 196
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
138-337 |
1.64e-15 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 76.84 E-value: 1.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 138 LNLKVE-----KGQTlALVGSSGCGKSTVVQLLERFYDP------LDGEMLFDgkNAKTLNIQWLRAQIGIVSQEPMLF- 205
Cdd:PRK11144 13 LCLTVNltlpaQGIT-AIFGRSGAGKTSLINAISGLTRPqkgrivLNGRVLFD--AEKGICLPPEKRRIGYVFQDARLFp 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 206 DCTIAENIAYG-DNSRQVPHEEIVNAAKeanihsfIDSLPDKYNTRvgdkgtqLSGGQKQRIAIARALVRQPQILLLDEA 284
Cdd:PRK11144 90 HYKVRGNLRYGmAKSMVAQFDKIVALLG-------IEPLLDRYPGS-------LSGGEKQRVAIGRALLTAPELLLMDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1708878085 285 TSALDTESEKIVQEALDK-AREGRTCIV-IAHRLSTI-QNADKIAVVQNGKVVEQG 337
Cdd:PRK11144 156 LASLDLPRKRELLPYLERlAREINIPILyVSHSLDEIlRLADRVVVLEQGKVKAFG 211
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
129-313 |
1.77e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 74.14 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 129 RPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNiqwLRAQIGIVSQ----EPML 204
Cdd:PRK13539 12 RGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD---VAEACHYLGHrnamKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 205 fdcTIAENIA-----YGDnsrqvpHEEIVNAAKEA-NIHSFIDsLPDKYntrvgdkgtqLSGGQKQRIAIARALVRQPQI 278
Cdd:PRK13539 89 ---TVAENLEfwaafLGG------EELDIAAALEAvGLAPLAH-LPFGY----------LSAGQKRRVALARLLVSNRPI 148
|
170 180 190
....*....|....*....|....*....|....*
gi 1708878085 279 LLLDEATSALDTESEKIVQEALdKAREGRTCIVIA 313
Cdd:PRK13539 149 WILDEPTAALDAAAVALFAELI-RAHLAQGGIVIA 182
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
128-335 |
2.00e-15 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.61 E-value: 2.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 128 NRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLErfydpldGEMLfDGKNAKTLNIQWLraQIGIvsqepmlfDC 207
Cdd:COG2401 39 RVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLA-------GALK-GTPVAGCVDVPDN--QFGR--------EA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 208 TIAENIAYGDNSRQVphEEIVNAAKeanihsfidsLPDKYNTRVgdKGTQLSGGQKQRIAIARALVRQPQILLLDEATSA 287
Cdd:COG2401 101 SLIDAIGRKGDFKDA--VELLNAVG----------LSDAVLWLR--RFKELSTGQKFRFRLALLLAERPKLLVIDEFCSH 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1708878085 288 LDTESEKIVQEALDKA--REGRTCIVIAHR---LSTIQnADKIAVVQNGKVVE 335
Cdd:COG2401 167 LDRQTAKRVARNLQKLarRAGITLVVATHHydvIDDLQ-PDLLIFVGYGGVPE 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
129-313 |
8.65e-15 |
|
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: 72.01 E-value: 8.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 129 RPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPMLFDCT 208
Cdd:TIGR01189 10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 209 IAENIAYgdnsrqvpheeivnaakEANIHSFIDSLPDKYNTRVGDKG------TQLSGGQKQRIAIARALVRQPQILLLD 282
Cdd:TIGR01189 90 ALENLHF-----------------WAAIHGGAQRTIEDALAAVGLTGfedlpaAQLSAGQQRRLALARLWLSRRPLWILD 152
|
170 180 190
....*....|....*....|....*....|.
gi 1708878085 283 EATSALDTESEKIVQEALDkAREGRTCIVIA 313
Cdd:TIGR01189 153 EPTTALDKAGVALLAGLLR-AHLARGGIVLL 182
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
1-335 |
2.03e-14 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 74.06 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 1 MYREHLHVP---YRNSVKKAH-IFGFCFALSQAMMFFTYAGCFrfgaYLVVNGHMQYKSVFLVFSAVV-FGAMALGQSSS 75
Cdd:COG4615 209 FFDEDLQPTaerYRDLRIRADtIFALANNWGNLLFFALIGLIL----FLLPALGWADPAVLSGFVLVLlFLRGPLSQLVG 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 76 FAPDYAKAKTSA---AHLFLLFERVPSIDSYSEEGEKPETFGgSIMIKDVAFNYPNRPEVK--ILQGLNLKVEKGQTLAL 150
Cdd:COG4615 285 ALPTLSRANVALrkiEELELALAAAEPAAADAAAPPAPADFQ-TLELRGVTYRYPGEDGDEgfTLGPIDLTIRRGELVFI 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 151 VGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIGIVSQEPMLFDctiaenIAYGdnsrqvpheeIVNA 230
Cdd:COG4615 364 VGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQLFSAVFSDFHLFD------RLLG----------LDGE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 231 AKEANIHSFIDSL--PDKynTRVGDKG---TQLSGGQKQRIAIARALVRQPQILLLDEATSALDTE-----SEKIVQEaL 300
Cdd:COG4615 428 ADPARARELLERLelDHK--VSVEDGRfstTDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPEfrrvfYTELLPE-L 504
|
330 340 350
....*....|....*....|....*....|....*
gi 1708878085 301 dKAReGRTCIVIAHRLSTIQNADKIAVVQNGKVVE 335
Cdd:COG4615 505 -KAR-GKTVIAISHDDRYFDLADRVLKMDYGKLVE 537
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
119-342 |
3.39e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 72.45 E-value: 3.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKD--VAFNYPNrPEVKILQGLNLKVEKGQTLALVGSSGCGKS-TVVQLLERFYDP--LDGEMLFDGKN-----AKTLNI 188
Cdd:PRK09473 15 VKDlrVTFSTPD-GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREilnlpEKELNK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 189 qwLRA-QIGIVSQEPMlfdCTIAENIAYGDNSRQV--PHEEIVNA-AKEANIHsFIDS--LPDKyNTRVGDKGTQLSGGQ 262
Cdd:PRK09473 94 --LRAeQISMIFQDPM---TSLNPYMRVGEQLMEVlmLHKGMSKAeAFEESVR-MLDAvkMPEA-RKRMKMYPHEFSGGM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 263 KQRIAIARALVRQPQILLLDEATSALD-TESEKIVQEALDKAREGRTCIV-IAHRLSTIQN-ADKIAVVQNGKVVEQGTH 339
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDvTVQAQIMTLLNELKREFNTAIImITHDLGVVAGiCDKVLVMYAGRTMEYGNA 246
|
...
gi 1708878085 340 QQL 342
Cdd:PRK09473 247 RDV 249
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
141-338 |
3.98e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 72.47 E-value: 3.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 141 KVEKGQTLALVGSSGCGKST---VVQLLERFYDPLDGEML-FDGKNAKTLNIQWLR----AQIGIVSQEPM--LFDC--- 207
Cdd:PRK11022 29 SVKQGEVVGIVGESGSGKSVsslAIMGLIDYPGRVMAEKLeFNGQDLQRISEKERRnlvgAEVAMIFQDPMtsLNPCytv 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 208 --TIAENI-AYGDNSRQVPHEEIVNAAKEANIhsfidslPDKyNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEA 284
Cdd:PRK11022 109 gfQIMEAIkVHQGGNKKTRRQRAIDLLNQVGI-------PDP-ASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1708878085 285 TSALD-TESEKIVQEALD-KAREGRTCIVIAHRLSTI-QNADKIAVVQNGKVVEQGT 338
Cdd:PRK11022 181 TTALDvTIQAQIIELLLElQQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGK 237
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
134-347 |
6.13e-14 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 70.59 E-value: 6.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 134 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL--ERFYDPLDGEMLFDGKNAKTLNIQwLRAQIGIVsqepMLFDCTIAe 211
Cdd:PRK09580 16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPE-DRAGEGIF----MAFQYPVE- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 212 niaYGDNSRQVPHEEIVNAAKEA---------NIHSFID------SLPDKYNTRVGDKGtqLSGGQKQRIAIARALVRQP 276
Cdd:PRK09580 90 ---IPGVSNQFFLQTALNAVRSYrgqepldrfDFQDLMEekiallKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEP 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1708878085 277 QILLLDEATSALDTESEKIVQEALDKAREG-RTCIVIAH--RLSTIQNADKIAVVQNGKVVEQGTHQ--QLLAEKG 347
Cdd:PRK09580 165 ELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDFTlvKQLEEQG 240
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
133-334 |
1.62e-13 |
|
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: 68.42 E-value: 1.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 133 KILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL-ERFYDPL-DGEMLFDGK-NAKTLNIQwlraqIGIVSQEPMLFDC-T 208
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAGViTGEILINGRpLDKNFQRS-----TGYVEQQDVHSPNlT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 209 IAENIAYGDNSRQvpheeivnaakeanihsfidslpdkyntrvgdkgtqLSGGQKQRIAIARALVRQPQILLLDEATSAL 288
Cdd:cd03232 96 VREALRFSALLRG------------------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1708878085 289 DTESEKIVQEALDK-AREGRTCIVIAHRLS--TIQNADKIAVVQ-NGKVV 334
Cdd:cd03232 140 DSQAAYNIVRFLKKlADSGQAILCTIHQPSasIFEKFDRLLLLKrGGKTV 189
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
144-320 |
3.08e-13 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 66.63 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 144 KGQTLALVGSSGCGKSTVVQLLERFYDPldgemlfDGKNAKTLNIQWLRAQIGIVSQepmlfdctiaeniaygdnsrqvp 223
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGP-------PGGGVIYIDGEDILEEVLDQLL----------------------- 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 224 heeivnaakeanihsfidslpdkyNTRVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALD-- 301
Cdd:smart00382 51 ------------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElr 106
|
170 180
....*....|....*....|....
gi 1708878085 302 -----KAREGRTCIVIAHRLSTIQ 320
Cdd:smart00382 107 lllllKSEKNLTVILTTNDEKDLG 130
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
120-348 |
3.28e-13 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 68.38 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 120 KDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNI-QWLRAQIGIV 198
Cdd:PRK10895 7 KNLAKAYKGR---RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 199 SQEPMLFD-CTIAENIA-----YGDNSRQVPHEEIVNAAKEANIHSFIDSLpdkyntrvgdkGTQLSGGQKQRIAIARAL 272
Cdd:PRK10895 84 PQEASIFRrLSVYDNLMavlqiRDDLSAEQREDRANELMEEFHIEHLRDSM-----------GQSLSGGERRRVEIARAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 273 VRQPQILLLDEATSALDTES----EKIVQEALDKareGRTCIVIAHRL-STIQNADKIAVVQNGKVVEQGTHQQLLAEKG 347
Cdd:PRK10895 153 AANPKFILLDEPFAGVDPISvidiKRIIEHLRDS---GLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229
|
.
gi 1708878085 348 I 348
Cdd:PRK10895 230 V 230
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
96-317 |
5.53e-13 |
|
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: 70.16 E-value: 5.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 96 RVPSIDSYSEEGEKPETFGGS--IMIKDVAFNYPNRPEV-----KILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLE-- 166
Cdd:TIGR00954 422 RVEEIESGREGGRNSNLVPGRgiVEYQDNGIKFENIPLVtpngdVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGel 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 167 ------RFYDPLDGEMLFdgknaktlniqwlraqigiVSQEPMLFDCTIAENIAYGDNS-----RQVPHEEIVNAAKEAN 235
Cdd:TIGR00954 502 wpvyggRLTKPAKGKLFY-------------------VPQRPYMTLGTLRDQIIYPDSSedmkrRGLSDKDLEQILDNVQ 562
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 236 IHSFIdslpdkynTR------VGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAreGRTC 309
Cdd:TIGR00954 563 LTHIL--------EReggwsaVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITL 632
|
....*...
gi 1708878085 310 IVIAHRLS 317
Cdd:TIGR00954 633 FSVSHRKS 640
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
119-334 |
6.68e-13 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 69.67 E-value: 6.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKDVafNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL--ERfyDPLDGEMLFDGKNAKTLNI-QWLRAQI 195
Cdd:COG3845 260 VENL--SVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPrERRRLGV 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 196 GIVSQEPMLF----DCTIAENIAYGDNSRqvphEEIVNAA--KEANIHSFIDSLPDKYNTRVGDKGT---QLSGGQKQRI 266
Cdd:COG3845 336 AYIPEDRLGRglvpDMSVAENLILGRYRR----PPFSRGGflDRKAIRAFAEELIEEFDVRTPGPDTparSLSGGNQQKV 411
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 267 AIARALVRQPQILLLDEATSALDTES-EKIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVV 334
Cdd:COG3845 412 ILARELSRDPKLLIAAQPTRGLDVGAiEFIHQRLLELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
108-344 |
1.36e-12 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 67.80 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 108 EKPETFGGSImiKDVaFNyPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDG----KNA 183
Cdd:COG4586 15 EKEPGLKGAL--KGL-FR-REYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfKRR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 184 KTLniqwlRAQIGIV----SQepMLFDCTIAENIA-----YGdnsrqVPHEEIvnaakEANIHSFID--SLPDKYNTRVg 252
Cdd:COG4586 91 KEF-----ARRIGVVfgqrSQ--LWWDLPAIDSFRllkaiYR-----IPDAEY-----KKRLDELVEllDLGELLDTPV- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 253 dkgTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLSTIQN-ADKIAVVQ 329
Cdd:COG4586 153 ---RQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVID 229
|
250
....*....|....*
gi 1708878085 330 NGKVVEQGTHQQLLA 344
Cdd:COG4586 230 HGRIIYDGSLEELKE 244
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
134-346 |
2.97e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.67 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 134 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLerfydplDGEMLFD-GKnaktLNIqwlrAQIGIVS---QEP------M 203
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDdGR----IIY----EQDLIVArlqQDPprnvegT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 204 LFDcTIAENIA--------YGDNSRQV---PHEEIVNA-AK-------------EANIHSFIDSL---PDKyntrvgdKG 255
Cdd:PRK11147 83 VYD-FVAEGIEeqaeylkrYHDISHLVetdPSEKNLNElAKlqeqldhhnlwqlENRINEVLAQLgldPDA-------AL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 256 TQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALdKAREGrTCIVIAHRLSTIQN-ADKIAVVQNGKVV 334
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFL-KTFQG-SIIFISHDRSFIRNmATRIVDLDRGKLV 232
|
250
....*....|...
gi 1708878085 335 E-QGTHQQLLAEK 346
Cdd:PRK11147 233 SyPGNYDQYLLEK 245
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
138-345 |
3.81e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.34 E-value: 3.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 138 LNLKVEKGQTLALVGSSGCGKSTvvqLLERFYDPLD--GEMLFDGKNAKTLNIQWLRAQIGIVSQE-PMLFdctiaenia 214
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMAGLLPgsGSIQFAGQPLEAWSAAELARHRAYLSQQqTPPF--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 215 ygdnsrQVP---------HEEIVNAAKEANIHSFIDS--LPDKYNTRVGdkgtQLSGGQKQRIAIARALVR-------QP 276
Cdd:PRK03695 83 ------AMPvfqyltlhqPDKTRTEAVASALNEVAEAlgLDDKLGRSVN----QLSGGEWQRVRLAAVVLQvwpdinpAG 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1708878085 277 QILLLDEATSALDtesekIVQE-ALDK-----AREGRTCIVIAHRLS-TIQNADKIAVVQNGKVVEQGTHQQLLAE 345
Cdd:PRK03695 153 QLLLLDEPMNSLD-----VAQQaALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTP 223
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
117-316 |
4.50e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 65.52 E-value: 4.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKnaktlniqwLRaqIG 196
Cdd:PRK09544 5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 IVSQEPMLfDCTIAENIAYGDNSRQ-VPHEEIVNAAKEANIHSFIDSLPDKyntrvgdkgtqLSGGQKQRIAIARALVRQ 275
Cdd:PRK09544 71 YVPQKLYL-DTTLPLTVNRFLRLRPgTKKEDILPALKRVQAGHLIDAPMQK-----------LSGGETQRVLLARALLNR 138
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1708878085 276 PQILLLDEATSALDTESEKIVQEALDKAREGRTCIV--IAHRL 316
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVlmVSHDL 181
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
109-344 |
1.07e-11 |
|
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: 66.00 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 109 KPETFGGSIM-IKDVAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYD-PLDGEMLFDGKNAKTL 186
Cdd:TIGR02633 249 EPHEIGDVILeARNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIR 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 187 N-IQWLRAQIGIVSQEP----MLFDCTIAENIAYGDNSRQVPHEEIVNAAKEANIHSFIDSLpdKYNTRVGDKG-TQLSG 260
Cdd:TIGR02633 329 NpAQAIRAGIAMVPEDRkrhgIVPILGVGKNITLSVLKSFCFKMRIDAAAELQIIGSAIQRL--KVKTASPFLPiGRLSG 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 261 GQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLSTIQN-ADKIAVVQNGKV----V 334
Cdd:TIGR02633 407 GNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLkgdfV 486
|
250
....*....|.
gi 1708878085 335 EQG-THQQLLA 344
Cdd:TIGR02633 487 NHAlTQEQVLA 497
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
127-292 |
1.47e-11 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 65.34 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 127 PNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTvvqlLERFYDPLDGEmlFDGKNAKTLNIQwlraqIGIVSQEPMLFD 206
Cdd:TIGR03719 16 PKK---EILKDISLSFFPGAKIGVLGLNGAGKST----LLRIMAGVDKD--FNGEARPQPGIK-----VGYLPQEPQLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 207 C-TIAENI-------------------AYGDNS--------RQVPHEEIVNAAKEANIHSFIDSLPDKYNTRVGD-KGTQ 257
Cdd:TIGR03719 82 TkTVRENVeegvaeikdaldrfneisaKYAEPDadfdklaaEQAELQEIIDAADAWDLDSQLEIAMDALRCPPWDaDVTK 161
|
170 180 190
....*....|....*....|....*....|....*
gi 1708878085 258 LSGGQKQRIAIARALVRQPQILLLDEATSALDTES 292
Cdd:TIGR03719 162 LSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES 196
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
116-337 |
2.08e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 63.75 E-value: 2.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 116 SIMIKDVAFNYPNRPEVkiLQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQI 195
Cdd:PRK15056 6 GIVVNDVTVTWRNGHTA--LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 196 GIVSQEPMLFDCTIAENIAYGDNS------RQVPHE-EIVNAAKEAnihsfIDSLPDKYNtRVGdkgtQLSGGQKQRIAI 268
Cdd:PRK15056 84 PQSEEVDWSFPVLVEDVVMMGRYGhmgwlrRAKKRDrQIVTAALAR-----VDMVEFRHR-QIG----ELSGGQKKRVFL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 269 ARALVRQPQILLLDEATSALDTESEKIVQEALDKAR-EGRTCIVIAHRLSTIQNADKIAVVQNGKVVEQG 337
Cdd:PRK15056 154 ARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRdEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASG 223
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
126-337 |
2.55e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 63.18 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 126 YPNRPEVKilqGLNLKVEKGQTLALVGSSGCGKS----TVVQLLERFYDPLDGEMLFDGKnakTLNIQWLRAQ-IGIVSQ 200
Cdd:PRK10418 13 QAAQPLVH---GVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGK---PVAPCALRGRkIATIMQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 201 EPM-LFDC--TIAEN-----IAYGDNSRQVPHEEIVNAAKEANIHSFIDSLPdkyntrvgdkgTQLSGGQKQRIAIARAL 272
Cdd:PRK10418 87 NPRsAFNPlhTMHTHaretcLALGKPADDATLTAALEAVGLENAARVLKLYP-----------FEMSGGMLQRMMIALAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1708878085 273 VRQPQILLLDEATSALDTESEKIVQEALDK--AREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQG 337
Cdd:PRK10418 156 LCEAPFIIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVARlADDVAVMSHGRIVEQG 223
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
131-344 |
3.11e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.52 E-value: 3.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 131 EVKILQGLNLKVEKGQTLALVGSSGCGKSTvvqLLERFYDPLDGEMlFDGK---NAKTLNIQWLRaQIGIVSQEPMLF-D 206
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKST---LLNALAGRIQGNN-FTGTilaNNRKPTKQILK-RTGFVTQDDILYpH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 207 CTIAENIAYGDNSR---QVPHEEIVNAAkEANIHSFidSLPDKYNTRVGDKGTQ-LSGGQKQRIAIARALVRQPQILLLD 282
Cdd:PLN03211 155 LTVRETLVFCSLLRlpkSLTKQEKILVA-ESVISEL--GLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1708878085 283 EATSALD-TESEKIVQEALDKAREGRTCIVIAHRLST--IQNADKIAVVQNGKVVEQGTHQQLLA 344
Cdd:PLN03211 232 EPTSGLDaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
139-345 |
3.61e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 64.27 E-value: 3.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 139 NLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGE----------MLFDgKNAKTLNIQWLRAQIGIVSQEPMLFDCT 208
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshitrLSFE-QLQKLVSDEWQRNNTDMLSPGEDDTGRT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 209 IAENIAYG--DNSRQvphEEIvnaAKEANIHSFIDSlPDKYntrvgdkgtqLSGGQKQRIAIARALVRQPQILLLDEATS 286
Cdd:PRK10938 102 TAEIIQDEvkDPARC---EQL---AQQFGITALLDR-RFKY----------LSTGETRKTLLCQALMSEPDLLILDEPFD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1708878085 287 ALDTESEKIVQEALDK-AREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQLLAE 345
Cdd:PRK10938 165 GLDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ 225
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
126-314 |
7.52e-11 |
|
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: 61.66 E-value: 7.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 126 YPNRPEVKILQGLNLKVEKG-----QTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAkTLNIQWLRA-QIGIVS 199
Cdd:cd03237 1 YTYPTMKKTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKAdYEGTVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 200 QepMLFDCTiaeNIAYGDNSRQVpheEIVNAAKeanihsfIDSLPDKyntRVgdkgTQLSGGQKQRIAIARALVRQPQIL 279
Cdd:cd03237 80 D--LLSSIT---KDFYTHPYFKT---EIAKPLQ-------IEQILDR---EV----PELSGGELQRVAIAACLSKDADIY 137
|
170 180 190
....*....|....*....|....*....|....*..
gi 1708878085 280 LLDEATSALDTESEKIVQEALDKAREG--RTCIVIAH 314
Cdd:cd03237 138 LLDEPSAYLDVEQRLMASKVIRRFAENneKTAFVVEH 174
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
128-333 |
1.58e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.05 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 128 NRPEVkilQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLN-----------IQWLRAQIG 196
Cdd:PRK10982 260 RQPSI---RDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainhgfalVTEERRSTG 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 IVSQEPMLFDCTIAENIAYGDNSRQVPHEEIvnaakEANIHSFIDSLPDK---YNTRVGdkgtQLSGGQKQRIAIARALV 273
Cdd:PRK10982 337 IYAYLDIGFNSLISNIRNYKNKVGLLDNSRM-----KSDTQWVIDSMRVKtpgHRTQIG----SLSGGNQQKVIIGRWLL 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1708878085 274 RQPQILLLDEATSALDTESE-KIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVVQNGKV 333
Cdd:PRK10982 408 TQPEILMLDEPTRGIDVGAKfEIYQLIAELAKKDKGIIIISSEMPELLGiTDRILVMSNGLV 469
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
134-338 |
2.10e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 60.61 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 134 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLE-RFYDP-------LDGEMLFDGKNAKTLNIQWL---RAQIGIVSQEP 202
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLarlRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 203 MLFdcTIAENIAYGdnsrQVPHEEIVNAA--KEANIHSFIDSLPDKyNTRVGDKGTQLSGGQKQRIAIARAL-------- 272
Cdd:PRK13547 96 FAF--SAREIVLLG----RYPHARRAGALthRDGEIAWQALALAGA-TALVGRDVTTLSGGELARVQFARVLaqlwpphd 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 273 -VRQPQILLLDEATSALD-TESEKIVQEALDKAREGRT-CIVIAHRLS-TIQNADKIAVVQNGKVVEQGT 338
Cdd:PRK13547 169 aAQPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADRIAMLADGAIVAHGA 238
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
138-350 |
2.22e-10 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 62.34 E-value: 2.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 138 LNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTlNIQWLRAQIGIVSQEPMLFDC-TIAENIAYG 216
Cdd:TIGR01257 1958 LCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMGYCPQFDAIDDLlTGREHLYLY 2036
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 217 DNSRQVPHEEIVNAA----KEANIHSFIDSLPDKYntrvgdkgtqlSGGQKQRIAIARALVRQPQILLLDEATSALDTES 292
Cdd:TIGR01257 2037 ARLRGVPAEEIEKVAnwsiQSLGLSLYADRLAGTY-----------SGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQA 2105
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 293 EKIVQEAL-DKAREGRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQLLAEKGIYY 350
Cdd:TIGR01257 2106 RRMLWNTIvSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFGDGY 2165
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
127-333 |
2.51e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.48 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 127 PNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYdP--LDGEMLFDGKNAKTLN-IQWLRAQIGIVSQE-- 201
Cdd:PRK13549 270 PVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAY-PgrWEGEIFIDGKPVKIRNpQQAIAQGIAMVPEDrk 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 202 -----PMLfdcTIAENIAYGDNSRQVPHEEIVNAAKEANIHSFIDSLPDKYNT---RVGdkgtQLSGGQKQRIAIARALV 273
Cdd:PRK13549 349 rdgivPVM---GVGKNITLAALDRFTGGSRIDDAAELKTILESIQRLKVKTASpelAIA----RLSGGNQQKAVLAKCLL 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1708878085 274 RQPQILLLDEATSALDT----ESEKIVQEAldkAREGRTCIVIAHRLSTIQN-ADKIAVVQNGKV 333
Cdd:PRK13549 422 LNPKILILDEPTRGIDVgakyEIYKLINQL---VQQGVAIIVISSELPEVLGlSDRVLVMHEGKL 483
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
124-323 |
2.57e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 59.19 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 124 FNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTlNIQWLRAQIGIVSQE-- 201
Cdd:PRK13540 9 FDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRsg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 202 --PMLfdcTIAENIAYG--DNSRQVPHEEIVNAAKEANIHSFIDSLpdkyntrvgdkgtqLSGGQKQRIAIARALVRQPQ 277
Cdd:PRK13540 85 inPYL---TLRENCLYDihFSPGAVGITELCRLFSLEHLIDYPCGL--------------LSSGQKRQVALLRLWMSKAK 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1708878085 278 ILLLDEATSALDTESEKIVQEALDKAR-EGRTCIVIAHRLSTIQNAD 323
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQEHRaKGGAVLLTSHQDLPLNKAD 194
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
142-314 |
9.87e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.80 E-value: 9.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 142 VEKGQTLALVGSSGCGKSTVVQLLErfydpldGEMLFDGKNAkTLNIQWlraQIGIVSQEPMLFDCTIAENIAYGDNS-R 220
Cdd:PRK10636 24 INPGQKVGLVGKNGCGKSTLLALLK-------NEISADGGSY-TFPGNW---QLAWVNQETPALPQPALEYVIDGDREyR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 221 QVphEEIVNAAKEAN-------IHSFIDSLpDKYNTR---------VGDKGTQL-------SGGQKQRIAIARALVRQPQ 277
Cdd:PRK10636 93 QL--EAQLHDANERNdghaiatIHGKLDAI-DAWTIRsraasllhgLGFSNEQLerpvsdfSGGWRMRLNLAQALICRSD 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 1708878085 278 ILLLDEATSALDTESeKIVQEALDKAREGrTCIVIAH 314
Cdd:PRK10636 170 LLLLDEPTNHLDLDA-VIWLEKWLKSYQG-TLILISH 204
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
234-338 |
1.28e-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: 58.01 E-value: 1.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 234 ANIHSFIDSLPD---KYnTRVGDKGTQLSGGQKQRIAIARALVRQ---PQILLLDEATSALDTESEKIVQEALDKARE-G 306
Cdd:cd03271 144 PKIARKLQTLCDvglGY-IKLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDkG 222
|
90 100 110
....*....|....*....|....*....|....*...
gi 1708878085 307 RTCIVIAHRLSTIQNADKI------AVVQNGKVVEQGT 338
Cdd:cd03271 223 NTVVVIEHNLDVIKCADWIidlgpeGGDGGGQVVASGT 260
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
129-314 |
1.39e-09 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 57.12 E-value: 1.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 129 RPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTL------NIQWLRAQIGIvsqEP 202
Cdd:PRK13538 11 RDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHQPGI---KT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 203 MLfdcTIAENIAYGDNSRQVPHEEIVNAAKEA-NIHSFIDsLPDKyntrvgdkgtQLSGGQKQRIAIARALVRQPQILLL 281
Cdd:PRK13538 88 EL---TALENLRFYQRLHGPGDDEALWEALAQvGLAGFED-VPVR----------QLSAGQQRRVALARLWLTRAPLWIL 153
|
170 180 190
....*....|....*....|....*....|....
gi 1708878085 282 DEATSALDTESEKIVQEALDK-AREGRTCIVIAH 314
Cdd:PRK13538 154 DEPFTAIDKQGVARLEALLAQhAEQGGMVILTTH 187
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
119-343 |
1.72e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 59.15 E-value: 1.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKDVaFNYPNRP------EVKILQG------LNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKnakTL 186
Cdd:PRK11288 242 IGDI-YGYRPRPlgevrlRLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGK---PI 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 187 NIQWLRAQI--GIV------SQEPMLFDCTIAENIAYGDNSRQVPHEEIVNAAKEA-NIHSFIDSLPDKynTRVGD-KGT 256
Cdd:PRK11288 318 DIRSPRDAIraGIMlcpedrKAEGIIPVHSVADNINISARRHHLRAGCLINNRWEAeNADRFIRSLNIK--TPSREqLIM 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 257 QLSGGQKQRIAIARALVRQPQILLLDEATSALD--TESEkIVQEALDKAREGRTCIVIAHRLSTIQN-ADKIAVVQNGKV 333
Cdd:PRK11288 396 NLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDvgAKHE-IYNVIYELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRI 474
|
250
....*....|....*
gi 1708878085 334 V-----EQGTHQQLL 343
Cdd:PRK11288 475 AgelarEQATERQAL 489
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
56-331 |
1.83e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.35 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 56 VFLVFSAVVF-----GAMALGQSSSF----APDYAKAKTSAAHLFLLFERVP---------SIDSYSEEGEKPETFGGSI 117
Cdd:TIGR00956 680 VFFFFVYILLtefnkGAKQKGEILVFrrgsLKRAKKAGETSASNKNDIEAGEvlgstdltdESDDVNDEKDMEKESGEDI 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 118 MI-KDVAFNYPNRPEVK-ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL-ERFYDPL--DGEMLFDGknaKTLNIQWLR 192
Cdd:TIGR00956 760 FHwRNLTYEVKIKKEKRvILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaERVTTGVitGGDRLVNG---RPLDSSFQR 836
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 193 AqIGIVSQEPM-LFDCTIAENIAYGDNSRQ---VPHEEivnaaKEANIHSFIDSLP-DKY-NTRVGDKGTQLSGGQKQRI 266
Cdd:TIGR00956 837 S-IGYVQQQDLhLPTSTVRESLRFSAYLRQpksVSKSE-----KMEYVEEVIKLLEmESYaDAVVGVPGEGLNVEQRKRL 910
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1708878085 267 AIARALVRQPQILL-LDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLSTI--QNADKIAVVQNG 331
Cdd:TIGR00956 911 TIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKlADHGQAILCTIHQPSAIlfEEFDRLLLLQKG 979
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
119-348 |
3.35e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.98 E-value: 3.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEmlfdgknaktlnIQWL-RAQIGI 197
Cdd:PRK15064 322 VENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGT------------VKWSeNANIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 198 VSQEP--------MLFDctiaeniaYGDNSRQVPHEEIVnaakeanIHSFIDSL---PDKYNTRVgdkgTQLSGGQKQRI 266
Cdd:PRK15064 387 YAQDHaydfendlTLFD--------WMSQWRQEGDDEQA-------VRGTLGRLlfsQDDIKKSV----KVLSGGEKGRM 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 267 AIARALVRQPQILLLDEATSALDTESEKIVQEALDKArEGrTCIVIAH-R--LSTIqnADKIAVVQNGKVVE-QGTHQQL 342
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKY-EG-TLIFVSHdRefVSSL--ATRIIEITPDGVVDfSGTYEEY 523
|
....*.
gi 1708878085 343 LAEKGI 348
Cdd:PRK15064 524 LRSQGI 529
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
117-333 |
4.50e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 57.95 E-value: 4.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRPevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLfdgKNAKTlniqwlraQIG 196
Cdd:PLN03073 509 ISFSDASFGYPGGP--LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF---RSAKV--------RMA 575
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 IVSQE----------PMLFdctiaeniaygdNSRQVPheeivnAAKEANIHSFIDSLPDKYNTRVGDKGTqLSGGQKQRI 266
Cdd:PLN03073 576 VFSQHhvdgldlssnPLLY------------MMRCFP------GVPEQKLRAHLGSFGVTGNLALQPMYT-LSGGQKSRV 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1708878085 267 AIARALVRQPQILLLDEATSALDTES-EKIVQEALdkAREGRTCIViAHRLSTIQNA-DKIAVVQNGKV 333
Cdd:PLN03073 637 AFAKITFKKPHILLLDEPSNHLDLDAvEALIQGLV--LFQGGVLMV-SHDEHLISGSvDELWVVSEGKV 702
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
130-292 |
6.39e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.44 E-value: 6.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 130 PEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGE-MLFDGknaktlniqwlrAQIGIVSQEPML-FDC 207
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPG------------IKVGYLPQEPQLdPEK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 208 TIAENI-------------------AYGDNS--------RQVPHEEIVNAAKEANIHSFID------SLPDkyntrvGD- 253
Cdd:PRK11819 86 TVRENVeegvaevkaaldrfneiyaAYAEPDadfdalaaEQGELQEIIDAADAWDLDSQLEiamdalRCPP------WDa 159
|
170 180 190
....*....|....*....|....*....|....*....
gi 1708878085 254 KGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTES 292
Cdd:PRK11819 160 KVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAES 198
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
117-323 |
1.15e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 56.56 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL-----ERFYDPL--------DGEMLFDGKNa 183
Cdd:PRK10938 261 IVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpQGYSNDLtlfgrrrgSGETIWDIKK- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 184 ktlniqwlraQIGIVSQEPML---FDCTIAENIAYG--DN---SRQVPHEEIVNAAKEANIHSFidslpdkyNTRVGDKG 255
Cdd:PRK10938 337 ----------HIGYVSSSLHLdyrVSTSVRNVILSGffDSigiYQAVSDRQQKLAQQWLDILGI--------DKRTADAP 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 256 TQ-LSGGQkQRIA-IARALVRQPQILLLDEATSALDTESEKIVQEALDK-AREGRT--------------CivIAHRLST 318
Cdd:PRK10938 399 FHsLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETqllfvshhaedapaC--ITHRLEF 475
|
....*
gi 1708878085 319 IQNAD 323
Cdd:PRK10938 476 VPDGD 480
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
142-317 |
1.29e-08 |
|
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: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 142 VEKGQTLALVGSSGCGKSTVVQLLE--------RFYDPLDG----------------EMLFDGKNAKTLNIQWlraqigi 197
Cdd:cd03236 23 PREGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDWdeildefrgselqnyfTKLLEGDVKVIVKPQY------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 198 VSQEPMLFDCTIAENIAYGDNSRQVphEEIVNAAKeanihsfIDSLPDKyntrvgdKGTQLSGGQKQRIAIARALVRQPQ 277
Cdd:cd03236 96 VDLIPKAVKGKVGELLKKKDERGKL--DELVDQLE-------LRHVLDR-------NIDQLSGGELQRVAIAAALARDAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1708878085 278 ILLLDEATSALDTESE----KIVQEAldkAREGRTCIVIAHRLS 317
Cdd:cd03236 160 FYFFDEPSSYLDIKQRlnaaRLIREL---AEDDNYVLVVEHDLA 200
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
1-68 |
1.47e-08 |
|
ABC transporter transmembrane region; This family represents a unit of six transmembrane helices. Many members of the ABC transporter family (pfam00005) have two such regions.
Pssm-ID: 459896 [Multi-domain] Cd Length: 274 Bit Score: 54.96 E-value: 1.47e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 1 MYREHLHVPYRNSVKKAHIFGFCFALSQAMMFFTYAGCFRFGAYLVVNGHMQYKS--VFLVFSAVVFGAM 68
Cdd:pfam00664 205 KYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYALALWFGAYLVISGELSVGDlvAFLSLFAQLFGPL 274
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
139-347 |
2.18e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.90 E-value: 2.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 139 NLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGE-MLFdGK--NAKTLNIqwlRAQIGIVSQEPMLF-DCTIAENIA 214
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEaWLF-GQpvDAGDIAT---RRRVGYMSQAFSLYgELTVRQNLE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 215 -----YgdnsrQVPHEEIVNAAKEAnIHSF-----IDSLPDkyntrvgdkgtQLSGGQKQRIAIARALVRQPQILLLDEA 284
Cdd:NF033858 362 lharlF-----HLPAAEIAARVAEM-LERFdladvADALPD-----------SLPLGIRQRLSLAVAVIHKPELLILDEP 424
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1708878085 285 TSALDTESEKIVQEAL-DKAREGRTCIVIA-HRLSTIQNADKIAVVQNGKVVEQGTHQQLLAEKG 347
Cdd:NF033858 425 TSGVDPVARDMFWRLLiELSREDGVTIFIStHFMNEAERCDRISLMHAGRVLASDTPAALVAARG 489
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
231-342 |
2.38e-08 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 55.79 E-value: 2.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 231 AKEANIHSFIDSLPD---KYnTRVGDKGTQLSGGQKQRIAIARALVRQ---PQILLLDEATSALDTESEK----IVQEAL 300
Cdd:TIGR00630 801 EAVPSISRKLQTLCDvglGY-IRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKklleVLQRLV 879
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1708878085 301 DKareGRTCIVIAHRLSTIQNADKI------AVVQNGKVVEQGTHQQL 342
Cdd:TIGR00630 880 DK---GNTVVVIEHNLDVIKTADYIidlgpeGGDGGGTVVASGTPEEV 924
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
129-300 |
2.52e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 53.70 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 129 RPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNiqwlRAQ-IGIVSQEPML-FD 206
Cdd:PRK13543 21 RNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD----RSRfMAYLGHLPGLkAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 207 CTIAENIAY-----GDNSRQVPHEEIVnaakeanihsfIDSLPDKYNTRVgdkgTQLSGGQKQRIAIARALVRQPQILLL 281
Cdd:PRK13543 97 LSTLENLHFlcglhGRRAKQMPGSALA-----------IVGLAGYEDTLV----RQLSAGQKKRLALARLWLSPAPLWLL 161
|
170
....*....|....*....
gi 1708878085 282 DEATSALDTESEKIVQEAL 300
Cdd:PRK13543 162 DEPYANLDLEGITLVNRMI 180
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
132-319 |
2.66e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 132 VKILQGLNLKVE-----KGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDgknaktLNI----QWLRAQigivsqep 202
Cdd:PRK13409 347 TKKLGDFSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------LKIsykpQYIKPD-------- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 203 mlFDCTIAENI-----AYGDNSRQvphEEIVnaaKEANIHSFIDSlpdkyntRVGDkgtqLSGGQKQRIAIARALVRQPQ 277
Cdd:PRK13409 413 --YDGTVEDLLrsitdDLGSSYYK---SEII---KPLQLERLLDK-------NVKD----LSGGELQRVAIAACLSRDAD 473
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1708878085 278 ILLLDEATSALDTESEKIVQEALDKAREGR--TCIVIAHRLSTI 319
Cdd:PRK13409 474 LYLLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMI 517
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
152-322 |
3.57e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 52.95 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 152 GSSGCGKSTVVQLLERFYDPLDGEMLFdgKNAKTLNIQ-----WLRAQIGIVSqepmlfDCTIAENIAYgdnsrqvpHEE 226
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYY--KNCNINNIAkpyctYIGHNLGLKL------EMTVFENLKF--------WSE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 227 IVNAAK--EANIHSF-IDSLPDKyntrvgdKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALD-K 302
Cdd:PRK13541 97 IYNSAEtlYAAIHYFkLHDLLDE-------KCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVmK 169
|
170 180
....*....|....*....|
gi 1708878085 303 AREGRTCIVIAHRLSTIQNA 322
Cdd:PRK13541 170 ANSGGIVLLSSHLESSIKSA 189
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
119-301 |
3.85e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKDVAFNYPNRpevKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMlfdgKNAKTLNIQWL---RAQI 195
Cdd:PRK11147 322 MENVNYQIDGK---QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI----HCGTKLEVAYFdqhRAEL 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 196 givsqEPmlfDCTIAENIAYGdnsRQvphEEIVNAaKEANIHSFI-DSL--PDKYNTRVgdkgTQLSGGQKQRIAIARAL 272
Cdd:PRK11147 395 -----DP---EKTVMDNLAEG---KQ---EVMVNG-RPRHVLGYLqDFLfhPKRAMTPV----KALSGGERNRLLLARLF 455
|
170 180
....*....|....*....|....*....
gi 1708878085 273 VRQPQILLLDEATSALDTESEKIVQEALD 301
Cdd:PRK11147 456 LKPSNLLILDEPTNDLDVETLELLEELLD 484
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
121-319 |
1.05e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 53.63 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 121 DVAFNYPNRpeVKILQGLNLKVE-----KGQTLALVGSSGCGKSTVVQLLErfydpldGEMLFD-GKNAKTLNI----QW 190
Cdd:COG1245 339 ETLVEYPDL--TKSYGGFSLEVEggeirEGEVLGIVGPNGIGKTTFAKILA-------GVLKPDeGEVDEDLKIsykpQY 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 191 LRAQIGIVSQEpMLFDcTIAENiaYGDNSRQvphEEIVNAAKeanihsfIDSLPDKYntrVGDkgtqLSGGQKQRIAIAR 270
Cdd:COG1245 410 ISPDYDGTVEE-FLRS-ANTDD--FGSSYYK---TEIIKPLG-------LEKLLDKN---VKD----LSGGELQRVAIAA 468
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1708878085 271 ALVRQPQILLLDEATSALDTESEKIVQEALDKAREGR--TCIVIAHRLSTI 319
Cdd:COG1245 469 CLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRgkTAMVVDHDIYLI 519
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
127-289 |
1.16e-07 |
|
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: 51.49 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 127 PNRPEVKILQGLNLKVEKGQTLALVGSSGCGKST----VVQLLERFYDPlDGEMLFDGKNAKTLNIQWlRAQIGIVSQEp 202
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSV-EGDIHYNGIPYKEFAEKY-PGEIIYVSEE- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 203 mlfdctiaeniaygDNsrQVPH---EEIVNAAKEANIHSFIdslpdkyntrvgdKGtqLSGGQKQRIAIARALVRQPQIL 279
Cdd:cd03233 92 --------------DV--HFPTltvRETLDFALRCKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVL 140
|
170
....*....|
gi 1708878085 280 LLDEATSALD 289
Cdd:cd03233 141 CWDNSTRGLD 150
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
230-337 |
1.47e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 230 AAKEANIHSFIDSLPDKYNTRVGD---KGtqLSGGQKQRIAIARALVRQPQILLLDEATSALDTESekivqeALDKAREG 306
Cdd:TIGR00956 181 AKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSAT------ALEFIRAL 252
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1708878085 307 RTCIVIAHRLSTI------QNA----DKIAVVQNGKVVEQG 337
Cdd:TIGR00956 253 KTSANILDTTPLVaiyqcsQDAyelfDKVIVLYEGYQIYFG 293
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
239-337 |
2.33e-07 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 50.40 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 239 FIDSLPDKYNT-----RVGDKGTQLSGGQKQRIAIARALVRQPQ--ILLLDEATSALDTESEKIVQEALDKAR-EGRTCI 310
Cdd:cd03238 64 FIDQLQFLIDVglgylTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVI 143
|
90 100 110
....*....|....*....|....*....|...
gi 1708878085 311 VIAHRLSTIQNADKI------AVVQNGKVVEQG 337
Cdd:cd03238 144 LIEHNLDVLSSADWIidfgpgSGKSGGKVVFSG 176
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
257-344 |
3.88e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 51.34 E-value: 3.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 257 QLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKARE--GRTCIVIAHRLSTI-QNADKIAVVQNGKV 333
Cdd:PRK15093 158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLsQWADKINVLYCGQT 237
|
90
....*....|.
gi 1708878085 334 VEQGTHQQLLA 344
Cdd:PRK15093 238 VETAPSKELVT 248
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
258-344 |
4.33e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.54 E-value: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 258 LSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAR-EGRTCIVIAHRLSTIQN-ADKIAVVQNGKV-- 333
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKaEGLSIILVSSEMPEVLGmSDRILVMHEGRIsg 475
|
90
....*....|....
gi 1708878085 334 ---VEQGTHQQLLA 344
Cdd:PRK10762 476 eftREQATQEKLMA 489
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
257-318 |
4.59e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.71 E-value: 4.59e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1708878085 257 QLSGGQKQRIAIARALVRQPQILLLDEATSALD----TESEKIVQEAldkAREGRTCIVIAHRLST 318
Cdd:COG1245 212 ELSGGELQRVAIAAALLRDADFYFFDEPSSYLDiyqrLNVARLIREL---AEEGKYVLVVEHDLAI 274
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
132-317 |
9.77e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 51.00 E-value: 9.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 132 VKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLL--ERFYDPLDGEMLFDG--KNAKTL-NIQWLRAQIGIVSQEpmlfd 206
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLagRKTGGYIEGDIRISGfpKKQETFaRISGYCEQNDIHSPQ----- 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 207 CTIAENIAYGDNSR---QVPHEEIVNAAKEANIHSFIDSLPDKYntrVGDKG-TQLSGGQKQRIAIARALVRQPQILLLD 282
Cdd:PLN03140 968 VTVRESLIYSAFLRlpkEVSKEEKMMFVDEVMELVELDNLKDAI---VGLPGvTGLSTEQRKRLTIAVELVANPSIIFMD 1044
|
170 180 190
....*....|....*....|....*....|....*.
gi 1708878085 283 EATSALDTESEKIVQEAL-DKAREGRTCIVIAHRLS 317
Cdd:PLN03140 1045 EPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPS 1080
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
134-333 |
1.17e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.17 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 134 ILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFdgknAKTLniqwlraQIGIVSQEPMLFdctiaeni 213
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL----AKGI-------KLGYFAQHQLEF-------- 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 214 AYGDNSrqvPHEEIVNAAKEANIHSFIDSLP------DKyntrVGDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSA 287
Cdd:PRK10636 388 LRADES---PLQHLARLAPQELEQKLRDYLGgfgfqgDK----VTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNH 460
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1708878085 288 LDTESEKIVQEALDKArEGrTCIVIAHRLSTIQN-ADKIAVVQNGKV 333
Cdd:PRK10636 461 LDLDMRQALTEALIDF-EG-ALVVVSHDRHLLRStTDDLYLVHDGKV 505
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
142-316 |
1.41e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 50.19 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 142 VEKGQTLALVGSSGCGKSTVVQLL---------------------ERF-----YDPLdgEMLFDGKNAKTLNIQWlraqi 195
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILsgelipnlgdyeeepswdevlKRFrgtelQNYF--KKLYNGEIKVVHKPQY----- 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 196 giVSQEPMLFDCTIAENIAYGDNSRQVphEEIVnaaKEANIHSFIDSlpdkyntrvgdKGTQLSGGQKQRIAIARALVRQ 275
Cdd:PRK13409 169 --VDLIPKVFKGKVRELLKKVDERGKL--DEVV---ERLGLENILDR-----------DISELSGGELQRVAIAAALLRD 230
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1708878085 276 PQILLLDEATSALDtesekiVQEALDKAR------EGRTCIVIAHRL 316
Cdd:PRK13409 231 ADFYFFDEPTSYLD------IRQRLNVARlirelaEGKYVLVVEHDL 271
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
257-339 |
2.08e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 47.35 E-value: 2.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 257 QLSGGQKQRIAIARAL----VRQPQILLLDEATSALDTESEKIVQEALDKAR-EGRTCIVIAHRLSTIQNADKIAVVqnG 331
Cdd:cd03227 77 QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLvKGAQVIVITHLPELAELADKLIHI--K 154
|
....*...
gi 1708878085 332 KVVEQGTH 339
Cdd:cd03227 155 KVITGVYK 162
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
256-348 |
3.25e-06 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 48.63 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 256 TQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDK-AREGRTCIVIAHRLSTIQNA-DKIAVVQNGKV 333
Cdd:PRK09700 408 TELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRL 487
|
90
....*....|....*
gi 1708878085 334 VEQGTHQQLLAEKGI 348
Cdd:PRK09700 488 TQILTNRDDMSEEEI 502
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
252-347 |
4.33e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 48.19 E-value: 4.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 252 GDKGTQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESE-KIVQEALDKAREGRTCIVIAHRLSTI-QNADKIAVVQ 329
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRnEVWDEVRSMVRDGATVLLTTQYMEEAeQLAHELTVID 218
|
90
....*....|....*...
gi 1708878085 330 NGKVVEQGTHQQLLAEKG 347
Cdd:NF000106 219 RGRVIADGKVDELKTKVG 236
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
138-333 |
7.80e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 47.74 E-value: 7.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 138 LNLKVEKGQTLALVGSSGCGKStvvQLLERFY---DPLDGEMLFDGKNAKTLNIQwLRAQIGIV-----SQEPMLF-DCT 208
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRT---ELAETLYglrPARGGRIMLNGKEINALSTA-QRLARGLVylpedRQSSGLYlDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 209 IAENI---AYGDNSRqvpheeIVNAAKEANIHsfidslpDKYNTRVGDKGTQ-------LSGGQKQRIAIARALVRQPQI 278
Cdd:PRK15439 358 LAWNVcalTHNRRGF------WIKPARENAVL-------ERYRRALNIKFNHaeqaartLSGGNQQKVLIAKCLEASPQL 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1708878085 279 LLLDEATSALDTESEK-IVQEALDKAREGRTCIVIAHRLSTI-QNADKIAVVQNGKV 333
Cdd:PRK15439 425 LIVDEPTRGVDVSARNdIYQLIRSIAAQNVAVLFISSDLEEIeQMADRVLVMHQGEI 481
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
258-329 |
9.02e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.64 E-value: 9.02e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1708878085 258 LSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKARE--GRTCIVIAHRLSTIQN-ADKIAVVQ 329
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
257-314 |
1.19e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 1.19e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1708878085 257 QLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKAreGRTCIVIAH 314
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKW--PKTFIVVSH 399
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
250-349 |
1.95e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.60 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 250 RVGDKGTQLSGGQKQRIAIARALVRQPQ---ILLLDEATSALDTES----EKIVQEALDKareGRTCIVIAHRLSTIQNA 322
Cdd:PRK00349 823 KLGQPATTLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDirklLEVLHRLVDK---GNTVVVIEHNLDVIKTA 899
|
90 100 110
....*....|....*....|....*....|....
gi 1708878085 323 DKIaV-------VQNGKVVEQGTHQQLLAEKGIY 349
Cdd:PRK00349 900 DWI-IdlgpeggDGGGEIVATGTPEEVAKVEASY 932
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
117-318 |
5.55e-05 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 44.93 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 117 IMIKDVAFNYPNRPevkILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFdGKNAKtlniqwlraqIG 196
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK----------LA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 197 IVSQ--EPMLFDCTIAENIAYGDNSRQVPHEEIvnaAKEANIHSFIDSLPDKyNTRVGdkgtQLSGGQKQRIAIARALVR 274
Cdd:TIGR03719 389 YVDQsrDALDPNKTVWEEISGGLDIIKLGKREI---PSRAYVGRFNFKGSDQ-QKKVG----QLSGGERNRVHLAKTLKS 460
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1708878085 275 QPQILLLDEATSALDTESEKIVQEALDKAreGRTCIVIAH------RLST 318
Cdd:TIGR03719 461 GGNVLLLDEPTNDLDVETLRALEEALLNF--AGCAVVISHdrwfldRIAT 508
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
258-337 |
8.42e-05 |
|
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: 43.40 E-value: 8.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 258 LSGGQKQRIAIARAL------VrqpqILLLDEATSAL-DTESEKIVqEALDKARE-GRTCIVIAHRLSTIQNADKI---- 325
Cdd:cd03270 138 LSGGEAQRIRLATQIgsgltgV----LYVLDEPSIGLhPRDNDRLI-ETLKRLRDlGNTVLVVEHDEDTIRAADHVidig 212
|
90
....*....|....
gi 1708878085 326 --AVVQNGKVVEQG 337
Cdd:cd03270 213 pgAGVHGGEIVAQG 226
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
119-337 |
1.73e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 43.34 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 119 IKDVAFNYPNRPEVKILQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPldgemlfdgkNAKTLNIQWLRAQIGIV 198
Cdd:PRK13545 24 LKDLFFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMP----------NKGTVDIKGSAALIAIS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 199 SQepMLFDCTIAENIA-----YGDNSRQVphEEIVNAAKE-ANIHSFIDSLPDKYntrvgdkgtqlSGGQKQRIAIARAL 272
Cdd:PRK13545 94 SG--LNGQLTGIENIElkglmMGLTKEKI--KEIIPEIIEfADIGKFIYQPVKTY-----------SSGMKSRLGFAISV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 273 VRQPQILLLDEATSALDtesEKIVQEALDKARE----GRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQG 337
Cdd:PRK13545 159 HINPDILVIDEALSVGD---QTFTKKCLDKMNEfkeqGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYG 225
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
256-325 |
1.96e-04 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 43.42 E-value: 1.96e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1708878085 256 TQLSGGQKQRIAIAraLV-----RQPQ-ILLLDEATSALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKI 325
Cdd:pfam02463 1076 DLLSGGEKTLVALA--LIfaiqkYKPApFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLREEMLEKADKL 1149
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
256-349 |
4.85e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.32 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 256 TQLSGGQKQRIAIARALVRQPQ---ILLLDEATSALDTESEKIVQEALDKARE-GRTCIVIAHRLSTIQNADKI------ 325
Cdd:COG0178 825 TTLSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDIRKLLEVLHRLVDkGNTVVVIEHNLDVIKTADWIidlgpe 904
|
90 100
....*....|....*....|....
gi 1708878085 326 AVVQNGKVVEQGTHQQLLAEKGIY 349
Cdd:COG0178 905 GGDGGGEIVAEGTPEEVAKVKASY 928
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
135-345 |
5.92e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.95 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 135 LQGLNLKVEKGQTLALVGSSGCGKSTVVQLLERFYDPLDGEMLFDGKNAKTLNIQWLRAQIgivsqepmlfdcTIAENIA 214
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQL------------TGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 215 YGDNSRQVPHEEIVNAAKE----ANIHSFIDSLPDKYntrvgdkgtqlSGGQKQRIAIARALVRQPQILLLDEATSALDt 290
Cdd:PRK13546 108 FKMLCMGFKRKEIKAMTPKiiefSELGEFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGD- 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 291 esEKIVQEALDKARE----GRTCIVIAHRLSTIQN-ADKIAVVQNGKVVEQGTHQQLLAE 345
Cdd:PRK13546 176 --QTFAQKCLDKIYEfkeqNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
221-346 |
1.18e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 221 QVPHEEI---------VNAAKEANIHSFIDSLPdkyntrVGDKGTQLSGGQKQRIAIARALV---RQPQILLLDEATSAL 288
Cdd:PRK00635 1660 QTPIEEVaetfpflkkIQKPLQALIDNGLGYLP------LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSL 1733
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1708878085 289 DTESEKIVQEALDK-AREGRTCIVIAHRLSTIQNADKIAVV------QNGKVVEQGTHQQLLAEK 346
Cdd:PRK00635 1734 DNQQKSALLVQLRTlVSLGHSVIYIDHDPALLKQADYLIEMgpgsgkTGGKILFSGPPKDISASK 1798
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
258-325 |
1.19e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 1.19e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1708878085 258 LSGGQKQRIAIARAL---VRQPQILLLDEATSALDTES-EKIVQEALDKAREGRTCIVIAHRLSTIQNADKI 325
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYV 881
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
257-347 |
1.39e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.49 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 257 QLSGGQKQRIAIARALVRQPQILLLDEATSALDTES-----EKIvqEALDKAREGRTCIViahrlST--IQNA---DKIA 326
Cdd:NF033858 136 KLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSrrqfwELI--DRIRAERPGMSVLV-----ATayMEEAerfDWLV 208
|
90 100
....*....|....*....|.
gi 1708878085 327 VVQNGKVVEQGTHQQLLAEKG 347
Cdd:NF033858 209 AMDAGRVLATGTPAELLARTG 229
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
142-165 |
2.06e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 39.53 E-value: 2.06e-03
10 20
....*....|....*....|....*
gi 1708878085 142 VEKGQTLALVGSSGCGKSTVV-QLL 165
Cdd:PRK01889 192 LSGGKTVALLGSSGVGKSTLVnALL 216
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
255-346 |
2.35e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.06 E-value: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 255 GTqLSGGQKQRIAIAralvrqPQI---L-----LLDEATSAL---DTesEKIVqEALDKARE-GRTCIVIAHRLSTIQNA 322
Cdd:PRK00349 488 GT-LSGGEAQRIRLA------TQIgsgLtgvlyVLDEPSIGLhqrDN--DRLI-ETLKHLRDlGNTLIVVEHDEDTIRAA 557
|
90 100 110
....*....|....*....|....*....|
gi 1708878085 323 DKI------AVVQNGKVVEQGTHQQLLAEK 346
Cdd:PRK00349 558 DYIvdigpgAGVHGGEVVASGTPEEIMKNP 587
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
258-346 |
2.58e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.00 E-value: 2.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 258 LSGGQKQRIAIARalvrqpQI--------LLLDEATSAL---DTesEKIVqEALDKARE-GRTCIVIAHRLSTIQNADKI 325
Cdd:TIGR00630 489 LSGGEAQRIRLAT------QIgsgltgvlYVLDEPSIGLhqrDN--RRLI-NTLKRLRDlGNTLIVVEHDEDTIRAADYV 559
|
90 100
....*....|....*....|....*..
gi 1708878085 326 ------AVVQNGKVVEQGTHQQLLAEK 346
Cdd:TIGR00630 560 idigpgAGEHGGEVVASGTPEEILANP 586
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
2-83 |
4.02e-03 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This group includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins.
Pssm-ID: 350001 [Multi-domain] Cd Length: 289 Bit Score: 38.70 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 2 YREHLHVPYRNSVKKAHIFGFCFALSQAMMFFTYAGCFRFGAYLVVNGHMqykSV-----FLVFSAVVfgAMALGQSSSF 76
Cdd:cd18557 201 YSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQL---TVgeltsFILYTIMV--ASSVGGLSSL 275
|
....*..
gi 1708878085 77 APDYAKA 83
Cdd:cd18557 276 LADIMKA 282
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
261-314 |
4.50e-03 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 38.72 E-value: 4.50e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1708878085 261 GQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALDKaregRTC--IVIAH 314
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNE----RNStmIIISH 210
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
257-292 |
4.59e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 36.06 E-value: 4.59e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1708878085 257 QLSGGQKQR---IAIARALVRQ----------PQILLLDEATSALDTES 292
Cdd:pfam13558 32 GLSGGEKQLlayLPLAAALAAQygsaegrppaPRLVFLDEAFAKLDEEN 80
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
140-325 |
9.36e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 37.06 E-value: 9.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 140 LKVEKGQTlALVGSSGCGKSTVVQLL-----ERFYDPLDGEMLFD-----GKNAKTLNiqwlRAQIGIVsqepmlFDcti 209
Cdd:cd03278 18 IPFPPGLT-AIVGPNGSGKSNIIDAIrwvlgEQSAKSLRGEKMSDvifagSETRKPAN----FAEVTLT------FD--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 210 aeniaygdNSRQVPheEIVNAAKeanIHSFIDSlPDKYNTRVgdkgTQLSGGQKQRIAIAR--AL--VRQPQILLLDEAT 285
Cdd:cd03278 84 --------NSDGRY--SIISQGD---VSEIIEA-PGKKVQRL----SLLSGGEKALTALALlfAIfrVRPSPFCVLDEVD 145
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1708878085 286 SALDTESEKIVQEALDKAREGRTCIVIAHRLSTIQNADKI 325
Cdd:cd03278 146 AALDDANVERFARLLKEFSKETQFIVITHRKGTMEAADRL 185
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
250-301 |
9.74e-03 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 37.79 E-value: 9.74e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1708878085 250 RVGdkgtQLSGGQKQRIAIARALVRQPQILLLDEATSALDTESEKIVQEALD 301
Cdd:PRK11819 442 KVG----VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALL 489
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
258-346 |
9.89e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.08 E-value: 9.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1708878085 258 LSGGQKQRI----AIARALVrqpQIL-LLDEATSAL---DTesEKIVqEALDKARE-GRTCIVIAHRLSTIQNADKI--- 325
Cdd:COG0178 486 LSGGEAQRIrlatQIGSGLV---GVLyVLDEPSIGLhqrDN--DRLI-ETLKRLRDlGNTVIVVEHDEDTIRAADYIidi 559
|
90 100
....*....|....*....|....
gi 1708878085 326 ---AVVQNGKVVEQGTHQQLLAEK 346
Cdd:COG0178 560 gpgAGEHGGEVVAQGTPEEILKNP 583
|
|
| |
