|
Name |
Accession |
Description |
Interval |
E-value |
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
205-779 |
0e+00 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 612.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 205 KKKQKVNLGRLMTLAKPELCVLFIASVALLASSGSQIAAPYFFGRVIQASMEEG-MSHLNKTIVLLSLIYLAGALAALVR 283
Cdd:COG1132 2 SKSPRKLLRRLLRYLRPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGdLSALLLLLLLLLGLALLRALLSYLQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 284 SWLFTLAGQRLVARIRKQLFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSA 363
Cdd:COG1132 82 RYLLARLAQRVVADLRRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDW 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 364 KLTGVLISVVPIVGIGAQRYGSFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLA 443
Cdd:COG1132 162 RLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 444 LASGFFNGVIGIIGQGAVVLVLWYGGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGASVRMFELMDRI 523
Cdd:COG1132 242 RLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 524 PSI-DLEGGKKLSTVNQVIQFQDVYFAYPsrPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISI 602
Cdd:COG1132 322 PEIpDPPGAVPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILI 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 603 GRTNLAELDLFWLRRKIALVSQEPVLFATTIAANIAYGC-EATQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSG 681
Cdd:COG1132 400 DGVDIRDLTLESLRRQIGVVPQDTFLFSGTIRENIRYGRpDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSG 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 682 GQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHE 761
Cdd:COG1132 480 GQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHE 559
|
570
....*....|....*...
gi 1005434824 762 TLLAKAGVYKKLVLRQLS 779
Cdd:COG1132 560 ELLARGGLYARLYRLQFG 577
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
214-774 |
0e+00 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 547.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 214 RLMTLAKPELCVLFIASVALLASSGSQIAAPYFFGRVIQASMEEGMSH-LNKTIVLLSLIYLAGALAALVRSWLFTLAGQ 292
Cdd:TIGR00958 151 RLLGLSGRDWPWLISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPaLASAIFFMCLLSIASSVSAGLRGGSFNYTMA 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 293 RLVARIRKQLFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISV 372
Cdd:TIGR00958 231 RINLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSPRLTMVTLIN 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 373 VPIVGIGAQRYGSFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGV 452
Cdd:TIGR00958 311 LPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETLQLNKRKALAYAGYLWT 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 453 IGIIGQGAVVLVLWYGGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGASVRMFELMDRIPSIDLEGGK 532
Cdd:TIGR00958 391 TSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFEYLDRKPNIPLTGTL 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 533 KLSTVNQVIQFQDVYFAYPSRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDL 612
Cdd:TIGR00958 471 APLNLEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDH 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 613 FWLRRKIALVSQEPVLFATTIAANIAYGCE-ATQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGGQKQRVAIAR 691
Cdd:TIGR00958 551 HYLHRQVALVGQEPVLFSGSVRENIAYGLTdTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIAR 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 692 ALLMNPDVLLLDEATSALDAESEHFVKEaiDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHETLLAKAGVYK 771
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLMEDQGCYK 708
|
...
gi 1005434824 772 KLV 774
Cdd:TIGR00958 709 HLV 711
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
207-778 |
3.68e-170 |
|
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: 503.46 E-value: 3.68e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 207 KQKVNLGRLMTLAKPELCVLFIASVALLASSGSQIAAPYFFGRVI-QASMEEGMSHLNKTIVLLSLIYLAGALAALVRSW 285
Cdd:TIGR02204 1 KRLRPLAALWPFVRPYRGRVLAALVALLITAAATLSLPYAVRLMIdHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 286 LFTLAGQRLVARIRKQLFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKL 365
Cdd:TIGR02204 81 LVTWLGERVVADIRRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 366 TGVLISVVPIVGIGAQRYGSFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALA 445
Cdd:TIGR02204 161 TSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVEKAYEAARQRIRT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 446 SGFFNGVIGIIGQGAVVLVLWYGGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGASVRMFELMDRIPS 525
Cdd:TIGR02204 241 RALLTAIVIVLVFGAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPD 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 526 IDL-EGGKKLST-VNQVIQFQDVYFAYPSRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIG 603
Cdd:TIGR02204 321 IKApAHPKTLPVpLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLD 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 604 RTNLAELDLFWLRRKIALVSQEPVLFATTIAANIAYG-CEATQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGG 682
Cdd:TIGR02204 401 GVDLRQLDPAELRARMALVPQDPVLFAASVMENIRYGrPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGG 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 683 QKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHET 762
Cdd:TIGR02204 481 QRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAE 560
|
570
....*....|....*.
gi 1005434824 763 LLAKAGVYKKLVLRQL 778
Cdd:TIGR02204 561 LIAKGGLYARLARLQF 576
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
204-778 |
4.15e-148 |
|
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: 451.21 E-value: 4.15e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 204 SKKKQKVNLGRLMTLAKPELCVLFIASVALLASSGSQIAAPYFFGRVI-QASMEEGMSHLNKTIVLLSLIYLAGALAALV 282
Cdd:COG2274 136 KRGEKPFGLRWFLRLLRRYRRLLLQVLLASLLINLLALATPLFTQVVIdRVLPNQDLSTLWVLAIGLLLALLFEGLLRLL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 283 RSWLFTLAGQRLVARIRKQLFASVVEQEVAFFDSNRTGELINRLSsDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLS 362
Cdd:COG2274 216 RSYLLLRLGQRIDLRLSSRFFRHLLRLPLSFFESRSVGDLASRFR-DVESIREFLTGSLLTALLDLLFVLIFLIVLFFYS 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 363 AKLTGVLISVVPIVGIgaqrYGSFVQGLRKRFQDELAAASSTAEEA----IANIRTVRSFSQERKSMNSYDTDIDKSYKS 438
Cdd:COG2274 295 PPLALVVLLLIPLYVL----LGLLFQPRLRRLSREESEASAKRQSLlvetLRGIETIKALGAESRFRRRWENLLAKYLNA 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 439 GAKLALASGFFNGVIGIIGQGAVVLVLWYGGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGASVRMFE 518
Cdd:COG2274 371 RFKLRRLSNLLSTLSGLLQQLATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDD 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 519 LMDRIPSIDLEGGKK-LSTVNQVIQFQDVYFAYPSRpDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKS 597
Cdd:COG2274 451 ILDLPPEREEGRSKLsLPRLKGDIELENVSFRYPGD-SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTS 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 598 GVISIGRTNLAELDLFWLRRKIALVSQEPVLFATTIAANIAYGC-EATQEEIEKAAEQANAHNFIASFEEGYQTQVGERG 676
Cdd:COG2274 530 GRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSGTIRENITLGDpDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGG 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 677 VKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVE 756
Cdd:COG2274 610 SNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVE 689
|
570 580
....*....|....*....|..
gi 1005434824 757 RGTHETLLAKAGVYKKLVLRQL 778
Cdd:COG2274 690 DGTHEELLARKGLYAELVQQQL 711
|
|
| ABC_6TM_AtABCB27_like |
cd18780 |
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ... |
229-516 |
4.68e-141 |
|
Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 and similar proteins; This group includes Arabidopsis ABC transporter B family member 27 (also known as AtABCB27, aluminum tolerance-related ATP-binding cassette transporter, transporter associated with antigen processing-like protein 2, AtTAP2, and ALS1) which may play a role in aluminum resistance. The ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family includes ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection, as well as ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family.
Pssm-ID: 350053 [Multi-domain] Cd Length: 295 Bit Score: 417.81 E-value: 4.68e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 229 ASVALLASSGSQIAAPYFFGRVIQA-------SMEEGMSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQ 301
Cdd:cd18780 1 GTIALLVSSGTNLALPYFFGQVIDAvtnhsgsGGEEALRALNQAVLILLGVVLIGSIATFLRSWLFTLAGERVVARLRKR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 302 LFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAQ 381
Cdd:cd18780 81 LFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLRYLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 382 RYGSFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQGAV 461
Cdd:cd18780 161 IYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1005434824 462 VLVLWYGGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGASVRM 516
Cdd:cd18780 241 VLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
541-777 |
1.32e-134 |
|
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: 399.22 E-value: 1.32e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIA 620
Cdd:cd03249 1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 621 LVSQEPVLFATTIAANIAYGC-EATQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPDV 699
Cdd:cd03249 81 LVSQEPVLFDGTIAENIRYGKpDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 700 LLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHETLLAKAGVYKKLVLRQ 777
Cdd:cd03249 161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
225-789 |
1.43e-128 |
|
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: 397.27 E-value: 1.43e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 225 VLFIASVALLASSGSQIAAPYFFGRVIQasMEEGMSHLNKTIVLLSLIY----LAGALAALVRSWLFTLAGQRLVARIRK 300
Cdd:COG5265 38 ALAALLLLLLAAALALVVPPLLKDAIDA--LLSGAAALLVVPVGLLLAYgllrLLSVLFGELRDALFARVTQRAVRRLAL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 301 QLFASVVEQEVAFFDSNRTGELinrlssdTQVIQNAlTVNVSMLLRY-----------IIQIIGSLAFMFSLSAkltgVL 369
Cdd:COG5265 116 EVFRHLHALSLRFHLERQTGGL-------SRDIERG-TKGIEFLLRFllfnilptlleIALVAGILLVKYDWWF----AL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 370 ISVVPIVGigaqrYGSF---VQGLRKRFQDELAAASSTaeeaiANIR---------TVRSFSQERKSMNSYDTDIDKSYK 437
Cdd:COG5265 184 ITLVTVVL-----YIAFtvvVTEWRTKFRREMNEADSE-----ANTRavdsllnyeTVKYFGNEAREARRYDEALARYER 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 438 SGAKLALASGFFNGVIGIIGQGAVVLVLWYGGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGASVRMF 517
Cdd:COG5265 254 AAVKSQTSLALLNFGQALIIALGLTAMMLMAAQGVVAGTMTVGDFVLVNAYLIQLYIPLNFLGFVYREIRQALADMERMF 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 518 ELMDRIPSI-DLEGGKKLSTVNQVIQFQDVYFAYpsRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPK 596
Cdd:COG5265 334 DLLDQPPEVaDAPDAPPLVVGGGEVRFENVSFGY--DPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVT 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 597 SGVISIGRTNLAELDLFWLRRKIALVSQEPVLFATTIAANIAYGC-EATQEEIEKAAEQANAHNFIASFEEGYQTQVGER 675
Cdd:COG5265 412 SGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRpDASEEEVEAAARAAQIHDFIESLPDGYDTRVGER 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 676 GVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIV 755
Cdd:COG5265 492 GLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIV 571
|
570 580 590
....*....|....*....|....*....|....
gi 1005434824 756 ERGTHETLLAKAGVYKKLVLRQLSVSQHENLSAG 789
Cdd:COG5265 572 ERGTHAELLAQGGLYAQMWARQQEEEEAEEALAA 605
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
214-773 |
2.32e-125 |
|
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: 387.54 E-value: 2.32e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 214 RLMTLAKPELCVLFIASVALL--ASSGSQIAApyffgrVIQASMEEGMSHLNKTIV-----LLSLIYLAGALAALVRSWL 286
Cdd:TIGR02203 4 RLWSYVRPYKAGLVLAGVAMIlvAATESTLAA------LLKPLLDDGFGGRDRSVLwwvplVVIGLAVLRGICSFVSTYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 287 FTLAGQRLVARIRKQLFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLT 366
Cdd:TIGR02203 78 LSWVSNKVVRDIRVRMFEKLLGLPVSFFDRQPTGTLLSRITFDSEQVASAATDAFIVLVRETLTVIGLFIVLLYYSWQLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 367 GVLISVVPIVGIGAQRYGSFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALAS 446
Cdd:TIGR02203 158 LIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 447 GFFNGVIGIIGQGAVVLVLWYGGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGASVRMFELMDRIPSI 526
Cdd:TIGR02203 238 SISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 527 DlEGGKKLSTVNQVIQFQDVYFAYPSRpDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTN 606
Cdd:TIGR02203 318 D-TGTRAIERARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 607 LAELDLFWLRRKIALVSQEPVLFATTIAANIAYG--CEATQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGGQK 684
Cdd:TIGR02203 396 LADYTLASLRRQVALVSQDVVLFNDTIANNIAYGrtEQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 685 QRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHETLL 764
Cdd:TIGR02203 476 QRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELL 555
|
....*....
gi 1005434824 765 AKAGVYKKL 773
Cdd:TIGR02203 556 ARNGLYAQL 564
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
541-773 |
5.94e-116 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 350.76 E-value: 5.94e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPDSdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIA 620
Cdd:cd03251 1 VEFKNVTFRYPGDGPP-VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 621 LVSQEPVLFATTIAANIAYGC-EATQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPDV 699
Cdd:cd03251 80 LVSQDVFLFNDTVAENIAYGRpGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1005434824 700 LLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHETLLAKAGVYKKL 773
Cdd:cd03251 160 LILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
214-768 |
7.80e-116 |
|
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: 362.54 E-value: 7.80e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 214 RLMTLAKPELCVLFIASVALLASSGSQIAAPYFFGRVIQASMEEG--MSHLNKTIVLLSLIYLAGALAALVRSWLFTLAG 291
Cdd:COG4988 7 RLKRLARGARRWLALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGapLSALLPLLGLLLAVLLLRALLAWLRERAAFRAA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 292 QRLVARIRKQLFASVVEQEVAFFDSNRTGELINRLSsdTQViqNALTVNVSmllRYIIQIIGS-------LAFMFSLSAK 364
Cdd:COG4988 87 ARVKRRLRRRLLEKLLALGPAWLRGKSTGELATLLT--EGV--EALDGYFA---RYLPQLFLAalvplliLVAVFPLDWL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 365 ------LTGVLISVVPI-VGIGAQRYgsfvqgLRKRFQdELAAASSTAEEAIANIRTVRSFSQ---ERKSMNSYDTDIDK 434
Cdd:COG4988 160 sglillVTAPLIPLFMIlVGKGAAKA------SRRQWR-ALARLSGHFLDRLRGLTTLKLFGRakaEAERIAEASEDFRK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 435 SYKSGAKLALASGFfngVIGIIGQGAVVLVLWYGG-SLVNKHeldVGILTAFMLytlnVAMAFAF------LSSVYGDFM 507
Cdd:COG4988 233 RTMKVLRVAFLSSA---VLEFFASLSIALVAVYIGfRLLGGS---LTLFAALFV----LLLAPEFflplrdLGSFYHARA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 508 QAVGASVRMFELMDRIPSIDLEGGKKLSTVNQV-IQFQDVYFAYPSRPDsdVLKGMSFELKPGETVALVGPSGGGKSTVI 586
Cdd:COG4988 303 NGIAAAEKIFALLDAPEPAAPAGTAPLPAAGPPsIELEDVSFSYPGGRP--ALDGLSLTIPPGERVALVGPSGAGKSTLL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 587 SLLERFYDPKSGVISIGRTNLAELDLFWLRRKIALVSQEPVLFATTIAANIAYGC-EATQEEIEKAAEQANAHNFIASFE 665
Cdd:COG4988 381 NLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRpDASDEELEAALEAAGLDEFVAALP 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 666 EGYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQ 745
Cdd:COG4988 461 DGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADR 540
|
570 580
....*....|....*....|...
gi 1005434824 746 VLVIDKGHIVERGTHETLLAKAG 768
Cdd:COG4988 541 ILVLDDGRIVEQGTHEELLAKNG 563
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
214-773 |
1.12e-113 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 357.41 E-value: 1.12e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 214 RLMTLAKPELCVLFIASVALLASSGSQIAAPYffgrVIQASMEEGMSHLNKTI------VLLSLIYLAGaLAALVRSWLF 287
Cdd:PRK11176 15 RLWPTIAPFKAGLIVAGVALILNAASDTFMLS----LLKPLLDDGFGKADRSVlkwmplVVIGLMILRG-ITSFISSYCI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 288 TLAGQRLVARIRKQLFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTG 367
Cdd:PRK11176 90 SWVSGKVVMTMRRRLFGHMMGMPVSFFDKQSTGTLLSRITYDSEQVASSSSGALITVVREGASIIGLFIMMFYYSWQLSL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 368 VLISVVPIVGIGAQRYGSFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASG 447
Cdd:PRK11176 170 ILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASS 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 448 FFNGVIGIIGQGAVVLVLwYGGSLVN-KHELDVGILTafMLYTLNVAM--AFAFLSSVYGDFMQAVGASVRMFELMDRIP 524
Cdd:PRK11176 250 ISDPIIQLIASLALAFVL-YAASFPSvMDTLTAGTIT--VVFSSMIALmrPLKSLTNVNAQFQRGMAACQTLFAILDLEQ 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 525 SIDlEGGKKLSTVNQVIQFQDVYFAYPSRpDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGR 604
Cdd:PRK11176 327 EKD-EGKRVIERAKGDIEFRNVTFTYPGK-EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 605 TNLAELDLFWLRRKIALVSQEPVLFATTIAANIAYGCEA--TQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGG 682
Cdd:PRK11176 405 HDLRDYTLASLRNQVALVSQNVHLFNDTIANNIAYARTEqySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGG 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 683 QKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHET 762
Cdd:PRK11176 485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAE 564
|
570
....*....|.
gi 1005434824 763 LLAKAGVYKKL 773
Cdd:PRK11176 565 LLAQNGVYAQL 575
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
541-777 |
1.31e-109 |
|
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: 334.58 E-value: 1.31e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPsrPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIA 620
Cdd:cd03253 1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 621 LVSQEPVLFATTIAANIAYGC-EATQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPDV 699
Cdd:cd03253 79 VVPQDTVLFNDTIGYNIRYGRpDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 700 LLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHETLLAKAGVYKKLVLRQ 777
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
211-773 |
1.14e-104 |
|
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: 333.66 E-value: 1.14e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 211 NLGRLMTLAKPE-----LCVLF-----IASVALLASSGsqiaapYFfgrvIQASMEEGMShLNktivllslIYLAgalAA 280
Cdd:COG4987 2 DLLRLLRLLRPHrgrllLGVLLglltlLAGIGLLALSG------WL----IAAAALAPPI-LN--------LFVP---IV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 281 LVRswLFTLA------GQRLV---------ARIRKQLFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLL 345
Cdd:COG4987 60 GVR--AFAIGrtvfryLERLVshdatlrllADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 346 RYIIQIIGSLAFMFSLSAKLTGVL-------ISVVP-IVGIGAQRYGSFVQGLRKRFQDELAAAsstaeeaIANIRTVRS 417
Cdd:COG4987 138 VALLVILAAVAFLAFFSPALALVLalglllaGLLLPlLAARLGRRAGRRLAAARAALRARLTDL-------LQGAAELAA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 418 FSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQGAVVLVLWYGGSLVNKHELDVGILTAFMLYTLNVAMAFA 497
Cdd:COG4987 211 YGALDRALARLDAAEARLAAAQRRLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 498 FLSSVYGDFMQAVGASVRMFELMDRIPSIDLEGGKKLSTVNQVIQFQDVYFAYPSRPdSDVLKGMSFELKPGETVALVGP 577
Cdd:COG4987 291 PLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEPAPAPGGPSLELEDVSFRYPGAG-RPVLDGLSLTLPPGERVAIVGP 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 578 SGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIALVSQEPVLFATTIAANIAYGC-EATQEEIEKAAEQAN 656
Cdd:COG4987 370 SGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAVVPQRPHLFDTTLRENLRLARpDATDEELWAALERVG 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 657 AHNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHR 736
Cdd:COG4987 450 LGDWLAALPDGLDTWLGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHR 529
|
570 580 590
....*....|....*....|....*....|....*..
gi 1005434824 737 LSTVRNADQVLVIDKGHIVERGTHETLLAKAGVYKKL 773
Cdd:COG4987 530 LAGLERMDRILVLEDGRIVEQGTHEELLAQNGRYRQL 566
|
|
| ABC_6TM_TAP_ABCB8_10_like |
cd18557 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ... |
229-515 |
1.26e-98 |
|
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: 307.95 E-value: 1.26e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 229 ASVALLASSGSQIAAPYFFGRVI-QASMEEGMSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQLFASVV 307
Cdd:cd18557 1 GLLFLLISSAAQLLLPYLIGRLIdTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 308 EQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAQRYGSFV 387
Cdd:cd18557 81 RQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 388 QGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQGAVVLVLWY 467
Cdd:cd18557 161 RKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLARKKALANALFQGITSLLIYLSLLLVLWY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1005434824 468 GGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGASVR 515
Cdd:cd18557 241 GGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASER 288
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
213-774 |
2.15e-97 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 314.98 E-value: 2.15e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 213 GRLMTLAKPELCVLFIASVALLASSGSQIAAPYFFGRVIQAsmeegMSHlNKTIVLLSLIYLAGALAALVRSWLFTLAGQ 292
Cdd:PRK13657 8 ARVLQYLGAEKRLGILLAVANVLLAAATFAEPILFGRIIDA-----ISG-KGDIFPLLAAWAGFGLFNIIAGVLVARHAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 293 RLVARIRKQL----FASVVEQEVAFFDSNRTGELINRL--SSDT------QVIQNALTVNVSMLLRyiiqiigsLAFMFS 360
Cdd:PRK13657 82 RLAHRRRLAVlteyFERIIQLPLAWHSQRGSGRALHTLlrGTDAlfglwlEFMREHLATLVALVVL--------LPLALF 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 361 LSAKLTGVLISVVPIVGIgaqrYGSFVQGLRKRFQDELAAASSTAEE----AIANIRTVRSFSQ---ERKSMNSYDTDID 433
Cdd:PRK13657 154 MNWRLSLVLVVLGIVYTL----ITTLVMRKTKDGQAAVEEHYHDLFAhvsdAIGNVSVVQSYNRieaETQALRDIADNLL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 434 KsyksgAKL------ALASGFfNGVIGIIgqgAVVLVLWYGGSLVNKHELDVGILTAFM-LYTLNVAMAFAFLSSVYGDF 506
Cdd:PRK13657 230 A-----AQMpvlswwALASVL-NRAASTI---TMLAILVLGAALVQKGQLRVGEVVAFVgFATLLIGRLDQVVAFINQVF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 507 MQAvgASVR-MFELMDRIPSI-DLEGGKKLSTVNQVIQFQDVYFAYPSRPDSdvLKGMSFELKPGETVALVGPSGGGKST 584
Cdd:PRK13657 301 MAA--PKLEeFFEVEDAVPDVrDPPGAIDLGRVKGAVEFDDVSFSYDNSRQG--VEDVSFEAKPGQTVAIVGPTGAGKST 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 585 VISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIALVSQEPVLFATTIAANIAYGCE-ATQEEIEKAAEQANAHNFIAS 663
Cdd:PRK13657 377 LINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGRPdATDEEMRAAAERAQAHDFIER 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 664 FEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNA 743
Cdd:PRK13657 457 KPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNA 536
|
570 580 590
....*....|....*....|....*....|.
gi 1005434824 744 DQVLVIDKGHIVERGTHETLLAKAGVYKKLV 774
Cdd:PRK13657 537 DRILVFDNGRVVESGSFDELVARGGRFAALL 567
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
541-768 |
3.06e-95 |
|
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: 296.83 E-value: 3.06e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYpsRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIA 620
Cdd:cd03254 3 IEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 621 LVSQEPVLFATTIAANIAYG-CEATQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPDV 699
Cdd:cd03254 81 VVLQDTFLFSGTIMENIRLGrPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005434824 700 LLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHETLLAKAG 768
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| ABC_6TM_ABCB10_like |
cd18573 |
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ... |
229-515 |
2.18e-93 |
|
Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, member 10) and similar proteins; This group includes the 6-TM subunit of the ABC10 (also known as ABC mitochondrial erythroid, ABC-me, mABC2, or ABCBA), which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. In mammals, ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane.
Pssm-ID: 350017 [Multi-domain] Cd Length: 294 Bit Score: 294.42 E-value: 2.18e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 229 ASVALLASSGSQIAAPYFFGRVIQASMEEGMSH------LNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQL 302
Cdd:cd18573 1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIeifglsLKTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 303 FASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAQR 382
Cdd:cd18573 81 FKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 383 YGSFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQGAVV 462
Cdd:cd18573 161 YGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAKKEALASGLFFGSTGFSGNLSLL 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1005434824 463 LVLWYGGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGASVR 515
Cdd:cd18573 241 SVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSR 293
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
536-754 |
1.40e-92 |
|
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: 289.76 E-value: 1.40e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 536 TVNQVIQFQDVYFAYPSRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWL 615
Cdd:cd03248 7 HLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 616 RRKIALVSQEPVLFATTIAANIAYGC-EATQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALL 694
Cdd:cd03248 87 HSKVSLVGQEPVLFARSLQDNIAYGLqSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 695 MNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHI 754
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
541-777 |
1.59e-85 |
|
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: 271.67 E-value: 1.59e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYpsRPDS-DVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKI 619
Cdd:cd03252 1 ITFEHVRFRY--KPDGpVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 620 ALVSQEPVLFATTIAANIAYGCEA-TQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPD 698
Cdd:cd03252 79 GVVLQENVLFNRSIRDNIALADPGmSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005434824 699 VLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHETLLAKAGVYKKLVLRQ 777
Cdd:cd03252 159 ILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
225-771 |
8.90e-84 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 278.13 E-value: 8.90e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 225 VLFIASVALLassgsQIAAPYFFGRVIQASMEEGMS--HLNKTIVLLSLIYLAGALAALV-RSWLFTlAGQRLVARIRKQ 301
Cdd:PRK10789 1 VALLIIIAML-----QLIPPKVVGIIVDGVTEQHMTtgQILMWIGTMVLIAVVVYLLRYVwRVLLFG-ASYQLAVELRED 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 302 LFASVVEQEVAFFDSNRTGELINRLSSDT-QVIQNA----LTVNVSMLLRYIIQIIGSLafmfSLSAKLTGVLISVVPIV 376
Cdd:PRK10789 75 FYRQLSRQHPEFYLRHRTGDLMARATNDVdRVVFAAgegvLTLVDSLVMGCAVLIVMST----QISWQLTLLALLPMPVM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 377 GIGAQRYGsfvQGLRKRF---QDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVI 453
Cdd:PRK10789 151 AIMIKRYG---DQLHERFklaQAAFSSLNDRTQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDPTI 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 454 gIIGQGAVVLVLWYGGS-LVNKHELDVGILTAFMLY-------TLNVAMAFAFL---SSVYGdfmqavgasvRMFELMDR 522
Cdd:PRK10789 228 -YIAIGMANLLAIGGGSwMVVNGSLTLGQLTSFVMYlglmiwpMLALAWMFNIVergSAAYS----------RIRAMLAE 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 523 IPSIDlEGGKKLSTVNQVIQFQDVYFAYPSRpDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISI 602
Cdd:PRK10789 297 APVVK-DGSEPVPEGRGELDVNIRQFTYPQT-DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRF 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 603 GRTNLAELDLFWLRRKIALVSQEPVLFATTIAANIAYGC-EATQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSG 681
Cdd:PRK10789 375 HDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRpDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSG 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 682 GQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHE 761
Cdd:PRK10789 455 GQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHD 534
|
570
....*....|
gi 1005434824 762 TLLAKAGVYK 771
Cdd:PRK10789 535 QLAQQSGWYR 544
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
541-753 |
9.88e-81 |
|
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: 256.16 E-value: 9.88e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPDsDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIA 620
Cdd:cd03228 1 IEFKNVSFSYPGRPK-PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 621 LVSQEPVLFATTIAANIaygceatqeeiekaaeqanahnfiasfeegyqtqvgergvkLSGGQKQRVAIARALLMNPDVL 700
Cdd:cd03228 80 YVPQDPFLFSGTIRENI-----------------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1005434824 701 LLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGH 753
Cdd:cd03228 119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
|
|
| ABC_6TM_TAP |
cd18572 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ... |
229-515 |
6.90e-80 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 258.63 E-value: 6.90e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 229 ASVALLASSGSQIAAPYFFGRVIQASMEEG-MSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQLFASVV 307
Cdd:cd18572 1 AFVFLVVAALSELAIPHYTGAVIDAVVADGsREAFYRAVLLLLLLSVLSGLFSGLRGGCFSYAGTRLVRRLRRDLFRSLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 308 EQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAQRYGSFV 387
Cdd:cd18572 81 RQDIAFFDATKTGELTSRLTSDCQKVSDPLSTNLNVFLRNLVQLVGGLAFMFSLSWRLTLLAFITVPVIALITKVYGRYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 388 QGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQGAVVLVLWY 467
Cdd:cd18572 161 RKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLSVRQALAYAGYVAVNTLLQNGTQVLVLFY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1005434824 468 GGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGASVR 515
Cdd:cd18572 241 GGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEK 288
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
225-749 |
6.07e-77 |
|
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: 258.76 E-value: 6.07e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 225 VLFIASVALLAssgsqiaapYFFGRVIQASmeEGMSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQLFA 304
Cdd:TIGR02857 17 LLIIAQAWLLA---------RVVDGLISAG--EPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRERLLE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 305 SVVEQEVAFFDSNRTGELInrlssdTQVIQ--NALTVNVSmllRYIIQIIGS-------LAFMFSLSAKLTGVLISVVPI 375
Cdd:TIGR02857 86 AVAALGPRWLQGRPSGELA------TLALEgvEALDGYFA---RYLPQLVLAvivplaiLAAVFPQDWISGLILLLTAPL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 376 VGIGAQRYGSFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDtDIDKSYKSGA----KLALASGF--- 448
Cdd:TIGR02857 157 IPIFMILIGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIR-RSSEEYRERTmrvlRIAFLSSAvle 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 449 FNGVIGIigqgAVVLVlWYGGSLVNkheldvGILT-AFMLYTLNVAMAFAF----LSSVYGDFMQAVGASVRMFELMDRI 523
Cdd:TIGR02857 236 LFATLSV----ALVAV-YIGFRLLA------GDLDlATGLFVLLLAPEFYLplrqLGAQYHARADGVAAAEALFAVLDAA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 524 PSIDLEGGKKLSTVNQVIQFQDVYFAYPSRPDsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIG 603
Cdd:TIGR02857 305 PRPLAGKAPVTAAPASSLEFSGVSVAYPGRRP--ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVN 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 604 RTNLAELDLFWLRRKIALVSQEPVLFATTIAANIAYGC-EATQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGG 682
Cdd:TIGR02857 383 GVPLADADADSWRDQIAWVPQHPFLFAGTIAENIRLARpDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGG 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 683 QKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVI 749
Cdd:TIGR02857 463 QAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529
|
|
| chvA |
TIGR01192 |
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ... |
214-776 |
5.12e-73 |
|
glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein in bacteria. It belongs to the larger ABC transporter superfamily with the characteristic ATP binding motif. The In general, this protein is in some ways implicated in osmoregulation and suggested to participate in the export of glucan from the cytoplasm to periplasm. The cyclic beta-1,2-glucan in the bactrerial periplasmic space is suggested to confer the property of high osmolority. It has also been demonstrated that mutants in this loci have lost functions of virulence and motility. It is unclear as to how virulence and osmoadaptaion are related. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 130260 [Multi-domain] Cd Length: 585 Bit Score: 249.81 E-value: 5.12e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 214 RLMTLAKPELCVLFIASVALLASSgsqIAAPYFFGRVIQASMeegmshlNKTIVLLSLIYLAG-ALAALVRSWLFTLAGQ 292
Cdd:TIGR01192 12 SYLNVHKNRVLLIVIANITLAAIT---IAEPILFGRIIDAIS-------SKSDVLPTLALWAGfGVFNTIAYVLVAREAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 293 RLVARIRKQL----FASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGV 368
Cdd:TIGR01192 82 RLAHGRRATLlteaFGRIISMPLSWHQQRGTSNALHTLLRATETLFGLWLEFMRQHLATFVALFLLIPTAFAMDWRLSIV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 369 LIsvvpIVGIGAQRYGSFVQGLRKRFQDELA----AASSTAEEAIANIRTVRSFSQ---ERKSMNSYDTDI-DKSYKSGA 440
Cdd:TIGR01192 162 LM----VLGILYILIAKLVMQRTKNGQAAVEhhyhNVFKHVSDSISNVSVVHSYNRieaETSALKQFTNNLlSAQYPVLD 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 441 KLALASGFfNGVIGIIgqgAVVLVLWYGGSLVNKHELDVGILTAFMLYTlnvAMAFAFLSSVYGDFMQAVGASVRM---F 517
Cdd:TIGR01192 238 WWALASGL-NRMASTI---SMMCILVIGTVLVIKGELSVGEVIAFIGFA---NLLIGRLDQMSGFITQIFEARAKLedfF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 518 ELMDRIPSIDLEG-GKKLSTVNQVIQFQDVYFAYPSrpDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPK 596
Cdd:TIGR01192 311 DLEDSVFQREEPAdAPELPNVKGAVEFRHITFEFAN--SSQGVFDVSFEAKAGQTVAIVGPTGAGKTTLINLLQRVYDPT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 597 SGVISIGRTNLAELDLFWLRRKIALVSQEPVLFATTIAANIAYGCE-ATQEEIEKAAEQANAHNFIASFEEGYQTQVGER 675
Cdd:TIGR01192 389 VGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREgATDEEVYEAAKAAAAHDFILKRSNGYDTLVGER 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 676 GVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIV 755
Cdd:TIGR01192 469 GNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLSTVRNADLVLFLDQGRLI 548
|
570 580
....*....|....*....|.
gi 1005434824 756 ERGTHETLLAKAGVYKKLVLR 776
Cdd:TIGR01192 549 EKGSFQELIQKDGRFYKLLRR 569
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18576 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
229-515 |
1.38e-71 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 236.23 E-value: 1.38e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 229 ASVALLASSGSQIAAPYFFGRVIQASMEEG-MSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQLFASVV 307
Cdd:cd18576 1 GLILLLLSSAIGLVFPLLAGQLIDAALGGGdTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 308 EQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAQRYGSFV 387
Cdd:cd18576 81 RLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 388 QGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQGAVVLVLWY 467
Cdd:cd18576 161 RKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1005434824 468 GGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGASVR 515
Cdd:cd18576 241 GGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASER 288
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
212-789 |
3.69e-70 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 241.93 E-value: 3.69e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 212 LGRLMTLAKPELCVLFIASVALLASSGSQIAAPYFFGRVIQASMEEGmsHLNKTIVL-LSLIYLA-GALAALVRSW---L 286
Cdd:PRK10790 11 LKRLLAYGSPWRKPLGLAVLMLWVAAAAEVSGPLLISYFIDNMVAKG--NLPLGLVAgLAAAYVGlQLLAAGLHYAqslL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 287 FTLAGQRLVARIRKQLFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLT 366
Cdd:PRK10790 89 FNRAAVGVVQQLRTDVMDAALRQPLSAFDTQPVGQLISRVTNDTEVIRDLYVTVVATVLRSAALIGAMLVAMFSLDWRMA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 367 GVLISVVPIVGIGAQRYGSFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQ-----ERKSMNSYdtdidKSYKSGAK 441
Cdd:PRK10790 169 LVAIMIFPAVLVVMVIYQRYSTPIVRRVRAYLADINDGFNEVINGMSVIQQFRQqarfgERMGEASR-----SHYMARMQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 442 LALASGF--------FNGVIgIIGqgavvLVLWYGGSLVNKheLDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGAS 513
Cdd:PRK10790 244 TLRLDGFllrpllslFSALI-LCG-----LLMLFGFSASGT--IEVGVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 514 VRMFELMDR------IPSIDLEGGKklstvnqvIQFQDVYFAYpsRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVIS 587
Cdd:PRK10790 316 ERVFELMDGprqqygNDDRPLQSGR--------IDIDNVSFAY--RDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLAS 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 588 LLERFYDPKSGVISIGRTNLAELDLFWLRRKIALVSQEPVLFATTIAANIAYGCEATQEEIEKAAEQANAHNFIASFEEG 667
Cdd:PRK10790 386 LLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLGRDISEEQVWQALETVQLAELARSLPDG 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 668 YQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVL 747
Cdd:PRK10790 466 LYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTIL 545
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1005434824 748 VIDKGHIVERGTHETLLAKAGVYK-----KLVLRQLSVSQHENLSAG 789
Cdd:PRK10790 546 VLHRGQAVEQGTHQQLLAAQGRYWqmyqlQLAGEELAASVREEESLS 592
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
274-774 |
2.03e-67 |
|
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: 237.15 E-value: 2.03e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 274 LAGALAALVRSWLFTLAGQRLVARIRKQL--------FASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLL 345
Cdd:TIGR03796 197 LLGMGLTALLQGVLTWLQLYYLRRLEIKLavgmsarfLWHILRLPVRFFAQRHAGDIASRVQLNDQVAEFLSGQLATTAL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 346 RyIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAQRYGSFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSM 425
Cdd:TIGR03796 277 D-AVMLVFYALLMLLYDPVLTLIGIAFAAINVLALQLVSRRRVDANRRLQQDAGKLTGVAISGLQSIETLKASGLESDFF 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 426 NSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQGAVVLVLWYGGSLVNKHELDVGILTAFMlytlnvAMAFAFLSSVYGd 505
Cdd:TIGR03796 356 SRWAGYQAKLLNAQQELGVLTQILGVLPTLLTSLNSALILVVGGLRVMEGQLTIGMLVAFQ------SLMSSFLEPVNN- 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 506 fMQAVGASVRMFEL-MDRIPSI--------DLEGGKKLSTVNQV------IQFQDVYFAYpSRPDSDVLKGMSFELKPGE 570
Cdd:TIGR03796 429 -LVGFGGTLQELEGdLNRLDDVlrnpvdplLEEPEGSAATSEPPrrlsgyVELRNITFGY-SPLEPPLIENFSLTLQPGQ 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 571 TVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIALVSQEPVLFATTIAANIA-YGCEATQEEIE 649
Cdd:TIGR03796 507 RVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQDIFLFEGTVRDNLTlWDPTIPDADLV 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 650 KAAEQANAHNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEhfvkEAIDRAMVNR- 728
Cdd:TIGR03796 587 RACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETE----KIIDDNLRRRg 662
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1005434824 729 -TVLVIAHRLSTVRNADQVLVIDKGHIVERGTHETLLAKAGVYKKLV 774
Cdd:TIGR03796 663 cTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAVGGAYARLI 709
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
541-758 |
2.24e-67 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 222.46 E-value: 2.24e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPdSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIA 620
Cdd:cd03245 3 IEFRNVSFSYPNQE-IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 621 LVSQEPVLFATTIAANIAYGC-EATQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPDV 699
Cdd:cd03245 82 YVPQDVTLFYGTLRDNITLGApLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1005434824 700 LLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERG 758
Cdd:cd03245 162 LLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
195-774 |
3.12e-66 |
|
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: 233.86 E-value: 3.12e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 195 ILNTSINAGSKKKQKVNLGRLMTLAKPELCVLFIASVALLASSGSQIAAPYFFGRVIQASMEEGMshlNKTIVLLSL--- 271
Cdd:TIGR01193 127 FISPTPEYKPIKEKENSLLKFIPLITRQKKLIVNIVIAAIIVTLISIAGSYYLQKIIDTYIPHKM---MGTLGIISIgli 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 272 -IYLAGALAALVRSWLFTLAGQRLVARIRKQLFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQ 350
Cdd:TIGR01193 204 iAYIIQQILSYIQIFLLNVLGQRLSIDIILSYIKHLFELPMSFFSTRRTGEIVSRFTDASSIIDALASTILSLFLDMWIL 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 351 IIGSLaFMFSLSAKLTGVLISVVPIVGIGAQrygSFVQGLRKRFQDELAAASSTAEEAIAN---IRTVRSFSQERKSMNS 427
Cdd:TIGR01193 284 VIVGL-FLVRQNMLLFLLSLLSIPVYAVIII---LFKRTFNKLNHDAMQANAVLNSSIIEDlngIETIKSLTSEAERYSK 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 428 YDTDIDKSYKSGAKLALASGFFNGVIGIIGQGAVVLVLWYGGSLVNKHELDVGILTAFmlytlNVAMAFaFLSSVYG--- 504
Cdd:TIGR01193 360 IDSEFGDYLNKSFKYQKADQGQQAIKAVTKLILNVVILWTGAYLVMRGKLTLGQLITF-----NALLSY-FLTPLENiin 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 505 ---DFMQAVGASVRMFELMdRIPSIDLEGGKK--LSTVNQVIQFQDVYFAYPSrpDSDVLKGMSFELKPGETVALVGPSG 579
Cdd:TIGR01193 434 lqpKLQAARVANNRLNEVY-LVDSEFINKKKRteLNNLNGDIVINDVSYSYGY--GSNILSDISLTIKMNSKTTIVGMSG 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 580 GGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIALVSQEPVLFATTIAANIAYGCE--ATQEEIEKAAEQANA 657
Cdd:TIGR01193 511 SGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSGSILENLLLGAKenVSQDEIWAACEIAEI 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 658 HNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIdRAMVNRTVLVIAHRL 737
Cdd:TIGR01193 591 KDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLDTITEKKIVNNL-LNLQDKTIIFVAHRL 669
|
570 580 590
....*....|....*....|....*....|....*..
gi 1005434824 738 STVRNADQVLVIDKGHIVERGTHETLLAKAGVYKKLV 774
Cdd:TIGR01193 670 SVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASLI 706
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
225-778 |
1.17e-65 |
|
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: 231.77 E-value: 1.17e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 225 VLFIASVALLASSGSqIAAPYFFGRVIQASMEEGMSHLnktIVLLSLIYLAGALAALvrswLFTLAGQRLVARIRKQLFA 304
Cdd:TIGR03797 138 LLAILAMGLLGTLLG-MLVPIATGILIGTAIPDADRSL---LVQIALALLAAAVGAA----AFQLAQSLAVLRLETRMDA 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 305 SV--------VEQEVAFFDSNRTGELINRLSSDTQvIQNALT-VNVSMLLRYIIQIIgSLAFMFSLSAKLT--GVLISVV 373
Cdd:TIGR03797 210 SLqaavwdrlLRLPVSFFRQYSTGDLASRAMGISQ-IRRILSgSTLTTLLSGIFALL-NLGLMFYYSWKLAlvAVALALV 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 374 PIVGIGAQ-----RYGSFVQGLRKRFQDELAAASSTaeeaIANIRTV-----------RSFSQERKSMNSYDtdidksyk 437
Cdd:TIGR03797 288 AIAVTLVLgllqvRKERRLLELSGKISGLTVQLING----ISKLRVAgaenrafarwaKLFSRQRKLELSAQ-------- 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 438 sGAKLALASgfFNGVIGIIGQGAVvlvLWYGGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGASVRMF 517
Cdd:TIGR03797 356 -RIENLLTV--FNAVLPVLTSAAL---FAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISILAVIPLWERAK 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 518 ELMDRIPSIDLEGGK--KLSTVnqvIQFQDVYFAYpsRPDSD-VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYD 594
Cdd:TIGR03797 430 PILEALPEVDEAKTDpgKLSGA---IEVDRVTFRY--RPDGPlILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFET 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 595 PKSGVISIGRTNLAELDLFWLRRKIALVSQEPVLFATTIAANIAYGCEATQEEIEKAAEQANAHNFIASFEEGYQTQVGE 674
Cdd:TIGR03797 505 PESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEDIRAMPMGMHTVISE 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 675 RGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRtvLVIAHRLSTVRNADQVLVIDKGHI 754
Cdd:TIGR03797 585 GGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIYVLDAGRV 662
|
570 580
....*....|....*....|....
gi 1005434824 755 VERGTHETLLAKAGVYKKLVLRQL 778
Cdd:TIGR03797 663 VQQGTYDELMAREGLFAQLARRQL 686
|
|
| ABC_6TM_ABCB9_like |
cd18784 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ... |
229-513 |
1.41e-65 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.
Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 220.26 E-value: 1.41e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 229 ASVALLASSGSQIAAPYFFGRVIQA-SMEEGMSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQLFASVV 307
Cdd:cd18784 1 AFFFLLAAAVGEIFIPYYTGQVIDGiVIEKSQDKFSRAIIIMGLLAIASSVAAGIRGGLFTLAMARLNIRIRNLLFRSIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 308 EQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAQRYGSFV 387
Cdd:cd18784 81 SQEIGFFDTVKTGDITSRLTSDTTTMSDTVSLNLNIFLRSLVKAIGVIVFMFKLSWQLSLVTLIGLPLIAIVSKVYGDYY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 388 QGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQGAVVLVLWY 467
Cdd:cd18784 161 KKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKDTYKLKIKEALAYGGYVWSNELTELALTVSTLYY 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1005434824 468 GGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGAS 513
Cdd:cd18784 241 GGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAA 286
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
541-759 |
1.05e-64 |
|
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: 215.44 E-value: 1.05e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYpsRPDSD-VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKI 619
Cdd:cd03244 3 IEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 620 ALVSQEPVLFATTIAANIAYGCEATQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPDV 699
Cdd:cd03244 81 SIIPQDPVLFSGTIRSNLDPFGEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 700 LLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGT 759
Cdd:cd03244 161 LVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
446-777 |
6.50e-63 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 221.62 E-value: 6.50e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 446 SGFFNGVIGIIGQGAVVLVLWYGGSLVNKHELDvGILTAFMLYT--------LNVAMAFAFLSSVygdfmqaVGASVRMF 517
Cdd:PRK11160 244 TGLSQALMILANGLTVVLMLWLAAGGVGGNAQP-GALIALFVFAalaafealMPVAGAFQHLGQV-------IASARRIN 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 518 ELMDRIPSIDLEGGKKLSTVNQVIQFQDVYFAYPSRPDSdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKS 597
Cdd:PRK11160 316 EITEQKPEVTFPTTSTAAADQVSLTLNNVSFTYPDQPQP-VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQ 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 598 GVISIGRTNLAELDLFWLRRKIALVSQEPVLFATTIAANIAYGC-EATQEEIEKAAEQANAHNFIASfEEGYQTQVGERG 676
Cdd:PRK11160 395 GEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAApNASDEALIEVLQQVGLEKLLED-DKGLNAWLGEGG 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 677 VKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVE 756
Cdd:PRK11160 474 RQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIE 553
|
330 340
....*....|....*....|.
gi 1005434824 757 RGTHETLLAKAGVYKKLVLRQ 777
Cdd:PRK11160 554 QGTHQELLAQQGRYYQLKQRL 574
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
293-737 |
7.35e-63 |
|
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: 220.31 E-value: 7.35e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 293 RLVARIRKQLFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNaltvnvsMLLRYIIQIIGSL-------AFMFSLSAKL 365
Cdd:TIGR02868 83 RSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQD-------LYVRVIVPAGVALvvgaaavAAIAVLSVPA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 366 TGVLIS-------VVPIVGIGAQR-YGSFVQGLRKRFQDELAAASSTAEEAIANIRTVRSfsqeRKSMNSYDTDIDKSYK 437
Cdd:TIGR02868 156 ALILAAglllagfVAPLVSLRAARaAEQALARLRGELAAQLTDALDGAAELVASGALPAA----LAQVEEADRELTRAER 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 438 SGAK-LALASGFFNGVIGIigqgAVVLVLWYGGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGASVRM 516
Cdd:TIGR02868 232 RAAAaTALGAALTLLAAGL----AVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERI 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 517 FELMD---RIPSIDLEGGKKLSTVNQVIQFQDVYFAYPsrPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFY 593
Cdd:TIGR02868 308 VEVLDaagPVAEGSAPAAGAVGLGKPTLELRDLSAGYP--GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLL 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 594 DPKSGVISIGRTNLAELDLFWLRRKIALVSQEPVLFATTIAANIAYGC-EATQEEIEKAAEQANAHNFIASFEEGYQTQV 672
Cdd:TIGR02868 386 DPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARpDATDEELWAALERVGLADWLRALPDGLDTVL 465
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005434824 673 GERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRL 737
Cdd:TIGR02868 466 GEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
225-798 |
1.50e-61 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 226.45 E-value: 1.50e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 225 VLFIASVALLASSGSqiaAPYF---FGrVIQASMEEGmSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQ 301
Cdd:PTZ00265 61 LLGVSFVCATISGGT---LPFFvsvFG-VIMKNMNLG-ENVNDIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 302 LFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAQ 381
Cdd:PTZ00265 136 FLKSVFYQDGQFHDNNPGSKLTSDLDFYLEQVNAGIGTKFITIFTYASAFLGLYIWSLFKNARLTLCITCVFPLIYICGV 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 382 RYGSFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTdidkSYKSGAKLALASGFFNGV-IGIIGqgA 460
Cdd:PTZ00265 216 ICNKKVKINKKTSLLYNNNTMSIIEEALVGIRTVVSYCGEKTILKKFNL----SEKLYSKYILKANFMESLhIGMIN--G 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 461 VVLV-----LWYG-----GSLVNKH---ELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGASVRMFELMDRIPSID 527
Cdd:PTZ00265 290 FILAsyafgFWYGtriiiSDLSNQQpnnDFHGGSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 528 L-EGGKKLSTVNQvIQFQDVYFAYPSRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRT- 605
Cdd:PTZ00265 370 NnDDGKKLKDIKK-IQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSh 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 606 NLAELDLFWLRRKIALVSQEPVLFATTIAANIAYG------CEATQEEIEK--AAEQANA-------------------- 657
Cdd:PTZ00265 449 NLKDINLKWWRSKIGVVSQDPLLFSNSIKNNIKYSlyslkdLEALSNYYNEdgNDSQENKnkrnscrakcagdlndmsnt 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 658 ------------------------------HNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATS 707
Cdd:PTZ00265 529 tdsneliemrknyqtikdsevvdvskkvliHDFVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATS 608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 708 ALDAESEHFVKEAID--RAMVNRTVLVIAHRLSTVRNADQVLVI--------------------------------DKG- 752
Cdd:PTZ00265 609 SLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIFVLsnrergstvdvdiigedptkdnkennnknnkdDNNn 688
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1005434824 753 --------------HIVERGTHETLLA-KAGVYKKLVLRQLSVSQHENLSAGDLDPNLLGS 798
Cdd:PTZ00265 689 nnnnnnnkinnagsYIIEQGTHDALMKnKNGIYYTMINNQKVSSKKSSNNDNDKDSDMKSS 749
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
263-774 |
1.65e-61 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 226.45 E-value: 1.65e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 263 NKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQLFASVVEQEVAFFD--SNRTGELINRLSSDTQVIQNALTVN 340
Cdd:PTZ00265 866 NKYSLYILVIAIAMFISETLKNYYNNVIGEKVEKTMKRRLFENILYQEISFFDqdKHAPGLLSAHINRDVHLLKTGLVNN 945
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 341 VSMLLRYIIQIIGS--LAFMFS--LSAKLTGVLISVVPIVGIGAqRYGSFVQGLRKRFQ-----------DELAAA-SST 404
Cdd:PTZ00265 946 IVIFTHFIVLFLVSmvMSFYFCpiVAAVLTGTYFIFMRVFAIRA-RLTANKDVEKKEINqpgtvfaynsdDEIFKDpSFL 1024
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 405 AEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGvigiIGQGAVVLV----LWYGGSLVNKHELDVg 480
Cdd:PTZ00265 1025 IQEAFYNMNTVIIYGLEDYFCNLIEKAIDYSNKGQKRKTLVNSMLWG----FSQSAQLFInsfaYWFGSFLIRRGTILV- 1099
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 481 ilTAFM--LYTLNVAMAFA-FLSSVYGDFMQAVGASVRMFELMDRIPSIDL--EGGKKLSTVNQV---IQFQDVYFAYPS 552
Cdd:PTZ00265 1100 --DDFMksLFTFLFTGSYAgKLMSLKGDSENAKLSFEKYYPLIIRKSNIDVrdNGGIRIKNKNDIkgkIEIMDVNFRYIS 1177
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 553 RPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPK------------------------------------ 596
Cdd:PTZ00265 1178 RPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtndmtneqdyqgdeeqnvgmknvne 1257
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 597 ------------------SGVISIGRTNLAELDLFWLRRKIALVSQEPVLFATTIAANIAYGCE-ATQEEIEKAAEQANA 657
Cdd:PTZ00265 1258 fsltkeggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEdATREDVKRACKFAAI 1337
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 658 HNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAI----DRAmvNRTVLVI 733
Cdd:PTZ00265 1338 DEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvdikDKA--DKTIITI 1415
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 1005434824 734 AHRLSTVRNADQVLVIDK----GHIVE-RGTHETLL-AKAGVYKKLV 774
Cdd:PTZ00265 1416 AHRIASIKRSDKIVVFNNpdrtGSFVQaHGTHEELLsVQDGVYKKYV 1462
|
|
| ABC_6TM_bac_exporter_ABCB8_10_like |
cd18575 |
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ... |
229-515 |
1.52e-60 |
|
Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 206.57 E-value: 1.52e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 229 ASVALLASSGSQIAAPYFFGRVI-QASMEEGMSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQLFASVV 307
Cdd:cd18575 1 ALIALLIAAAATLALGQGLRLLIdQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 308 EQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAQRYGSFV 387
Cdd:cd18575 81 RLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 388 QGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQGAVVLVLWY 467
Cdd:cd18575 161 RRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRARALLTALVIFLVFGAIVFVLWL 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1005434824 468 GGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGASVR 515
Cdd:cd18575 241 GAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQRAAGAAER 288
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
499-773 |
3.12e-60 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 214.71 E-value: 3.12e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 499 LSSVYGDFMQAVGASVRMFELMDrIPSIDLEGGKKLSTVNQVIQFQDVYFAYPSrPDSDVLKG-MSFELKPGETVALVGP 577
Cdd:PRK11174 307 LGTFYHAKAQAVGAAESLVTFLE-TPLAHPQQGEKELASNDPVTIEAEDLEILS-PDGKTLAGpLNFTLPAGQRIALVGP 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 578 SGGGKSTVISLLERFYdPKSGVISIGRTNLAELDLFWLRRKIALVSQEPVLFATTIAANIAYG-CEATQEEIEKAAEQAN 656
Cdd:PRK11174 385 SGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGnPDASDEQLQQALENAW 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 657 AHNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHR 736
Cdd:PRK11174 464 VSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQ 543
|
250 260 270
....*....|....*....|....*....|....*..
gi 1005434824 737 LSTVRNADQVLVIDKGHIVERGTHETLLAKAGVYKKL 773
Cdd:PRK11174 544 LEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATL 580
|
|
| ABC_6TM_LmrA_like |
cd18551 |
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ... |
226-515 |
4.43e-56 |
|
Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar proteins; This group represents the six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA from Lactococcus lactis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349995 [Multi-domain] Cd Length: 289 Bit Score: 194.19 E-value: 4.43e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 226 LFIASVALLASSGSQIAAPYFFGRVIQASMEEGMShlNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQLFAS 305
Cdd:cd18551 1 LILALLLSLLGTAASLAQPLLVKNLIDALSAGGSS--GGLLALLVALFLLQAVLSALSSYLLGRTGERVVLDLRRRLWRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 306 VVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAQRYGS 385
Cdd:cd18551 79 LLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLGR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 386 FVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQGAVVLVL 465
Cdd:cd18551 159 RIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVVL 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1005434824 466 WYGGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGASVR 515
Cdd:cd18551 239 GVGGARVASGALTVGTLVAFLLYLFQLITPLSQLSSFFTQLQKALGALER 288
|
|
| ABC_6TM_Pgp_ABCB1_D1_like |
cd18577 |
Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ... |
226-516 |
1.30e-55 |
|
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: 193.46 E-value: 1.30e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 226 LFIASVALLASSGSQIAAPYFFGRVIQA-----SMEEGMSHLNKTIVLLSLIYLAGALAALVRSWL----FTLAGQRLVA 296
Cdd:cd18577 1 LIIGLLAAIAAGAALPLMTIVFGDLFDAftdfgSGESSPDEFLDDVNKYALYFVYLGIGSFVLSYIqtacWTITGERQAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 297 RIRKQLFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIV 376
Cdd:cd18577 81 RIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPLI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 377 GIGAQRYGSFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGII 456
Cdd:cd18577 161 AIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVSGLGLGLLFFI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1005434824 457 GQGAVVLVLWYGGSLVNKHELDVG-ILTAFMLyTLNVAMAFAFLSSVYGDFMQAVGASVRM 516
Cdd:cd18577 241 IFAMYALAFWYGSRLVRDGEISPGdVLTVFFA-VLIGAFSLGQIAPNLQAFAKARAAAAKI 300
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
265-766 |
1.20e-54 |
|
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: 198.43 E-value: 1.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 265 TIVLLSLI----YLAGALAALVRSWLFTLAGQRLVARIRKQLFASVVEQEVAFFDSNRTGELinrlsSDTQVIQNALTVN 340
Cdd:COG4618 58 TLLMLTLLalglYAVMGLLDAVRSRILVRVGARLDRRLGPRVFDAAFRAALRGGGGAAAQAL-----RDLDTLRQFLTGP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 341 VSM------------LLRYIIQ-IIGSLAfmfslsakLTGVLISVVpiVGIGAQRygsFVQGLRKRFQDELAAASSTAEE 407
Cdd:COG4618 133 GLFalfdlpwapiflAVLFLFHpLLGLLA--------LVGALVLVA--LALLNER---LTRKPLKEANEAAIRANAFAEA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 408 AIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQGAVVLVLWYGGSLVNKHELDVG------I 481
Cdd:COG4618 200 ALRNAEVIEAMGMLPALRRRWQRANARALALQARASDRAGGFSALSKFLRLLLQSAVLGLGAYLVIQGEITPGamiaasI 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 482 LTAFMLYTLNVAMAfaflssVYGDFMQAVGASVRMFELMDRIPsiDLEGGKKLSTVNQVIQFQDVYFAYPSRpDSDVLKG 561
Cdd:COG4618 280 LMGRALAPIEQAIG------GWKQFVSARQAYRRLNELLAAVP--AEPERMPLPRPKGRLSVENLTVVPPGS-KRPILRG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 562 MSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGrtnLAELDLfW----LRRKIALVSQEPVLFATTIAANI 637
Cdd:COG4618 351 VSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLD---GADLSQ-WdreeLGRHIGYLPQDVELFDGTIAENI 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 638 AYGCEATQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFV 717
Cdd:COG4618 427 ARFGDADPEKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAAL 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1005434824 718 KEAIDRA-MVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHETLLAK 766
Cdd:COG4618 507 AAAIRALkARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABC_6TM_Pgp_ABCB1_D2_like |
cd18578 |
Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ... |
216-526 |
5.50e-54 |
|
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: 189.59 E-value: 5.50e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 216 MTLAKPELCVLFIASVALLASSGSQIAAPYFFGRVIQASMEEGMSHLNKTIVLLSLIYLAGALAALV----RSWLFTLAG 291
Cdd:cd18578 1 LKLNKPEWPLLLLGLIGAIIAGAVFPVFAILFSKLISVFSLPDDDELRSEANFWALMFLVLAIVAGIayflQGYLFGIAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 292 QRLVARIRKQLFASVVEQEVAFFD--SNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVL 369
Cdd:cd18578 81 ERLTRRLRKLAFRAILRQDIAWFDdpENSTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 370 ISVVPIVGIGAQRYGSFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFF 449
Cdd:cd18578 161 LATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 450 NGVIGIIGQGAVVLVLWYGGSLVNKHELDVG-ILTAFMLYTL---NVAMAFAFLSsvygDFMQAVGASVRMFELMDRIPS 525
Cdd:cd18578 241 FGLSQSLTFFAYALAFWYGGRLVANGEYTFEqFFIVFMALIFgaqSAGQAFSFAP----DIAKAKAAAARIFRLLDRKPE 316
|
.
gi 1005434824 526 I 526
Cdd:cd18578 317 I 317
|
|
| ABC_6TM_exporters |
cd07346 |
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ... |
226-515 |
5.95e-54 |
|
Six-transmembrane helical domain of the ATP-binding cassette transporters; This family represents a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in this family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349983 [Multi-domain] Cd Length: 292 Bit Score: 188.53 E-value: 5.95e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 226 LFIASVALLASSGSQIAAPYFFGRVI-QASMEEGMSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQLFA 304
Cdd:cd07346 1 LLLALLLLLLATALGLALPLLTKLLIdDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 305 SVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAQRYG 384
Cdd:cd07346 81 HLQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 385 SFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQGAVVLV 464
Cdd:cd07346 161 RRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1005434824 465 LWYGGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGASVR 515
Cdd:cd07346 241 LLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLER 291
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
541-767 |
1.90e-52 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 182.15 E-value: 1.90e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPsrPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIA 620
Cdd:COG1122 1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 621 LVSQEPV--LFATTIAANIAYGCEA---TQEEIEKAAEQAnahnfIASFE-EGYQtqvgERGV-KLSGGQKQRVAIARAL 693
Cdd:COG1122 79 LVFQNPDdqLFAPTVEEDVAFGPENlglPREEIRERVEEA-----LELVGlEHLA----DRPPhELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1005434824 694 LMNPDVLLLDEATSALDAESEHFVKEAIDR-AMVNRTVLVIAHRLSTV-RNADQVLVIDKGHIVERGTHETLLAKA 767
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
223-770 |
3.50e-52 |
|
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: 197.86 E-value: 3.50e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 223 LCVLFIASVALLASSGSQIAAPYFFGRVIQASMEEGMShlNKTIVLLSLIYLAGAL---AALVRSWLFTLAGQRLVARIR 299
Cdd:TIGR00957 964 LFITFLSIFLFVCNHVSALASNYWLSLWTDDPMVNGTQ--NNTSLRLSVYGALGILqgfAVFGYSMAVSIGGIQASRVLH 1041
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 300 KQLFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFsLSAKLTGVLISVVPIVGIG 379
Cdd:TIGR00957 1042 QDLLHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVIL-LATPIAAVIIPPLGLLYFF 1120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 380 AQRYGSFVQGLRKRFQD-ELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQ 458
Cdd:TIGR00957 1121 VQRFYVASSRQLKRLESvSRSPVYSHFNETLLGVSVIRAFEEQERFIHQSDLKVDENQKAYYPSIVANRWLAVRLECVGN 1200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 459 GAVVLVLWYggSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGASVRMFEL--MDRIPSIDLEGGKKLST 536
Cdd:TIGR00957 1201 CIVLFAALF--AVISRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYseTEKEAPWQIQETAPPSG 1278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 537 VNQV--IQFQDVYFAYpsRPDSD-VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLF 613
Cdd:TIGR00957 1279 WPPRgrVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLH 1356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 614 WLRRKIALVSQEPVLFATTIAANIAYGCEATQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARAL 693
Cdd:TIGR00957 1357 DLRFKITIIPQDPVLFSGSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARAL 1436
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 694 LMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHETLLAKAGVY 770
Cdd:TIGR00957 1437 LRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIF 1513
|
|
| ABC_membrane |
pfam00664 |
ABC transporter transmembrane region; This family represents a unit of six transmembrane ... |
226-488 |
7.86e-52 |
|
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: 182.07 E-value: 7.86e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 226 LFIASVALLASSGSQIAAPYFFGRVIQASMEEGMSH---LNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQL 302
Cdd:pfam00664 1 LILAILLAILSGAISPAFPLVLGRILDVLLPDGDPEtqaLNVYSLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 303 FASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAQR 382
Cdd:pfam00664 81 FKKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 383 YGSFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQGAVV 462
Cdd:pfam00664 161 FAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYA 240
|
250 260
....*....|....*....|....*.
gi 1005434824 463 LVLWYGGSLVNKHELDVGILTAFMLY 488
Cdd:pfam00664 241 LALWFGAYLVISGELSVGDLVAFLSL 266
|
|
| ABC_6TM_ABCB8_like |
cd18574 |
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ... |
269-515 |
7.12e-49 |
|
Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B member 8, mitochondrial, and similar proteins; This group includes ABCB8, which is one of the three ATP-binding cassette (ABC) transporters found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. ABCB8 is essential for maintenance of normal cardiac function, involves mitochondrial iron export, and plays a role in the maturation of cytosolic Fe/S cluster-containing enzymes. ABCB8 is a half-molecule ABC protein that contains one TMD fused to a NBD, which dimerize to form a functional transporter.
Pssm-ID: 350018 [Multi-domain] Cd Length: 295 Bit Score: 174.66 E-value: 7.12e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 269 LSLIYLAGALAALVRSWLFTLAGQRLVARIRKQLFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYI 348
Cdd:cd18574 48 LLGLYLLQSLLTFAYISLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLRSV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 349 IQIIGSLAFMFSLSAKLTGVLISVVP-IVGIGAQrYGSFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNS 427
Cdd:cd18574 128 TQTVGCVVSLYLISPKLTLLLLVIVPvVVLVGTL-YGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELEL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 428 YDTDIDKSYKSGAKLALASGFFNGVIGIIGQGAVVLVLWYGGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFM 507
Cdd:cd18574 207 YEEEVEKAAKLNEKLGLGIGIFQGLSNLALNGIVLGVLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYV 286
|
....*...
gi 1005434824 508 QAVGASVR 515
Cdd:cd18574 287 KGKSAGAR 294
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
541-759 |
1.08e-48 |
|
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: 171.06 E-value: 1.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYpsRPD-SDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKI 619
Cdd:cd03369 7 IEVENLSVRY--APDlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 620 ALVSQEPVLFATTIAANIAYGCEATQEEIEKAAEqanahnfiasfeegyqtqVGERGVKLSGGQKQRVAIARALLMNPDV 699
Cdd:cd03369 85 TIIPQDPTLFSGTIRSNLDPFDEYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 700 LLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGT 759
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
541-763 |
1.89e-48 |
|
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: 170.82 E-value: 1.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPsrpDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYD-----PKSGVISIGRTNLAELDLF-- 613
Cdd:cd03260 1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 614 WLRRKIALVSQEPVLFATTIAANIAYGC--------EATQEEIEKAAEQAnahnfiASFEEgyqtqVGER--GVKLSGGQ 683
Cdd:cd03260 78 ELRRRVGMVFQKPNPFPGSIYDNVAYGLrlhgiklkEELDERVEEALRKA------ALWDE-----VKDRlhALGLSGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 684 KQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTV-RNADQVLVIDKGHIVERGTHET 762
Cdd:cd03260 147 QQRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFGPTEQ 226
|
.
gi 1005434824 763 L 763
Cdd:cd03260 227 I 227
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
541-754 |
2.74e-48 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 170.00 E-value: 2.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIA 620
Cdd:COG4619 1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 621 LVSQEPVLFATTIAANIAY-----GCEATQEEIEKAAEQANahnfiasFEEGY-QTQVGErgvkLSGGQKQRVAIARALL 694
Cdd:COG4619 78 YVPQEPALWGGTVRDNLPFpfqlrERKFDRERALELLERLG-------LPPDIlDKPVER----LSGGERQRLALIRALL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1005434824 695 MNPDVLLLDEATSALDAESEHFVKEAIDR--AMVNRTVLVIAH--RLSTvRNADQVLVIDKGHI 754
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHdpEQIE-RVADRVLTLEAGRL 209
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
542-753 |
4.00e-48 |
|
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: 169.57 E-value: 4.00e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 542 QFQDVYFAYPSRpDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIAL 621
Cdd:cd03225 1 ELKNLSFSYPDG-ARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 622 VSQEP--VLFATTIAANIAYGCEA---TQEEIEKAAEQANAHNFIASFEEgYQTQvgergvKLSGGQKQRVAIARALLMN 696
Cdd:cd03225 80 VFQNPddQFFGPTVEEEVAFGLENlglPEEEIEERVEEALELVGLEGLRD-RSPF------TLSGGQKQRVAIAGVLAMD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1005434824 697 PDVLLLDEATSALDAESEHFVKEAIDRamVNR---TVLVIAHRLSTVRN-ADQVLVIDKGH 753
Cdd:cd03225 153 PDILLLDEPTAGLDPAGRRELLELLKK--LKAegkTIIIVTHDLDLLLElADRVIVLEDGK 211
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
436-766 |
1.74e-47 |
|
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: 177.54 E-value: 1.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 436 YKSGAKLALAS---GFFNGVIGIIGQGAVVLVLWYGGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGA 512
Cdd:TIGR01842 211 SKYLSAQSAASdraGMLSNLSKYFRIVLQSLVLGLGAYLAIDGEITPGMMIAGSILVGRALAPIDGAIGGWKQFSGARQA 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 513 SVRMFELMDRIPSIDleGGKKLSTVNQVIQFQDVYFAYPSrPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERF 592
Cdd:TIGR01842 291 YKRLNELLANYPSRD--PAMPLPEPEGHLSVENVTIVPPG-GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGI 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 593 YDPKSGVISIGRTNLAELDLFWLRRKIALVSQEPVLFATTIAANIA-YGCEATQEEIEKAAEQANAHNFIASFEEGYQTQ 671
Cdd:TIGR01842 368 WPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTVAENIArFGENADPEKIIEAAKLAGVHELILRLPDGYDTV 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 672 VGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNR-TVLVIAHRLSTVRNADQVLVID 750
Cdd:TIGR01842 448 IGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGiTVVVITHRPSLLGCVDKILVLQ 527
|
330
....*....|....*.
gi 1005434824 751 KGHIVERGTHETLLAK 766
Cdd:TIGR01842 528 DGRIARFGERDEVLAK 543
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
540-765 |
7.92e-47 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 175.09 E-value: 7.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYPSRPDSDV--LKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAEL---DLFW 614
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGVraVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLsrrSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 615 LRRKIALVSQEPV--LFAT-TIAANIAYGCE----ATQEEIEKAAEQA-NAHNFIASFEEGYQTQvgergvkLSGGQKQR 686
Cdd:COG1123 340 LRRRVQMVFQDPYssLNPRmTVGDIIAEPLRlhglLSRAERRERVAELlERVGLPPDLADRYPHE-------LSGGQRQR 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 687 VAIARALLMNPDVLLLDEATSALDAESEHFVKEAID--RAMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHETL 763
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEV 492
|
..
gi 1005434824 764 LA 765
Cdd:COG1123 493 FA 494
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
540-766 |
5.85e-45 |
|
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: 161.59 E-value: 5.85e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYPSRPDSD-VLKGMSFELKPGETVALVGPSGGGKSTV---ISLLERfydPKSGVISIGRTNLAELDLFWL 615
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVtALKDVSLSVPKGEIFGIIGRSGAGKSTLircINGLER---PTSGSVLVDGTDLTLLSGKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 616 ---RRKIALVSQEPVLFAT-TIAANIAYGCEATQEEIEKAAEQANAH-NFI--ASFEEGYQTQvgergvkLSGGQKQRVA 688
Cdd:cd03258 78 rkaRRRIGMIFQHFNLLSSrTVFENVALPLEIAGVPKAEIEERVLELlELVglEDKADAYPAQ-------LSGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 689 IARALLMNPDVLLLDEATSALDAESEHFVKEAIDRamVNR----TVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHETL 763
Cdd:cd03258 151 IARALANNPKVLLCDEATSALDPETTQSILALLRD--INRelglTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEEV 228
|
...
gi 1005434824 764 LAK 766
Cdd:cd03258 229 FAN 231
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
541-758 |
1.07e-44 |
|
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: 158.63 E-value: 1.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRpDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFwLRRKIA 620
Cdd:cd03247 1 LSINNVSFSYPEQ-EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-LSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 621 LVSQEPVLFATTIAANIaygceatqeeiekaaeqanahnfiasfeegyqtqvgerGVKLSGGQKQRVAIARALLMNPDVL 700
Cdd:cd03247 79 VLNQRPYLFDTTLRNNL--------------------------------------GRRFSGGERQRLALARILLQDAPIV 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 701 LLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERG 758
Cdd:cd03247 121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178
|
|
| ABC_6TM_TAP2 |
cd18590 |
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ... |
244-513 |
2.61e-44 |
|
Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen processing 2 (TAP2); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350034 [Multi-domain] Cd Length: 289 Bit Score: 161.74 E-value: 2.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 244 PYFFGRVIQA-SMEEGMSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQLFASVVEQEVAFFDSNRTGEL 322
Cdd:cd18590 16 PYYTGRVIDIlGGEYQHNAFTSAIGLMCLFSLGSSLSAGLRGGLFMCTLSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 323 INRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAQRYGSFVQGLRKRFQDELAAAS 402
Cdd:cd18590 96 TSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 403 STAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQGAVVLVLWYGGSLVNKHELDVGIL 482
Cdd:cd18590 176 ELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKDRRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSL 255
|
250 260 270
....*....|....*....|....*....|.
gi 1005434824 483 TAFMLYTLNVAMAFAFLSSVYGDFMQAVGAS 513
Cdd:cd18590 256 VSFILYQKNLGSYVRTLVYIYGDMLSNVGAA 286
|
|
| ABC_6TM_MsbA_like |
cd18552 |
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ... |
226-516 |
3.35e-44 |
|
Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 161.44 E-value: 3.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 226 LFIASVALLASSGSQIAAPYFFGRVIQASMEEG-MSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQLFA 304
Cdd:cd18552 1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKdLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 305 SVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAQRYG 384
Cdd:cd18552 81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 385 SFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQGAVVLV 464
Cdd:cd18552 161 KRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 465 LWYGGSLVNKHELDVGILTAFMlytlnVAMAFAF-----LSSVYGDFMQAVGASVRM 516
Cdd:cd18552 241 LWYGGYQVISGELTPGEFISFI-----TALLLLYqpikrLSNVNANLQRGLAAAERI 292
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
541-752 |
3.91e-44 |
|
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: 158.02 E-value: 3.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPD--SDVLKGMSFELKPGETVALVGPSGGGKSTVISLLerfydpksgvisigrtnLAELDL----FW 614
Cdd:cd03250 1 ISVEDASFTWDSGEQetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-----------------LGELEKlsgsVS 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 615 LRRKIALVSQEPVLFATTIAANIAYGCEATQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALL 694
Cdd:cd03250 64 VPGSIAYVSQEPWIQNGTIRENILFGKPFDEERYEKVIKACALEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 695 MNPDVLLLDEATSALDAE-SEHFVKEAIDRAMV-NRTVLVIAHRLSTVRNADQVLVIDKG 752
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHvGRHIFENCILGLLLnNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
540-765 |
4.28e-44 |
|
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: 167.00 E-value: 4.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYPSRpDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPK---SGVISIGRTNLAELDLFWLR 616
Cdd:COG1123 4 LLEVRDLSVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 617 RKIALVSQEP--VLFATTIAANIAYGCEA---TQEEIEKAAEQANAHNFIASFEEGYQTQvgergvkLSGGQKQRVAIAR 691
Cdd:COG1123 83 RRIGMVFQDPmtQLNPVTVGDQIAEALENlglSRAEARARVLELLEAVGLERRLDRYPHQ-------LSGGQRQRVAIAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 692 ALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNR--TVLVIAHRLSTV-RNADQVLVIDKGHIVERGTHETLLA 765
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERgtTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILA 232
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
266-768 |
3.52e-43 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 169.77 E-value: 3.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 266 IVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQLFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLL 345
Cdd:PLN03232 953 IVVYALLGFGQVAVTFTNSFWLISSSLHAAKRLHDAMLNSILRAPMLFFHTNPTGRVINRFSKDIGDIDRNVANLMNMFM 1032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 346 RYIIQIIGSLAFMFSLSaklTGVLISVVPIVGIGAQRYGSF------VQGLRKRFQDELAAASSTAEEAIANIRTVRSFS 419
Cdd:PLN03232 1033 NQLWQLLSTFALIGTVS---TISLWAIMPLLILFYAAYLYYqstsreVRRLDSVTRSPIYAQFGEALNGLSSIRAYKAYD 1109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 420 QERK-SMNSYDTDID---KSYKSGAKLALASGFFNGVIgiIGQGAVVLVLWYGGSlvNKHELDVGILTAFMLYTLNVAma 495
Cdd:PLN03232 1110 RMAKiNGKSMDNNIRftlANTSSNRWLTIRLETLGGVM--IWLTATFAVLRNGNA--ENQAGFASTMGLLLSYTLNIT-- 1183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 496 fAFLSSVYGDFMQAVGA--SVR----MFELMDRIPSIDlEGGKKLST--VNQVIQFQDVYFAYpsRPD-SDVLKGMSFEL 566
Cdd:PLN03232 1184 -TLLSGVLRQASKAENSlnSVErvgnYIDLPSEATAII-ENNRPVSGwpSRGSIKFEDVHLRY--RPGlPPVLHGLSFFV 1259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 567 KPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIALVSQEPVLFATTIAANIAYGCEATQE 646
Cdd:PLN03232 1260 SPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDA 1339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 647 EIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMV 726
Cdd:PLN03232 1340 DLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFK 1419
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1005434824 727 NRTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHETLLAKAG 768
Cdd:PLN03232 1420 SCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461
|
|
| ABC_6TM_YknU_like |
cd18542 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ... |
226-515 |
3.76e-43 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 158.36 E-value: 3.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 226 LFIASVALLASSGSQIAAPYFFGRVIQASMEEG-MSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQLFA 304
Cdd:cd18542 1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGlRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 305 SVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAQRYG 384
Cdd:cd18542 81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 385 SFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQGAVVLV 464
Cdd:cd18542 161 KKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLNIKLAKLLAKYWPLMDFLSGLQIVLV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1005434824 465 LWYGGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGASVR 515
Cdd:cd18542 241 LWVGGYLVINGEITLGELVAFISYLWMLIWPVRQLGRLINDMSRASASAER 291
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
540-758 |
1.14e-42 |
|
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: 154.97 E-value: 1.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYPSRPDSD-VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELD---LFWL 615
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSrrlRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 616 RRKIALVSQEPvlFAT-----TIAANIA-----YGCEATQEEIEKAAEQANAH-NFIASFEEGYQTQvgergvkLSGGQK 684
Cdd:cd03257 81 RKEIQMVFQDP--MSSlnprmTIGEQIAeplriHGKLSKKEARKEAVLLLLVGvGLPEEVLNRYPHE-------LSGGQR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 685 QRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAID--RAMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERG 758
Cdd:cd03257 152 QRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKklQEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
541-759 |
1.36e-42 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 158.32 E-value: 1.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPDS-DVLKGMSFELKPGETVALVGPSGGGKST---VISLLERfydPKSGVISIGRTNLAELD---LF 613
Cdd:COG1135 2 IELENLSKTFPTKGGPvTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTALSereLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 614 WLRRKIALVSQEPVLFAT-TIAANIAYGCEAT---QEEI-EKAAE---------QANAhnfiasfeegYQTQvgergvkL 679
Cdd:COG1135 79 AARRKIGMIFQHFNLLSSrTVAENVALPLEIAgvpKAEIrKRVAEllelvglsdKADA----------YPSQ-------L 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 680 SGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRamVNR----TVLVIAHRLSTVRN-ADQVLVIDKGHI 754
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKD--INRelglTIVLITHEMDVVRRiCDRVAVLENGRI 219
|
....*
gi 1005434824 755 VERGT 759
Cdd:COG1135 220 VEQGP 224
|
|
| ABC_6TM_Tm288_like |
cd18547 |
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ... |
226-515 |
1.43e-42 |
|
Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm288) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349991 [Multi-domain] Cd Length: 298 Bit Score: 156.79 E-value: 1.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 226 LFIASVALLASSGSQIAAPYFFGRVI-------QASMEEGMSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARI 298
Cdd:cd18547 1 LILVIILAIISTLLSVLGPYLLGKAIdliieglGGGGGVDFSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 299 RKQLFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGI 378
Cdd:cd18547 81 RKDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 379 GAQRYGSFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQ 458
Cdd:cd18547 161 VTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEINEELYKASFKAQFYSGLLMPIMNFINN 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 459 GAVVLVLWYGGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGASVR 515
Cdd:cd18547 241 LGYVLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAER 297
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
540-765 |
2.10e-42 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 154.38 E-value: 2.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTV---ISLLERfydPKSGVISIGRTNLA--ELDLFW 614
Cdd:COG1126 1 MIEIENLHKSFGDLE---VLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDLTdsKKDINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 615 LRRKIALVSQEPVLFA-TTIAANIAYGC-----EATQEEIEKA---------AEQANAhnfiasfeegYQTQvgergvkL 679
Cdd:COG1126 75 LRRKVGMVFQQFNLFPhLTVLENVTLAPikvkkMSKAEAEERAmellervglADKADA----------YPAQ-------L 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 680 SGGQKQRVAIARALLMNPDVLLLDEATSALDAEsehFVKEAIDrAMVN-----RTVLVIAHRLSTVRN-ADQVLVIDKGH 753
Cdd:COG1126 138 SGGQQQRVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLD-VMRDlakegMTMVVVTHEMGFAREvADRVVFMDGGR 213
|
250
....*....|..
gi 1005434824 754 IVERGTHETLLA 765
Cdd:COG1126 214 IVEEGPPEEFFE 225
|
|
| ABC_6TM_YknV_like |
cd18545 |
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ... |
226-516 |
9.50e-42 |
|
Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349989 [Multi-domain] Cd Length: 293 Bit Score: 154.55 E-value: 9.50e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 226 LFIASVALLASSGSQIAAPYFFGRVIQASMEEG-MSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQLFA 304
Cdd:cd18545 2 LLLALLLMLLSTAASLAGPYLIKIAIDEYIPNGdLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 305 SVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAQRYG 384
Cdd:cd18545 82 HLQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 385 SFVqglRKRFQD---ELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQGAV 461
Cdd:cd18545 162 RRA---RKAWQRvrkKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNRENRKANMRAVRLNALFWPLVELISALGT 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 462 VLVLWYGGSLVNKHELDVGILTAFMLYtlnVAMAFA---FLSSVYGDFMQAVGASVRM 516
Cdd:cd18545 239 ALVYWYGGKLVLGGAITVGVLVAFIGY---VGRFWQpirNLSNFYNQLQSAMASAERI 293
|
|
| ABC_6TM_TmrA_like |
cd18544 |
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ... |
226-489 |
3.34e-41 |
|
Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (TrmA) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349988 [Multi-domain] Cd Length: 294 Bit Score: 152.93 E-value: 3.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 226 LFIASVALLASSGSQIAAPYFFGRVIQ---ASMEEGMSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQL 302
Cdd:cd18544 1 FILALLLLLLATALELLGPLLIKRAIDdyiVPGQGDLQGLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 303 FASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAQR 382
Cdd:cd18544 81 FSHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 383 YGSFVqglRKRFQD-------------ElaaasstaeeAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFF 449
Cdd:cd18544 161 FRKKS---RKAYREvreklsrlnaflqE----------SISGMSVIQLFNREKREFEEFDEINQEYRKANLKSIKLFALF 227
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1005434824 450 NGVIGIIGQGAVVLVLWYGGSLVNKHELDVGILTAFMLYT 489
Cdd:cd18544 228 RPLVELLSSLALALVLWYGGGQVLSGAVTLGVLYAFIQYI 267
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
541-768 |
1.25e-40 |
|
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: 150.27 E-value: 1.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYP--SRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISI-GRTNLAELDLFWLRR 617
Cdd:TIGR04520 1 IEVENVSFSYPesEKP---ALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVdGLDTLDEENLWEIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 618 KIALVSQEP--VLFATTIAANIAYGCE---ATQEEIEKAAEQAnahnfIASFE-EGYQTQVGERgvkLSGGQKQRVAIAR 691
Cdd:TIGR04520 78 KVGMVFQNPdnQFVGATVEDDVAFGLEnlgVPREEMRKRVDEA-----LKLVGmEDFRDREPHL---LSGGQKQRVAIAG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 692 ALLMNPDVLLLDEATSALDAESEHFVKEAIDRamVNR----TVLVIAHRLSTVRNADQVLVIDKGHIVERGT------HE 761
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRK--LNKeegiTVISITHDMEEAVLADRVIVMNKGKIVAEGTpreifsQV 227
|
....*..
gi 1005434824 762 TLLAKAG 768
Cdd:TIGR04520 228 ELLKEIG 234
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
538-761 |
1.68e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 150.55 E-value: 1.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 538 NQVIQFQDVYFAYP--SRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWL 615
Cdd:PRK13635 3 EEIIRVEHISFRYPdaATY---ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 616 RRKIALVSQEP--VLFATTIAANIAYGCE-------ATQEEIEKAAEQANAHNFiASFEEGyqtqvgergvKLSGGQKQR 686
Cdd:PRK13635 80 RRQVGMVFQNPdnQFVGATVQDDVAFGLEnigvpreEMVERVDQALRQVGMEDF-LNREPH----------RLSGGQKQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 687 VAIARALLMNPDVLLLDEATSALDAESEHFVKEAIdRAMVNR---TVLVIAHRLSTVRNADQVLVIDKGHIVERGTHE 761
Cdd:PRK13635 149 VAIAGVLALQPDIIILDEATSMLDPRGRREVLETV-RQLKEQkgiTVLSITHDLDEAAQADRVIVMNKGEILEEGTPE 225
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
541-767 |
1.69e-40 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 149.06 E-value: 1.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIG----RTNLAELdlfwlR 616
Cdd:COG1131 1 IEVRGLTKRYGDKT---ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLgedvARDPAEV-----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 617 RKIALVSQEPVLFAT-TIAANIAYGCEA---TQEEIEKAAEQAnahnfIASF--EEGYQTQVGergvKLSGGQKQRVAIA 690
Cdd:COG1131 73 RRIGYVPQEPALYPDlTVRENLRFFARLyglPRKEARERIDEL-----LELFglTDAADRKVG----TLSGGMKQRLGLA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 691 RALLMNPDVLLLDEATSALDAESEHFVKEAIdRAMV--NRTVLVIAHRLSTV-RNADQVLVIDKGHIVERGTHETLLAKA 767
Cdd:COG1131 144 LALLHDPELLILDEPTSGLDPEARRELWELL-RELAaeGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKARL 222
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
541-757 |
1.78e-40 |
|
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: 148.39 E-value: 1.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPDS-DVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELdlfwlRRKI 619
Cdd:cd03293 1 LEVRNVSKTYGGGGGAvTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGP-----GPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 620 ALVSQEPVLFA-TTIAANIAYGCEATqeEIEKAAEQANAHNFIA-----SFEEGYQTQvgergvkLSGGQKQRVAIARAL 693
Cdd:cd03293 76 GYVFQQDALLPwLTVLDNVALGLELQ--GVPKAEARERAEELLElvglsGFENAYPHQ-------LSGGMRQRVALARAL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1005434824 694 LMNPDVLLLDEATSALDAesehFVKEAIDRAMVN------RTVLVIAHRLS-TVRNADQVLVIDK--GHIVER 757
Cdd:cd03293 147 AVDPDVLLLDEPFSALDA----LTREQLQEELLDiwretgKTVLLVTHDIDeAVFLADRVVVLSArpGRIVAE 215
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
541-765 |
2.07e-40 |
|
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: 149.18 E-value: 2.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPDS-DVLKGMSFELKPGETVALVGPSGGGKST---VISLLERfydPKSGVISIGRTNLAELDLFWLR 616
Cdd:COG1124 2 LEVRNLSVSYGQGGRRvPVLKDVSLEVAPGESFGLVGESGSGKSTllrALAGLER---PWSGEVTFDGRPVTRRRRKAFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 617 RKIALVSQEPvlFAT-----TIAANIA-----YGCEATQEEIEKAAEQANAHnfiASFEEGYQTQvgergvkLSGGQKQR 686
Cdd:COG1124 79 RRVQMVFQDP--YASlhprhTVDRILAeplriHGLPDREERIAELLEQVGLP---PSFLDRYPHQ-------LSGGQRQR 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 687 VAIARALLMNPDVLLLDEATSALD----AESEHFVKEAidRAMVNRTVLVIAHRLSTV-RNADQVLVIDKGHIVERGTHE 761
Cdd:COG1124 147 VAIARALILEPELLLLDEPTSALDvsvqAEILNLLKDL--REERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVA 224
|
....
gi 1005434824 762 TLLA 765
Cdd:COG1124 225 DLLA 228
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
541-754 |
3.16e-40 |
|
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: 145.82 E-value: 3.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYP--SRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRK 618
Cdd:cd03246 1 LEVENVSFRYPgaEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 619 IALVSQEPVLFATTIAANIaygceatqeeiekaaeqanahnfiasfeegyqtqvgergvkLSGGQKQRVAIARALLMNPD 698
Cdd:cd03246 78 VGYLPQDDELFSGSIAENI-----------------------------------------LSGGQRQRLGLARALYGNPR 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 699 VLLLDEATSALDAESEHFVKEAIDRA-MVNRTVLVIAHRLSTVRNADQVLVIDKGHI 754
Cdd:cd03246 117 ILVLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| ABC_6TM_TAP1 |
cd18589 |
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ... |
233-513 |
1.55e-39 |
|
Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen processing 1 (TAP1); This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.
Pssm-ID: 350033 [Multi-domain] Cd Length: 289 Bit Score: 148.00 E-value: 1.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 233 LLASSGSQIAAPYFFGRVIQASMEEGM-SHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQLFASVVEQEV 311
Cdd:cd18589 5 VVLSSLGEMAIPYYTGRMTDWIMNKDApEAFTAAITVMSLLTIASAVSEFVCDLIYNITMSRIHSRLQGLVFAAVLRQEI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 312 AFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAQRYGSFVQGLR 391
Cdd:cd18589 85 AFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLALLTALGLPLLLLVPKFVGKFQQSLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 392 KRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQGAVVLVLWYGGSL 471
Cdd:cd18589 165 VQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTYRLNKKEAAAYAVSMWTSSFSGLALKVGILYYGGQL 244
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1005434824 472 VNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGAS 513
Cdd:cd18589 245 VTAGTVSSGDLVTFVLYELQFTSAVEVLLSYYPSVMKAVGSS 286
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
540-764 |
3.00e-39 |
|
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: 145.96 E-value: 3.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKI 619
Cdd:COG1120 1 MLEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 620 ALVSQEPVL-FATTIAANIAYGC-----------EATQEEIEKAAEQANAHNFIasfeegyqtqvgERGV-KLSGGQKQR 686
Cdd:COG1120 78 AYVPQEPPApFGLTVRELVALGRyphlglfgrpsAEDREAVEEALERTGLEHLA------------DRPVdELSGGERQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 687 VAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDR--AMVNRTVLVIAHRLS-TVRNADQVLVIDKGHIVERGTHETL 763
Cdd:COG1120 146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225
|
.
gi 1005434824 764 L 764
Cdd:COG1120 226 L 226
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
541-758 |
4.07e-39 |
|
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: 144.20 E-value: 4.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSrpdSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLfwLRRKIA 620
Cdd:cd03259 1 LELKGLSKTYGS---VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP--ERRNIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 621 LVSQEPVLFAT-TIAANIAYGCEA---TQEEIEKAAEQANAHNFIASFEEGYQTQvgergvkLSGGQKQRVAIARALLMN 696
Cdd:cd03259 76 MVFQDYALFPHlTVAENIAFGLKLrgvPKAEIRARVRELLELVGLEGLLNRYPHE-------LSGGQQQRVALARALARE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 697 PDVLLLDEATSALDAES----EHFVKEAIDRAMVnrTVLVIAHRLS-TVRNADQVLVIDKGHIVERG 758
Cdd:cd03259 149 PSLLLLDEPLSALDAKLreelREELKELQRELGI--TTIYVTHDQEeALALADRIAVMNEGRIVQVG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
542-753 |
4.52e-39 |
|
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: 142.00 E-value: 4.52e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 542 QFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIAL 621
Cdd:cd00267 1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 622 VSQepvlfattiaaniaygceatqeeiekaaeqanahnfiasfeegyqtqvgergvkLSGGQKQRVAIARALLMNPDVLL 701
Cdd:cd00267 78 VPQ------------------------------------------------------LSGGQRQRVALARALLLNPDLLL 103
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1005434824 702 LDEATSALDAESEHFVKEAIDRAMV-NRTVLVIAHRLSTVRNA-DQVLVIDKGH 753
Cdd:cd00267 104 LDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAELAaDRVIVLKDGK 157
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
532-759 |
5.36e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 145.90 E-value: 5.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 532 KKLSTVnqVIQFQDVYFAYPSRpDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELD 611
Cdd:PRK13632 1 IKNKSV--MIKVENVSFSYPNS-ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 612 LFWLRRKIALVSQEP--VLFATTIAANIAYGCE-------ATQEEIEKAAEQANAHNFIaSFEEGYqtqvgergvkLSGG 682
Cdd:PRK13632 78 LKEIRKKIGIIFQNPdnQFIGATVEDDIAFGLEnkkvppkKMKDIIDDLAKKVGMEDYL-DKEPQN----------LSGG 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005434824 683 QKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAID--RAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGT 759
Cdd:PRK13632 147 QKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGK 225
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
540-763 |
1.53e-38 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 143.69 E-value: 1.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELdlfwlRRKI 619
Cdd:COG1121 6 AIELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA-----RRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 620 ALVSQEPVL---FATTIAANIAYGC-----------EATQEEIEKAAEQANAHNFIasfeegyQTQVGErgvkLSGGQKQ 685
Cdd:COG1121 78 GYVPQRAEVdwdFPITVRDVVLMGRygrrglfrrpsRADREAVDEALERVGLEDLA-------DRPIGE----LSGGQQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 686 RVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDR-AMVNRTVLVIAHRLSTVR-NADQVLVIDKGHIVERGTHETL 763
Cdd:COG1121 147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVReYFDRVLLLNRGLVAHGPPEEVL 226
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
541-765 |
1.69e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 142.97 E-value: 1.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPdsdvlkgMSFEL--KPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFwlRRK 618
Cdd:COG3840 2 LRLDDLTYRYGDFP-------LRFDLtiAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA--ERP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 619 IALVSQEPVLFA-TTIAANIAYGC-------EATQEEIEKAAEQANahnfIASFEEGYQTQvgergvkLSGGQKQRVAIA 690
Cdd:COG3840 73 VSMLFQENNLFPhLTVAQNIGLGLrpglkltAEQRAQVEQALERVG----LAGLLDRLPGQ-------LSGGQRQRVALA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 691 RALLMNPDVLLLDEATSALD----AESEHFVKEAIDRAmvNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHETLLA 765
Cdd:COG3840 142 RCLVRKRPILLLDEPFSALDpalrQEMLDLVDELCRER--GLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLD 219
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
535-756 |
1.84e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 144.08 E-value: 1.84e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 535 STVNQVIQFQDVYFAYPSRPDS-DVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDlf 613
Cdd:COG1116 2 SAAAPALELRGVSKRFPTGGGGvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 614 wlrRKIALVSQEPVLFA-TTIAANIAYGCEATQEEIEKAAEQANAhnFIA-----SFEEGYQTQvgergvkLSGGQKQRV 687
Cdd:COG1116 80 ---PDRGVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERARE--LLElvglaGFEDAYPHQ-------LSGGMRQRV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 688 AIARALLMNPDVLLLDEATSALDA--------ESEHFVKEAidramvNRTVLVIAH------RLstvrnADQVLVIDK-- 751
Cdd:COG1116 148 AIARALANDPEVLLMDEPFGALDAltrerlqdELLRLWQET------GKTVLFVTHdvdeavFL-----ADRVVVLSArp 216
|
....*
gi 1005434824 752 GHIVE 756
Cdd:COG1116 217 GRIVE 221
|
|
| ABC_6TM_exporter_like |
cd18563 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
226-516 |
2.65e-38 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 144.57 E-value: 2.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 226 LFIASVALLASSGSQIAAPYFFGRVI-----QASMEEGMSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRK 300
Cdd:cd18563 1 LILGFLLMLLGTALGLVPPYLTKILIddvliQLGPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 301 QLFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGA 380
Cdd:cd18563 81 DLYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 381 QRYGSFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQGA 460
Cdd:cd18563 161 YFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANIRAEKLWATFFPLLTFLTSLG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1005434824 461 VVLVLWYGGSLVNKHELDVGILTAFMLYTlnvAMAFA---FLSSVYGDFMQAVGASVRM 516
Cdd:cd18563 241 TLIVWYFGGRQVLSGTMTLGTLVAFLSYL---GMFYGplqWLSRLNNWITRALTSAERI 296
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
559-707 |
3.37e-38 |
|
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: 139.32 E-value: 3.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 559 LKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIALVSQEPVLF-ATTIAANI 637
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 638 AYGC-------EATQEEIEKAAEQANAHNFIASFeegyqtqVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATS 707
Cdd:pfam00005 81 RLGLllkglskREKDARAEEALEKLGLGDLADRP-------VGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
540-765 |
3.74e-38 |
|
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: 142.43 E-value: 3.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELD---LFWLR 616
Cdd:COG1127 5 MIEVRNLTKSFGDRV---VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSekeLYELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 617 RKIALVSQEPVLF-ATTIAANIAYGCEA----TQEEIEKAAEQANAhnfiasfeegyqtQVGERGVK------LSGGQKQ 685
Cdd:COG1127 82 RRIGMLFQGGALFdSLTVFENVAFPLREhtdlSEAEIRELVLEKLE-------------LVGLPGAAdkmpseLSGGMRK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 686 RVAIARALLMNPDVLLLDEATSALDAESehfvKEAID------RAMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERG 758
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPIT----SAVIDelirelRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEG 224
|
....*..
gi 1005434824 759 THETLLA 765
Cdd:COG1127 225 TPEELLA 231
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
540-756 |
4.98e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 141.34 E-value: 4.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYPsrPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAEL---DLFWLR 616
Cdd:COG2884 1 MIRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLkrrEIPYLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 617 RKIALVSQE-PVLFATTIAANIAYGCEAT---QEEIEKAAEQAnahnfiasFEegyqtQVGERG------VKLSGGQKQR 686
Cdd:COG2884 79 RRIGVVFQDfRLLPDRTVYENVALPLRVTgksRKEIRRRVREV--------LD-----LVGLSDkakalpHELSGGEQQR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005434824 687 VAIARALLMNPDVLLLDEATSALDAES-----EHFVKeaidramVNR---TVLVIAHRLSTVRNADQ-VLVIDKGHIVE 756
Cdd:COG2884 146 VAIARALVNRPELLLADEPTGNLDPETsweimELLEE-------INRrgtTVLIATHDLELVDRMPKrVLELEDGRLVR 217
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
541-753 |
5.07e-38 |
|
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: 139.63 E-value: 5.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPsrpDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFW--LRRK 618
Cdd:cd03229 1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 619 IALVSQEPVLFAT-TIAANIAYGceatqeeiekaaeqanahnfiasfeegyqtqvgergvkLSGGQKQRVAIARALLMNP 697
Cdd:cd03229 78 IGMVFQDFALFPHlTVLENIALG--------------------------------------LSGGQQQRVALARALAMDP 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1005434824 698 DVLLLDEATSALDAESEHFVKEAID--RAMVNRTVLVIAHRLSTVRN-ADQVLVIDKGH 753
Cdd:cd03229 120 DVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
540-756 |
6.94e-38 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 140.95 E-value: 6.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYPSRPDS-DVLKGMSFELKPGETVALVGPSGGGKST---VISLLERfydPKSGVISIGRTNL-----AEL 610
Cdd:COG1136 4 LLELRNLTKSYGTGEGEvTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDIsslseREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 611 DLFWlRRKIALVSQEPVLFAT-TIAANIAYGCEATQEEIEKAAEQAN-----------AHNFIAsfeegyqtqvgergvK 678
Cdd:COG1136 81 ARLR-RRHIGFVFQFFNLLPElTALENVALPLLLAGVSRKERRERARellervglgdrLDHRPS---------------Q 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 679 LSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDR--AMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVE 756
Cdd:COG1136 145 LSGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
541-774 |
1.78e-37 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 152.20 E-value: 1.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYpsRPD-SDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKI 619
Cdd:PLN03130 1238 IKFEDVVLRY--RPElPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 620 ALVSQEPVLFATTIAANIAYGCEATQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPDV 699
Cdd:PLN03130 1316 GIIPQAPVLFSGTVRFNLDPFNEHNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKI 1395
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1005434824 700 LLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHETLLAKAG-VYKKLV 774
Cdd:PLN03130 1396 LVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLSNEGsAFSKMV 1471
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
540-768 |
2.38e-37 |
|
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: 139.99 E-value: 2.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLfWLRRKI 619
Cdd:COG4555 1 MIEVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR-EARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 620 ALVSQEPVLFAT-TIAANIAYGCEA---TQEEIEKAAEQAnAHNFIasFEEGYQTQVGErgvkLSGGQKQRVAIARALLM 695
Cdd:COG4555 77 GVLPDERGLYDRlTVRENIRYFAELyglFDEELKKRIEEL-IELLG--LEEFLDRRVGE----LSTGMKKKVALARALVH 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1005434824 696 NPDVLLLDEATSALDAESEHFVKEAIdRAMVN--RTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHETLLAKAG 768
Cdd:COG4555 150 DPKVLLLDEPTNGLDVMARRLLREIL-RALKKegKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREEIG 224
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
541-754 |
2.77e-37 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 138.82 E-value: 2.77e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNL--AELDLFWLRRK 618
Cdd:cd03262 1 IEIKNLHKSFGDFH---VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 619 IALVSQEPVLFA-TTIAANIAYGCEATQ----EEIEKAAEQANAHNFIASFEEGYQTQvgergvkLSGGQKQRVAIARAL 693
Cdd:cd03262 78 VGMVFQQFNLFPhLTVLENITLAPIKVKgmskAEAEERALELLEKVGLADKADAYPAQ-------LSGGQQQRVAIARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 694 LMNPDVLLLDEATSALDAEsehFVKEAIDrAMVN-----RTVLVIAHRLSTVRN-ADQVLVIDKGHI 754
Cdd:cd03262 151 AMNPKVMLFDEPTSALDPE---LVGEVLD-VMKDlaeegMTMVVVTHEMGFAREvADRVIFMDDGRI 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
541-765 |
3.90e-37 |
|
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: 139.17 E-value: 3.90e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAEL---DLFWLRR 617
Cdd:cd03261 1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLseaELYRLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 618 KIALVSQEPVLF-ATTIAANIAYGC-EATQ---EEI-EKAAEQANAhnfiasfeegyqtqVGERGVK------LSGGQKQ 685
Cdd:cd03261 78 RMGMLFQSGALFdSLTVFENVAFPLrEHTRlseEEIrEIVLEKLEA--------------VGLRGAEdlypaeLSGGMKK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 686 RVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDR--AMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHET 762
Cdd:cd03261 144 RVALARALALDPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEE 223
|
...
gi 1005434824 763 LLA 765
Cdd:cd03261 224 LRA 226
|
|
| ABC_6TM_TmrB_like |
cd18541 |
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ... |
226-503 |
4.45e-37 |
|
Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug resistance proteins TmrAB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the heterodimeric Thermus thermophilus multidrug resistance proteins A and B (TmrAB), a homolog of the Antigen Translocation Complex Tap, and similar proteins. TmrAB has been shown to able to restore antigen processing in human TAP-deficient cells. The 6-transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349985 [Multi-domain] Cd Length: 293 Bit Score: 141.01 E-value: 4.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 226 LFIASVALLASSGSQIAAPYFFGRVIQAsMEEGMSHLNKTIVLLSLIYLAGALAALVR-SWLFTL--AGQRLVARIRKQL 302
Cdd:cd18541 1 YLLGILFLILVDLLQLLIPRIIGRAIDA-LTAGTLTASQLLRYALLILLLALLIGIFRfLWRYLIfgASRRIEYDLRNDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 303 FASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAQR 382
Cdd:cd18541 80 FAHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 383 YGSFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQGAVV 462
Cdd:cd18541 160 LGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGLSFL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1005434824 463 LVLWYGGSLVNKHELDVGILTAFMLYtLNV----AMAFAFLSSVY 503
Cdd:cd18541 240 IVLWYGGRLVIRGTITLGDLVAFNSY-LGMliwpMMALGWVINLI 283
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
541-754 |
1.21e-36 |
|
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: 137.24 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPDS-DVLKGMSFELKPGETVALVGPSGGGKST---VISLLERfydPKSGVISIGRTNL-----AELD 611
Cdd:cd03255 1 IELKNLSKTYGGGGEKvQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDIsklseKELA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 612 LFwLRRKIALVSQEPVLFAT-TIAANIAYGCEATQEEIEKAAEQAnahnfIASFEE-GYQTQVGERGVKLSGGQKQRVAI 689
Cdd:cd03255 78 AF-RRRHIGFVFQSFNLLPDlTALENVELPLLLAGVPKKERRERA-----EELLERvGLGDRLNHYPSELSGGQQQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 690 ARALLMNPDVLLLDEATSALDAESEHFVKEAIdRAMV---NRTVLVIAHRLSTVRNADQVLVIDKGHI 754
Cdd:cd03255 152 ARALANDPKIILADEPTGNLDSETGKEVMELL-RELNkeaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
541-774 |
4.58e-36 |
|
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: 136.96 E-value: 4.58e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPS--RPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRK 618
Cdd:cd03288 20 IKIHDLCVRYENnlKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 619 IALVSQEPVLFATTIAANIAYGCEATQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPD 698
Cdd:cd03288 97 LSIILQDPILFSGSIRFNLDPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 699 VLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHETLLA-KAGVYKKLV 774
Cdd:cd03288 177 ILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAqEDGVFASLV 253
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
541-765 |
6.46e-36 |
|
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: 135.89 E-value: 6.46e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPDsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIA 620
Cdd:cd03295 1 IEFENVTKRYGGGKK--AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 621 LVSQEPVLFA-TTIAANIayGCEATQEEIEKAAEQANAHNFI-------ASFEEGYQTQvgergvkLSGGQKQRVAIARA 692
Cdd:cd03295 79 YVIQQIGLFPhMTVEENI--ALVPKLLKWPKEKIRERADELLalvgldpAEFADRYPHE-------LSGGQQQRVGVARA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005434824 693 LLMNPDVLLLDEATSALDAES-----EHFVKeaIDRAmVNRTVLVIAHRL-STVRNADQVLVIDKGHIVERGTHETLLA 765
Cdd:cd03295 150 LAADPPLLLMDEPFGALDPITrdqlqEEFKR--LQQE-LGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEILR 225
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
535-763 |
2.18e-35 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 135.16 E-value: 2.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 535 STVNQVIQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYD--PK---SGVISIGRTNL-- 607
Cdd:COG1117 6 STLEPKIEVRNLNVYYGDKQ---ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLDGEDIyd 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 608 AELDLFWLRRKIALVSQEPVLFATTIAANIAYGCE-------ATQEEI-EKAAEQAnahnfiASFEEgyqtqVGER---- 675
Cdd:COG1117 83 PDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGLRlhgikskSELDEIvEESLRKA------ALWDE-----VKDRlkks 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 676 GVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLS-TVRNADQVLVIDKGHI 754
Cdd:COG1117 152 ALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQqAARVSDYTAFFYLGEL 231
|
....*....
gi 1005434824 755 VERGTHETL 763
Cdd:COG1117 232 VEFGPTEQI 240
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
544-758 |
2.22e-35 |
|
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: 132.17 E-value: 2.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 544 QDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIALVS 623
Cdd:cd03214 3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 624 QepvlfattiaaniaygceatqeeiekAAEQANAHNFIasfEEGYQTqvgergvkLSGGQKQRVAIARALLMNPDVLLLD 703
Cdd:cd03214 80 Q--------------------------ALELLGLAHLA---DRPFNE--------LSGGERQRVLLARALAQEPPILLLD 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 704 EATSALDAESEHFVKEAIDR--AMVNRTVLVIAHRLS-TVRNADQVLVIDKGHIVERG 758
Cdd:cd03214 123 EPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
541-759 |
6.44e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 136.43 E-value: 6.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKST---VISLLERfydPKSGVISI-GRtnlaelDLF-WL 615
Cdd:COG1118 3 IEVRNISKRFGSFT---LLDDVSLEIASGELVALLGPSGSGKTTllrIIAGLET---PDSGRIVLnGR------DLFtNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 616 ---RRKIALVSQEPVLFA-TTIAANIAYGCEA---TQEEI-EKAAEQANAHNfIASFEEGYQTQvgergvkLSGGQKQRV 687
Cdd:COG1118 71 pprERRVGFVFQHYALFPhMTVAENIAFGLRVrppSKAEIrARVEELLELVQ-LEGLADRYPSQ-------LSGGQRQRV 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005434824 688 AIARALLMNPDVLLLDEATSALDAesehFVKEAIDRAM------VNRTVLVIAH-RLSTVRNADQVLVIDKGHIVERGT 759
Cdd:COG1118 143 ALARALAVEPEVLLLDEPFGALDA----KVRKELRRWLrrlhdeLGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGT 217
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
540-759 |
8.90e-35 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 135.70 E-value: 8.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYP-SRPDSDVLKGMSFELKPGETVALVGPSGGGKST---VISLLERfydPKSG-VISIGR--TNLAELDL 612
Cdd:PRK11153 1 MIELKNISKVFPqGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGrVLVDGQdlTALSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 613 FWLRRKIALVSQEPVLFAT-TIAANIAYGCEA---TQEEIEKA----------AEQANAhnfiasfeegYQTQvgergvk 678
Cdd:PRK11153 78 RKARRQIGMIFQHFNLLSSrTVFDNVALPLELagtPKAEIKARvtellelvglSDKADR----------YPAQ------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 679 LSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIdrAMVNR----TVLVIAHRLSTVRN-ADQVLVIDKGH 753
Cdd:PRK11153 141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELL--KDINRelglTIVLITHEMDVVKRiCDRVAVIDAGR 218
|
....*.
gi 1005434824 754 IVERGT 759
Cdd:PRK11153 219 LVEQGT 224
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
541-763 |
9.65e-35 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 136.00 E-value: 9.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFwlRRKIA 620
Cdd:COG3842 6 LELENVSKRYGDVT---ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 621 LVSQEPVLFA-TTIAANIAYGCEA---TQEEIEKAAEQANAHNFIASFEEGYQTQvgergvkLSGGQKQRVAIARALLMN 696
Cdd:COG3842 81 MVFQDYALFPhLTVAENVAFGLRMrgvPKAEIRARVAELLELVGLEGLADRYPHQ-------LSGGQQQRVALARALAPE 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 697 PDVLLLDEATSALDAesehFVKEAIdRAMVNR-------TVLVIAHRLS---TVrnADQVLVIDKGHIVERGTHETL 763
Cdd:COG3842 154 PRVLLLDEPLSALDA----KLREEM-REELRRlqrelgiTFIYVTHDQEealAL--ADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_6TM_exporter_like |
cd18550 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
226-523 |
7.53e-34 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 131.84 E-value: 7.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 226 LFIASVALLASSGSQIAAPYFFGRVI-QASMEEGMSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQLFA 304
Cdd:cd18550 1 LALVLLLILLSALLGLLPPLLLREIIdDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 305 SVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAQRYG 384
Cdd:cd18550 81 HLQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 385 SFVQGLRKRFQDELAAASSTAEEA--IANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQGAVV 462
Cdd:cd18550 161 RRRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAARFARRSRELRDLGVRQALAGRWFFAALGLFTAIGPA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1005434824 463 LVLWYGGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGasvrmfeLMDRI 523
Cdd:cd18550 241 LVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLA-------LFERI 294
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
541-754 |
1.24e-33 |
|
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: 127.13 E-value: 1.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAElDLFWLRRKIA 620
Cdd:cd03230 1 IEVRNLSKRYGKKT---ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 621 LVSQEPVLFAT-TIAANIaygceatqeeiekaaeqanahnfiasfeegyqtqvgergvKLSGGQKQRVAIARALLMNPDV 699
Cdd:cd03230 77 YLPEEPSLYENlTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPEL 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 700 LLLDEATSALDAESEHFVKEAIDR-AMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHI 754
Cdd:cd03230 117 LILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
540-755 |
3.40e-33 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 128.25 E-value: 3.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYPSrpDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAEL---DLFWLR 616
Cdd:COG3638 2 MLELRNLSKRYPG--GTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALrgrALRRLR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 617 RKIALVSQEPVLFA-TTIAANIAYGCEA------------TQEEIEKA---------AEQANahnfiasfeegyqtqvgE 674
Cdd:COG3638 80 RRIGMIFQQFNLVPrLSVLTNVLAGRLGrtstwrsllglfPPEDRERAlealervglADKAY-----------------Q 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 675 RGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAES-----EHFVKEAIDRamvNRTVLVIAHRLSTVRN-ADQVLV 748
Cdd:COG3638 143 RADQLSGGQQQRVAIARALVQEPKLILADEPVASLDPKTarqvmDLLRRIARED---GITVVVNLHQVDLARRyADRIIG 219
|
....*..
gi 1005434824 749 IDKGHIV 755
Cdd:COG3638 220 LRDGRVV 226
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
558-765 |
3.68e-33 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 128.33 E-value: 3.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTV---ISLLERfydPKSGVISIGRTnlaELD-----------LFWLRRKIALVS 623
Cdd:PRK11264 18 VLHGIDLEVKPGEVVAIIGPSGSGKTTLlrcINLLEQ---PEAGTIRVGDI---TIDtarslsqqkglIRQLRQHVGFVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 624 QEPVLFA-TTIAANIAYGCEATQEEIEKAAEqANAHNFIAsfeegyqtQVGERGV------KLSGGQKQRVAIARALLMN 696
Cdd:PRK11264 92 QNFNLFPhRTVLENIIEGPVIVKGEPKEEAT-ARARELLA--------KVGLAGKetsyprRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1005434824 697 PDVLLLDEATSALDAEsehFVKEAID--RAMV--NRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHETLLA 765
Cdd:PRK11264 163 PEVILFDEPTSALDPE---LVGEVLNtiRQLAqeKRTMVIVTHEMSFARDvADRAIFMDQGRIVEQGPAKALFA 233
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
542-752 |
5.14e-33 |
|
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: 126.88 E-value: 5.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 542 QFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIgrtnlAELDLFWLRRKIAL 621
Cdd:cd03235 1 EVEDLTVSYGGHP---VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRV-----FGKPLEKERKRIGY 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 622 VSQEPVL---FATTIAANIAYGCEA--------TQEEIEKAAEqanAHNF--IASFEEgyqTQVGErgvkLSGGQKQRVA 688
Cdd:cd03235 73 VPQRRSIdrdFPISVRDVVLMGLYGhkglfrrlSKADKAKVDE---ALERvgLSELAD---RQIGE----LSGGQQQRVL 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1005434824 689 IARALLMNPDVLLLDEATSALDAESEHFVKEAIDR-AMVNRTVLVIAHRLSTV-RNADQVLVIDKG 752
Cdd:cd03235 143 LARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVlEYFDRVLLLNRT 208
|
|
| ABC_6TM_exporter_like |
cd18564 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
226-488 |
5.20e-33 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 129.55 E-value: 5.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 226 LFIASVALLASSGSQIAAP----YFFGRVIQASMEEGMSHLNK-----TIVLLSL-------IYLAGALAALVRSWLFTL 289
Cdd:cd18564 1 LALALLALLLETALRLLEPwplkVVIDDVLGDKPLPGLLGLAPllgpdPLALLLLaaaalvgIALLRGLASYAGTYLTAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 290 AGQRLVARIRKQLFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVL 369
Cdd:cd18564 81 VGQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 370 ISVVPIVGIGAQRYGSFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFF 449
Cdd:cd18564 161 LAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFARENRKSLRAGLRAARLQALL 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 1005434824 450 NGVIGIIGQGAVVLVLWYGGSLVNKHELDVGILTAFMLY 488
Cdd:cd18564 241 SPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAY 279
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
541-761 |
1.72e-32 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 126.28 E-value: 1.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSrpdSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIG------RTNLAELDLFW 614
Cdd:COG4161 3 IQLKNINCFYGS---HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAghqfdfSQKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 615 LRRKIALVSQE----PVLfatTIAAN-IAYGCEATQEEIEKAAEQAN---AHNFIASFEEGYQTQvgergvkLSGGQKQR 686
Cdd:COG4161 80 LRQKVGMVFQQynlwPHL---TVMENlIEAPCKVLGLSKEQAREKAMkllARLRLTDKADRFPLH-------LSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 687 VAIARALLMNPDVLLLDEATSALDAESEHFVKEAI-DRAMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHE 761
Cdd:COG4161 150 VAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIrELSQTGITQVIVTHEVEFARKvASQVVYMEKGRIIEQGDAS 226
|
|
| ABC_6TM_Tm287_like |
cd18548 |
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ... |
226-514 |
2.75e-32 |
|
Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 127.13 E-value: 2.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 226 LFIASVALLASSGSQIAAPYFFGRVI-QASMEEGMSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQLFA 304
Cdd:cd18548 1 AILAPLFKLLEVLLELLLPTLMADIIdEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 305 SVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAQRYG 384
Cdd:cd18548 81 KIQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 385 SFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQGAVVLV 464
Cdd:cd18548 161 KKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTSLKAGRLMALLNPLMMLIMNLAIVAI 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1005434824 465 LWYGGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVygdFMQAVGASV 514
Cdd:cd18548 241 LWFGGHLINAGSLQVGDLVAFINYLMQILMSLMMLSMV---FVMLPRASA 287
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
563-766 |
4.32e-32 |
|
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: 125.83 E-value: 4.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 563 SFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAEL---DLFWLRRK-IALVSQEPVLFA-TTIAANI 637
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMsrkELRELRRKkISMVFQSFALLPhRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 638 AYGCE----ATQEEIEKAAEQANAHNfIASFEEGYQTQvgergvkLSGGQKQRVAIARALLMNPDVLLLDEATSALD--- 710
Cdd:cd03294 124 AFGLEvqgvPRAEREERAAEALELVG-LEGWEHKYPDE-------LSGGMQQRVGLARALAVDPDILLMDEAFSALDpli 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1005434824 711 -AE-SEHFVKEaidRAMVNRTVLVIAHRLS-TVRNADQVLVIDKGHIVERGTHETLLAK 766
Cdd:cd03294 196 rREmQDELLRL---QAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABC_6TM_Rv0194_D1_like |
cd18543 |
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ... |
226-515 |
4.99e-32 |
|
Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349987 [Multi-domain] Cd Length: 291 Bit Score: 126.44 E-value: 4.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 226 LFIASVALLASSGSQIAAPYFFGRVI-QASMEEGMSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQLFA 304
Cdd:cd18543 1 LILALLAALLATLAGLAIPLLTRRAIdGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 305 SVVEQEVAFFDSNRTGELINRLSSDTQVIQnALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAQRYG 384
Cdd:cd18543 81 HLQRLDGAFHDRWQSGQLLSRATSDLSLVQ-RFLAFGPFLLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 385 SFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQGAVVLV 464
Cdd:cd18543 160 RRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAV 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1005434824 465 LWYGGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGASVR 515
Cdd:cd18543 240 LALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAAAER 290
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
541-759 |
1.72e-31 |
|
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: 123.45 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSrpDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISI---GRTNLAELDLFWLRR 617
Cdd:cd03256 1 IEVENLSKTYPN--GKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIdgtDINKLKGKALRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 618 KIALVSQEPVLFA-TTIAANIAYGCEA------------TQEEIEKAAEqanahnfiasfeegYQTQVG------ERGVK 678
Cdd:cd03256 79 QIGMIFQQFNLIErLSVLENVLSGRLGrrstwrslfglfPKEEKQRALA--------------ALERVGlldkayQRADQ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 679 LSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRA--MVNRTVLVIAHRLSTVR-NADQVLVIDKGHIV 755
Cdd:cd03256 145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInrEEGITVIVSLHQVDLAReYADRIVGLKDGRIV 224
|
....
gi 1005434824 756 ERGT 759
Cdd:cd03256 225 FDGP 228
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
541-761 |
3.05e-31 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 122.43 E-value: 3.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSrpdSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIG------RTNLAELDLFW 614
Cdd:PRK11124 3 IQLNGINCFYGA---HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAgnhfdfSKTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 615 LRRKIALVSQEPVLFA-TTIAANIAygcEA-------TQEEIEKAAEQANAHNFIASFEEGYQTQvgergvkLSGGQKQR 686
Cdd:PRK11124 80 LRRNVGMVFQQYNLWPhLTVQQNLI---EApcrvlglSKDQALARAEKLLERLRLKPYADRFPLH-------LSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 687 VAIARALLMNPDVLLLDEATSALDAE-SEHFVKEAIDRAMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHE 761
Cdd:PRK11124 150 VAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARKtASRVVYMENGHIVEQGDAS 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
558-765 |
3.42e-31 |
|
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: 124.78 E-value: 3.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPK---SGVISIGRTNLAELD---LFWLR-RKIALVSQE----- 625
Cdd:COG0444 20 AVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSekeLRKIRgREIQMIFQDpmtsl 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 626 -PVLfatTIAANIA----YGCEATQEEIEKAAEQA-------NAHNFIASF--EegyqtqvgergvkLSGGQKQRVAIAR 691
Cdd:COG0444 100 nPVM---TVGDQIAeplrIHGGLSKAEARERAIELlervglpDPERRLDRYphE-------------LSGGMRQRVMIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 692 ALLMNPDVLLLDEATSALDAESEhfvKEAID-----RAMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHETLLA 765
Cdd:COG0444 164 ALALEPKLLIADEPTTALDVTIQ---AQILNllkdlQRELGLAILFITHDLGVVAEiADRVAVMYAGRIVEEGPVEELFE 240
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
561-763 |
4.96e-31 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 124.46 E-value: 4.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 561 GMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISI-GR--TNLAELDLFWLRRKIALVSQEPvlFAT-----T 632
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFdGQdiTGLSGRELRPLRRRMQMVFQDP--YASlnprmT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 633 IAANIAYGCEAtQEEIEKAAEQANAHNFIAsfeegyqtQVG-----------ErgvkLSGGQKQRVAIARALLMNPDVLL 701
Cdd:COG4608 114 VGDIIAEPLRI-HGLASKAERRERVAELLE--------LVGlrpehadryphE----FSGGQRQRIGIARALALNPKLIV 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1005434824 702 LDEATSALDAesehfvkeAIdRAMV-----------NRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHETL 763
Cdd:COG4608 181 CDEPVSALDV--------SI-QAQVlnlledlqdelGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRDEL 245
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
239-792 |
5.46e-31 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 131.25 E-value: 5.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 239 SQIAAPYFFGRVIQaSMEEGMSHLnKTIVLLSLIYLAGALAALVRSWLFTLAGqRLVARIRKQLFASVVEQEVAFFDSNR 318
Cdd:PLN03232 316 SQFVGPVILSHLLQ-SMQEGDPAW-VGYVYAFLIFFGVTFGVLCESQYFQNVG-RVGFRLRSTLVAAIFHKSLRLTHEAR 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 319 ----TGELINRLSSDTQVIQN-----------ALTVNVSMLLRYiiQIIGSLAFMFSLsakltgVLISVVPIVGIgaqry 383
Cdd:PLN03232 393 knfaSGKVTNMITTDANALQQiaeqlhglwsaPFRIIVSMVLLY--QQLGVASLFGSL------ILFLLIPLQTL----- 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 384 gsFVQGLRKRFQDELA---AASSTAEEAIANIRTVRSFSQErKSMNSYDTDI---DKSYKSGAKL--ALASGFFNG---V 452
Cdd:PLN03232 460 --IVRKMRKLTKEGLQwtdKRVGIINEILASMDTVKCYAWE-KSFESRIQGIrneELSWFRKAQLlsAFNSFILNSipvV 536
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 453 IGIIGQGAVVLVlwyGGSLVNKHELDVGILTAFMLYTLNvaMAFAFLSsvygdfmQAVGASV---RMFELM---DRI--P 524
Cdd:PLN03232 537 VTLVSFGVFVLL---GGDLTPARAFTSLSLFAVLRSPLN--MLPNLLS-------QVVNANVslqRIEELLlseERIlaQ 604
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 525 SIDLEGGKKlstvnqVIQFQDVYFAYPSRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLerfydpksgvisIGR 604
Cdd:PLN03232 605 NPPLQPGAP------AISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAM------------LGE 666
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 605 TNLAELDLFWLRRKIALVSQEPVLFATTIAANIAYGCEATQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGGQK 684
Cdd:PLN03232 667 LSHAETSSVVIRGSVAYVPQVSWIFNATVRENILFGSDFESERYWRAIDVTALQHDLDLLPGRDLTEIGERGVNISGGQK 746
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 685 QRVAIARALLMNPDVLLLDEATSALDAESEHFVKEA-IDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHETL 763
Cdd:PLN03232 747 QRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFDScMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAEL 826
|
570 580 590
....*....|....*....|....*....|.
gi 1005434824 764 LAKAGVYKKLVLR--QLSVSQHENLSAGDLD 792
Cdd:PLN03232 827 SKSGSLFKKLMENagKMDATQEVNTNDENIL 857
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
550-734 |
7.60e-31 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 119.84 E-value: 7.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 550 YPSRPDsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLA--ELDLFWLRRKIALVSQEP- 626
Cdd:TIGR01166 1 YPGGPE--VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDysRKGLLERRQRVGLVFQDPd 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 627 -VLFATTIAANIAYG---CEATQEEIEKAAEQANAHNFIASFEEGYQTQvgergvkLSGGQKQRVAIARALLMNPDVLLL 702
Cdd:TIGR01166 79 dQLFAADVDQDVAFGplnLGLSEAEVERRVREALTAVGASGLRERPTHC-------LSGGEKKRVAIAGAVAMRPDVLLL 151
|
170 180 190
....*....|....*....|....*....|..
gi 1005434824 703 DEATSALDAESEHFVKEAIDRAMVNRTVLVIA 734
Cdd:TIGR01166 152 DEPTAGLDPAGREQMLAILRRLRAEGMTVVIS 183
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
271-759 |
9.62e-31 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 130.67 E-value: 9.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 271 LIYLAGALAALVRSWLFTLAGQRLVARIRKQLFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQ 350
Cdd:PTZ00243 1006 GIVLLGTFSVPLRFFLSYEAMRRGSRNMHRDLLRSVSRGTMSFFDTTPLGRILNRFSRDIDILDNTLPMSYLYLLQCLFS 1085
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 351 IIGSLAFMFslsAKLTGVLISVVPIVGIG---AQRYGSFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNS 427
Cdd:PTZ00243 1086 ICSSILVTS---ASQPFVLVALVPCGYLYyrlMQFYNSANREIRRIKSVAKSPVFTLLEEALQGSATITAYGKAHLVMQE 1162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 428 YDTDIDKSYKS-----------GAKLALASGFFNGVIGIIGQGAVVLVlwyggslVNKHE-------LDVGILTAFMLYT 489
Cdd:PTZ00243 1163 ALRRLDVVYSCsylenvanrwlGVRVEFLSNIVVTVIALIGVIGTMLR-------ATSQEiglvslsLTMAMQTTATLNW 1235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 490 L--NVAMAFAFLSSV-----YGD-----FMQAVGASVRMFE-----LMDRIPSIDLEGGKKLSTVNQVIQ-----FQDVY 547
Cdd:PTZ00243 1236 LvrQVATVEADMNSVerllyYTDevpheDMPELDEEVDALErrtgmAADVTGTVVIEPASPTSAAPHPVQagslvFEGVQ 1315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 548 FAY----PSrpdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIALVS 623
Cdd:PTZ00243 1316 MRYreglPL-----VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIP 1390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 624 QEPVLFATTIAANIAYGCEATQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALLM-NPDVLLL 702
Cdd:PTZ00243 1391 QDPVLFDGTVRQNVDPFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKkGSGFILM 1470
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 703 DEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGT 759
Cdd:PTZ00243 1471 DEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGS 1527
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
540-766 |
1.21e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 122.15 E-value: 1.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYPSRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKI 619
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 620 ALVSQEP--VLFATTIAANIAYGCE---ATQEEIEKAAEQANAHNFIASFEEgyqtqvgERGVKLSGGQKQRVAIARALL 694
Cdd:PRK13650 84 GMVFQNPdnQFVGATVEDDVAFGLEnkgIPHEEMKERVNEALELVGMQDFKE-------REPARLSGGQKQRVAIAGAVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1005434824 695 MNPDVLLLDEATSALDAESEHFVKEAID--RAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHETLLAK 766
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKgiRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSR 230
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
540-759 |
1.55e-30 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 120.48 E-value: 1.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYPSrpDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAEL---DLFWLR 616
Cdd:TIGR02315 1 MLEVENLSKVYPN--GKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLrgkKLRKLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 617 RKIALVSQEPVLFA-TTIAANIAYGceatqeeiekaaeQANAHNFIASF-----EEGYQ------TQVG------ERGVK 678
Cdd:TIGR02315 79 RRIGMIFQHYNLIErLTVLENVLHG-------------RLGYKPTWRSLlgrfsEEDKEralsalERVGladkayQRADQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 679 LSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRamVNR----TVLVIAHRLSTVRN-ADQVLVIDKGH 753
Cdd:TIGR02315 146 LSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKR--INKedgiTVIINLHQVDLAKKyADRIVGLKAGE 223
|
....*.
gi 1005434824 754 IVERGT 759
Cdd:TIGR02315 224 IVFDGA 229
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
537-782 |
1.60e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 121.83 E-value: 1.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 537 VNQVIQFQDVYFAYPSRPDSdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKS---GVISIGRTNLAELDLF 613
Cdd:PRK13640 2 KDNIVEFKHVSFTYPDSKKP-ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 614 WLRRKIALVSQEP--VLFATTIAANIAYGCEATQ---EE----IEKAAEQANAHNFIASfEEGYqtqvgergvkLSGGQK 684
Cdd:PRK13640 81 DIREKVGIVFQNPdnQFVGATVGDDVAFGLENRAvprPEmikiVRDVLADVGMLDYIDS-EPAN----------LSGGQK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 685 QRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMV--NRTVLVIAHRLSTVRNADQVLVIDKGHIVERGT--- 759
Cdd:PRK13640 150 QRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKknNLTVISITHDIDEANMADQVLVLDDGKLLAQGSpve 229
|
250 260 270
....*....|....*....|....*....|....
gi 1005434824 760 ---HETLLAKAG-----VYK---KLVLRQLSVSQ 782
Cdd:PRK13640 230 ifsKVEMLKEIGldipfVYKlknKLKEKGISVPQ 263
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
541-711 |
6.27e-30 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 121.72 E-value: 6.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKST---VISLLErfyDPKSGVISI-GR--TNLAELDlfw 614
Cdd:COG3839 4 LELENVSKSYGGVE---ALKDIDLDIEDGEFLVLLGPSGCGKSTllrMIAGLE---DPTSGEILIgGRdvTDLPPKD--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 615 lrRKIALVSQEPVLF-ATTIAANIAYGCEA---TQEEIEKAAEQAnAHnfiasfeegyQTQVGE---RGVK-LSGGQKQR 686
Cdd:COG3839 75 --RNIAMVFQSYALYpHMTVYENIAFPLKLrkvPKAEIDRRVREA-AE----------LLGLEDlldRKPKqLSGGQRQR 141
|
170 180
....*....|....*....|....*
gi 1005434824 687 VAIARALLMNPDVLLLDEATSALDA 711
Cdd:COG3839 142 VALGRALVREPKVFLLDEPLSNLDA 166
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
481-773 |
8.24e-30 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 127.55 E-value: 8.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 481 ILTAFMLYT-----LNVAMAFAFLS--SV--YGDFM------QAVGASV---RMFELM---DRI--PSIDLEGGKKlstv 537
Cdd:PLN03130 538 TVVSFGVFTllggdLTPARAFTSLSlfAVlrFPLFMlpnlitQAVNANVslkRLEELLlaeERVllPNPPLEPGLP---- 613
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 538 nqVIQFQDVYFAYPSRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIgrtnlaeldlfwLRR 617
Cdd:PLN03130 614 --AISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV------------IRG 679
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 618 KIALVSQEPVLFATTIAANIAYGCEATQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALLMNP 697
Cdd:PLN03130 680 TVAYVPQVSWIFNATVRDNILFGSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNS 759
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 698 DVLLLDEATSALDAESEHFVKEA-IDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHETLLAKAGVYKKL 773
Cdd:PLN03130 760 DVYIFDDPLSALDAHVGRQVFDKcIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMIKEEGTYEELSNNGPLFQKL 836
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
558-767 |
9.89e-30 |
|
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: 118.21 E-value: 9.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLfwLRRKIALVSQEPVLFA-TTIAAN 636
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP--EKRDISYVPQNYALFPhMTVYKN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 637 IAYGC---EATQEEIEKAAEQanahnfIASFEeGYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAES 713
Cdd:cd03299 92 IAYGLkkrKVDKKEIERKVLE------IAEML-GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 714 EHFVKEAIDRAM--VNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHETLLAKA 767
Cdd:cd03299 165 KEKLREELKKIRkeFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKP 221
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
537-767 |
1.46e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 119.04 E-value: 1.46e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 537 VNQVIQFQDVYFAYPSRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLR 616
Cdd:PRK13642 1 MNKILEVENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 617 RKIALVSQEP--VLFATTIAANIAYGCE----ATQEEIEKAAEQANAHNFIasfeeGYQTQVGERgvkLSGGQKQRVAIA 690
Cdd:PRK13642 81 RKIGMVFQNPdnQFVGATVEDDVAFGMEnqgiPREEMIKRVDEALLAVNML-----DFKTREPAR---LSGGQKQRVAVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 691 RALLMNPDVLLLDEATSALD----AESEHFVKEAIDRAMVnrTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHETLLAK 766
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQL--TVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFAT 230
|
.
gi 1005434824 767 A 767
Cdd:PRK13642 231 S 231
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
475-752 |
2.80e-29 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 123.76 E-value: 2.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 475 HELDVGILT----AFMlytlNVAMAFAFLSSVYGDF--MQAVGASVRMF-ELMDRIPSIDLEGGKKLSTVNQVIQFQDVY 547
Cdd:COG4178 294 GEITLGGLMqaasAFG----QVQGALSWFVDNYQSLaeWRATVDRLAGFeEALEAADALPEAASRIETSEDGALALEDLT 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 548 FAypsRPDSDVL-KGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGviSIGRTNLAELdLFwlrrkialVSQEP 626
Cdd:COG4178 370 LR---TPDGRPLlEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSG--RIARPAGARV-LF--------LPQRP 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 627 VLFATTIAANIAYGCEATQ---EEIEKAAEQANAHNFIASFEEgyqtqVGERGVKLSGGQKQRVAIARALLMNPDVLLLD 703
Cdd:COG4178 436 YLPLGTLREALLYPATAEAfsdAELREALEAVGLGHLAERLDE-----EADWDQVLSLGEQQRLAFARLLLHKPDWLFLD 510
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1005434824 704 EATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKG 752
Cdd:COG4178 511 EATSALDEENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
541-759 |
2.85e-29 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 116.67 E-value: 2.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLfwLRRKIA 620
Cdd:cd03296 3 IEVRNVSKRFGDFV---ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV--QERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 621 LVSQEPVLFA-TTIAANIAYGCEA--TQEEIEKAAEQANAHNFI-----ASFEEGYQTQvgergvkLSGGQKQRVAIARA 692
Cdd:cd03296 78 FVFQHYALFRhMTVFDNVAFGLRVkpRSERPPEAEIRAKVHELLklvqlDWLADRYPAQ-------LSGGQRQRVALARA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1005434824 693 LLMNPDVLLLDEATSALDA----ESEHFVKEAIDRAMVNrTVLVIAHRLSTVRNADQVLVIDKGHIVERGT 759
Cdd:cd03296 151 LAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHVT-TVFVTHDQEEALEVADRVVVMNKGRIEQVGT 220
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
558-759 |
2.93e-29 |
|
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: 116.57 E-value: 2.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFwlRRKIALVSQEPVLFA-TTIAAN 636
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVFQNYALFPhLTVFEN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 637 IAYGCE---ATQEEIEKAAEQANAHNFIASFEEGYQTQvgergvkLSGGQKQRVAIARALLMNPDVLLLDEATSALDAES 713
Cdd:cd03300 93 IAFGLRlkkLPKAEIKERVAEALDLVQLEGYANRKPSQ-------LSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1005434824 714 EHFVKEAIDR--AMVNRTVLVIAHRLS---TVrnADQVLVIDKGHIVERGT 759
Cdd:cd03300 166 RKDMQLELKRlqKELGITFVFVTHDQEealTM--SDRIAVMNKGKIQQIGT 214
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
538-767 |
4.63e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 117.16 E-value: 4.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 538 NQVIQFQDVYFAYPSrPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRR 617
Cdd:PRK13648 5 NSIIVFKNVSFQYQS-DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 618 KIALVSQEP--VLFATTIAANIAYGCE-------ATQEEIEKAAEQANAHNFiasfeEGYQTQvgergvKLSGGQKQRVA 688
Cdd:PRK13648 84 HIGIVFQNPdnQFVGSIVKYDVAFGLEnhavpydEMHRRVSEALKQVDMLER-----ADYEPN------ALSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 689 IARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNR--TVLVIAHRLSTVRNADQVLVIDKGHIVERGTHETLLAK 766
Cdd:PRK13648 153 IAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDH 232
|
.
gi 1005434824 767 A 767
Cdd:PRK13648 233 A 233
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
537-769 |
7.76e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 116.76 E-value: 7.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 537 VNQVIQFQDVYFAYPSrpDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLR 616
Cdd:PRK13647 1 MDNIIEVEDLHFRYKD--GTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 617 RKIALVSQEP--VLFATTIAANIAYG---CEATQEEIEKAAEQANAHNFIASFEEgyqtqvgERGVKLSGGQKQRVAIAR 691
Cdd:PRK13647 79 SKVGLVFQDPddQVFSSTVWDDVAFGpvnMGLDKDEVERRVEEALKAVRMWDFRD-------KPPYHLSYGQKKRVAIAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 692 ALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVN-RTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHETLLAKAGV 769
Cdd:PRK13647 152 VLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLTDEDIV 231
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
539-758 |
1.74e-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: 113.03 E-value: 1.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 539 QVIQFQDVYFAYPSRPDS---DVLKGMSFELKPGETVALVGPSGGGKSTVISLL--ERFYDPKSGVISIGRTNLaelDLF 613
Cdd:cd03213 2 VTLSFRNLTVTVKSSPSKsgkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPL---DKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 614 WLRRKIALVSQEPVLFAT-TIAANIAYgceatqeeiekAAEQanahnfiasfeegyqtqvgeRGvkLSGGQKQRVAIARA 692
Cdd:cd03213 79 SFRKIIGYVPQDDILHPTlTVRETLMF-----------AAKL--------------------RG--LSGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005434824 693 LLMNPDVLLLDEATSALDAESEHFVKEAIDR-AMVNRTVLVIAHRLST--VRNADQVLVIDKGHIVERG 758
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
541-754 |
1.90e-28 |
|
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: 113.66 E-value: 1.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPsrPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELD---LFWLRR 617
Cdd:cd03292 1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraIPYLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 618 KIALVSQEPVLFAT-TIAANIAYGCEATQE---EIEKAAEQANAHNFIASFEEGYQTQvgergvkLSGGQKQRVAIARAL 693
Cdd:cd03292 79 KIGVVFQDFRLLPDrNVYENVAFALEVTGVpprEIRKRVPAALELVGLSHKHRALPAE-------LSGGEQQRVAIARAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005434824 694 LMNPDVLLLDEATSALDAESEHFVKEAIDRamVNR---TVLVIAHRLSTVRN-ADQVLVIDKGHI 754
Cdd:cd03292 152 VNSPTILIADEPTGNLDPDTTWEIMNLLKK--INKagtTVVVATHAKELVDTtRHRVIALERGKL 214
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
545-755 |
1.91e-28 |
|
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: 113.51 E-value: 1.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 545 DVYFAYpsRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLfwlRRKIALVSQ 624
Cdd:cd03226 4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKER---RKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 625 EP--VLFATTIAANIAYGCEATQEEIEKAAEQANAHNfIASFEEGYQTQvgergvkLSGGQKQRVAIARALLMNPDVLLL 702
Cdd:cd03226 79 DVdyQLFTDSVREELLLGLKELDAGNEQAETVLKDLD-LYALKERHPLS-------LSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 703 DEATSALDAESEHFVKEAIDR-AMVNRTVLVIAHR---LSTVrnADQVLVIDKGHIV 755
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDyefLAKV--CDRVLLLANGAIV 205
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
540-776 |
2.59e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 115.17 E-value: 2.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYPSrpDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLA--ELDLFWLRR 617
Cdd:PRK13639 1 ILETRDLKYSYPD--GTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 618 KIALVSQEP--VLFATTIAANIAYG---CEATQEEIEKAAEQAnahnFIASFEEGYQTQVGERgvkLSGGQKQRVAIARA 692
Cdd:PRK13639 79 TVGIVFQNPddQLFAPTVEEDVAFGplnLGLSKEEVEKRVKEA----LKAVGMEGFENKPPHH---LSGGQKKRVAIAGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 693 LLMNPDVLLLDEATSALD----AESEHFVKEAIDRAMvnrTVLVIAHRLSTV-RNADQVLVIDKGHIVERGTHETLLAKA 767
Cdd:PRK13639 152 LAMKPEIIVLDEPTSGLDpmgaSQIMKLLYDLNKEGI---TIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
....*....
gi 1005434824 768 GVYKKLVLR 776
Cdd:PRK13639 229 ETIRKANLR 237
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
540-764 |
3.58e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 113.65 E-value: 3.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDV--YFAypsrpDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIG--RTNLAELDLFWL 615
Cdd:PRK09493 1 MIEFKNVskHFG-----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDglKVNDPKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 616 RRKIALVSQEPVLFATTIA-ANIAYGC----EATQEEIEKAAEQANAHNFIASFEEGYQTQvgergvkLSGGQKQRVAIA 690
Cdd:PRK09493 76 RQEAGMVFQQFYLFPHLTAlENVMFGPlrvrGASKEEAEKQARELLAKVGLAERAHHYPSE-------LSGGQQQRVAIA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1005434824 691 RALLMNPDVLLLDEATSALDAESEHFV-KEAIDRAMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHETLL 764
Cdd:PRK09493 149 RALAVKPKLMLFDEPTSALDPELRHEVlKVMQDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVLI 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
555-765 |
3.82e-28 |
|
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: 112.91 E-value: 3.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 555 DSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFW-LRRKIALVSQEPVLFAT-T 632
Cdd:cd03224 12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIGYVPEGRRIFPElT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 633 IAANIAYGCEATQEEIEKAaeqanahnfiaSFEEGYQ------TQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEAT 706
Cdd:cd03224 92 VEENLLLGAYARRRAKRKA-----------RLERVYElfprlkERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1005434824 707 SALdaeSEHFVKE---AIDRamVNR---TVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHETLLA 765
Cdd:cd03224 161 EGL---APKIVEEifeAIRE--LRDegvTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELLA 221
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
541-759 |
5.55e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 114.37 E-value: 5.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAY-PSRP-DSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAE--LDLFWLR 616
Cdd:PRK13637 3 IKIENLTHIYmEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkVKLSDIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 617 RKIALVSQEP--VLFATTIAANIAYGCE---ATQEEIEKAAEQAnaHNFIASFEEGYQTQvgeRGVKLSGGQKQRVAIAR 691
Cdd:PRK13637 83 KKVGLVFQYPeyQLFEETIEKDIAFGPInlgLSEEEIENRVKRA--MNIVGLDYEDYKDK---SPFELSGGQKRRVAIAG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1005434824 692 ALLMNPDVLLLDEATSALDAESEHFVKEAID--RAMVNRTVLVIAHRLSTV-RNADQVLVIDKGHIVERGT 759
Cdd:PRK13637 158 VVAMEPKILILDEPTAGLDPKGRDEILNKIKelHKEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGT 228
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
541-764 |
6.32e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 113.29 E-value: 6.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIA 620
Cdd:COG4559 2 LEAENLSVRLGGRT---LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 621 LVSQEPVL-FATTIAANIA---YGCEATQEEIEKAAEQANAHNFIASFEEG-YQTqvgergvkLSGGQKQRVAIARAL-- 693
Cdd:COG4559 79 VLPQHSSLaFPFTVEEVVAlgrAPHGSSAAQDRQIVREALALVGLAHLAGRsYQT--------LSGGEQQRVQLARVLaq 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 694 LMNPD-----VLLLDEATSALD-AESEHFVKEAIDRAMVNRTVLVIAHRLS-TVRNADQVLVIDKGHIVERGTHETLL 764
Cdd:COG4559 151 LWEPVdggprWLFLDEPTSALDlAHQHAVLRLARQLARRGGGVVAVLHDLNlAAQYADRILLLHQGRLVAQGTPEEVL 228
|
|
| ABC_6TM_Rv0194_D2_like |
cd18546 |
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ... |
226-516 |
9.15e-28 |
|
Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and similar proteins; This group includes the six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ATP-binding/permease protein Rv0194 from Mycobacterium tuberculosis and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349990 [Multi-domain] Cd Length: 292 Bit Score: 114.12 E-value: 9.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 226 LFIASVALLASSGSQIAAPYFFGRVIqasmEEGMSHLNKTIVLL-SLIYLAGALAALVRSWLFTL----AGQRLVARIRK 300
Cdd:cd18546 1 LALALLLVVVDTAASLAGPLLVRYGI----DSGVRAGDLGVLLLaAAAYLAVVLAGWVAQRAQTRltgrTGERLLYDLRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 301 QLFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGA 380
Cdd:cd18546 77 RVFAHLQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALAT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 381 ---QRYGSFVQGL-RKR-------FQDelaaasstaeeAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFF 449
Cdd:cd18546 157 rwfRRRSSRAYRRaRERiaavnadLQE-----------TLAGIRVVQAFRRERRNAERFAELSDDYRDARLRAQRLVAIY 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 450 NGVIGIIGQGAVVLVLWYGGSLVNKHELDVGILTAFMLYtlnVAMAFA---FLSSVYGDFMQAVGASVRM 516
Cdd:cd18546 226 FPGVELLGNLATAAVLLVGAWRVAAGTLTVGVLVAFLLY---LRRFFApiqQLSQVFDSYQQARAALEKI 292
|
|
| ABC_6TM_exporter_like |
cd18778 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
226-488 |
1.01e-27 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 113.79 E-value: 1.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 226 LFIASVALLASSGSQIAAPYFFGRVIQ--ASMEEGMSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQLF 303
Cdd:cd18778 1 LILTLLCALLSTLLGLVPPWLIRELVDlvTIGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 304 ASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAQRY 383
Cdd:cd18778 81 DKLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 384 GSFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQGAVVL 463
Cdd:cd18778 161 SKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLGTVL 240
|
250 260
....*....|....*....|....*
gi 1005434824 464 VLWYGGSLVNKHELDVGILTAFMLY 488
Cdd:cd18778 241 VLGFGGRLVLAGELTIGDLVAFLLY 265
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
559-765 |
1.26e-27 |
|
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: 118.25 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 559 LKGMSFELKPGETVALVGPSGGGKST----VISLLerfydPKSGVISIGRTNLAELD---LFWLRRKIALVSQEPvlFAT 631
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-----PSEGEIRFDGQDLDGLSrraLRPLRRRMQVVFQDP--FGS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 632 -----TIAANIAYGCEATQEEIEKAAEQANAhnfIASFEEgyqtqVG-----------ErgvkLSGGQKQRVAIARALLM 695
Cdd:COG4172 375 lsprmTVGQIIAEGLRVHGPGLSAAERRARV---AEALEE-----VGldpaarhryphE----FSGGQRQRIAIARALIL 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 696 NPDVLLLDEATSALDaesehfvkeaidramvnRTV-------------------LVIAHRLSTVRN-ADQVLVIDKGHIV 755
Cdd:COG4172 443 EPKLLVLDEPTSALD-----------------VSVqaqildllrdlqrehglayLFISHDLAVVRAlAHRVMVMKDGKVV 505
|
250
....*....|
gi 1005434824 756 ERGTHETLLA 765
Cdd:COG4172 506 EQGPTEQVFD 515
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
541-758 |
1.61e-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: 111.05 E-value: 1.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPdsdvlkgMSFELK--PGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLfwLRRK 618
Cdd:cd03298 1 VRLDKIRFSYGEQP-------MHFDLTfaQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPP--ADRP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 619 IALVSQEPVLFA-TTIAANIAYGC-------EATQEEIEKAAEQANAHNFIASFEEgyqtqvgergvKLSGGQKQRVAIA 690
Cdd:cd03298 72 VSMLFQENNLFAhLTVEQNVGLGLspglkltAEDRQAIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALA 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1005434824 691 RALLMNPDVLLLDEATSALD----AESEHFVKEAidRAMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERG 758
Cdd:cd03298 141 RVLVRDKPVLLLDEPFAALDpalrAEMLDLVLDL--HAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
541-780 |
2.11e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 112.81 E-value: 2.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAY-PSRP-DSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLA----ELDLFW 614
Cdd:PRK13634 3 ITFQKVEHRYqYKTPfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkkNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 615 LRRKIALVSQ--EPVLFATTIAANIAYGCE---ATQEEIEKAAEQANAhnfiasfEEGYQTQVGERG-VKLSGGQKQRVA 688
Cdd:PRK13634 83 LRKKVGIVFQfpEHQLFEETVEKDICFGPMnfgVSEEDAKQKAREMIE-------LVGLPEELLARSpFELSGGQMRRVA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 689 IARALLMNPDVLLLDEATSALDAESEHFVKEAIDR--AMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHETLLA 765
Cdd:PRK13634 156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPREIFA 235
|
250
....*....|....*
gi 1005434824 766 KAgvyKKLVLRQLSV 780
Cdd:PRK13634 236 DP---DELEAIGLDL 247
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
540-764 |
2.31e-27 |
|
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: 111.71 E-value: 2.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSG-VISI-GRTnLAELDLFWLRR 617
Cdd:COG1119 3 LLELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLfGER-RGGEDVWELRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 618 KIALVSQEpvlFATTIAANI---------AYG-----CEATQEEIEKAAEQANAHNFIASFEEGYQTqvgergvkLSGGQ 683
Cdd:COG1119 79 RIGLVSPA---LQLRFPRDEtvldvvlsgFFDsiglyREPTDEQRERARELLELLGLAHLADRPFGT--------LSQGE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 684 KQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVN--RTVLVIAHRLSTVRNA-DQVLVIDKGHIVERGTH 760
Cdd:COG1119 148 QRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAGPK 227
|
....
gi 1005434824 761 ETLL 764
Cdd:COG1119 228 EEVL 231
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
555-763 |
2.58e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 114.05 E-value: 2.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 555 DSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLfwLRRKIALVSQEPVLFA-TTI 633
Cdd:PRK11432 18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSI--QQRDICMVFQSYALFPhMSL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 634 AANIAYGCE---ATQEEIEKAAEQANAHNFIASFEEGYQTQVgergvklSGGQKQRVAIARALLMNPDVLLLDEATSALD 710
Cdd:PRK11432 96 GENVGYGLKmlgVPKEERKQRVKEALELVDLAGFEDRYVDQI-------SGGQQQRVALARALILKPKVLLFDEPLSNLD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1005434824 711 AESEHFVKEAIdRAM---VNRTVLVIAHRLS---TVrnADQVLVIDKGHIVERGTHETL 763
Cdd:PRK11432 169 ANLRRSMREKI-RELqqqFNITSLYVTHDQSeafAV--SDTVIVMNKGKIMQIGSPQEL 224
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
559-766 |
3.17e-27 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 113.14 E-value: 3.17e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 559 LKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELD---LFWLRRKIALVSQ----------- 624
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADpeaQKLLRQKIQIVFQnpygslnprkk 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 625 ------EPVLFATTIAAniaygceatQEEIEKAAEQanahnfiasfeegyQTQVGERGVK-------LSGGQKQRVAIAR 691
Cdd:PRK11308 111 vgqileEPLLINTSLSA---------AERREKALAM--------------MAKVGLRPEHydryphmFSGGQRQRIAIAR 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 692 ALLMNPDVLLLDEATSALDAesehfvkeAIdRAMV-----------NRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGT 759
Cdd:PRK11308 168 ALMLDPDVVVADEPVSALDV--------SV-QAQVlnlmmdlqqelGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGT 238
|
....*..
gi 1005434824 760 HETLLAK 766
Cdd:PRK11308 239 KEQIFNN 245
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
563-758 |
4.34e-27 |
|
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: 109.69 E-value: 4.34e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 563 SFELK-----PGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAE----LDLFWLRRKIALVSQEPVLFA-TT 632
Cdd:cd03297 12 DFTLKidfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkINLPPQQRKIGLVFQQYALFPhLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 633 IAANIAYGCEATQEEIEKAAEQAnahnFIASFEegyQTQVGERGV-KLSGGQKQRVAIARALLMNPDVLLLDEATSALDA 711
Cdd:cd03297 92 VRENLAFGLKRKRNREDRISVDE----LLDLLG---LDHLLNRYPaQLSGGEKQRVALARALAAQPELLLLDEPFSALDR 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1005434824 712 ES----EHFVKEAidRAMVNRTVLVIAHRLSTV-RNADQVLVIDKGHIVERG 758
Cdd:cd03297 165 ALrlqlLPELKQI--KKNLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
563-765 |
1.20e-26 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 112.12 E-value: 1.20e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 563 SFELKPGETVALVGPSGGGKSTVISL---LERfydPKSGVISIG---------RTNL-AEldlfwlRRKIALVSQEPVLF 629
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGgevlqdsarGIFLpPH------RRRIGYVFQEARLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 630 AT-TIAANIAYGCeatqeeieKAAEQANAHnfiASFEEgyqtqV----G-----ERGV-KLSGGQKQRVAIARALLMNPD 698
Cdd:COG4148 90 PHlSVRGNLLYGR--------KRAPRAERR---ISFDE-----VvellGighllDRRPaTLSGGERQRVAIGRALLSSPR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1005434824 699 VLLLDEATSALDAESehfvKEAI--------DRamVNRTVLVIAHRLSTV-RNADQVLVIDKGHIVERGTHETLLA 765
Cdd:COG4148 154 LLLMDEPLAALDLAR----KAEIlpylerlrDE--LDIPILYVSHSLDEVaRLADHVVLLEQGRVVASGPLAEVLS 223
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
540-764 |
1.33e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 109.48 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKI 619
Cdd:PRK13548 2 MLEARNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 620 ALVSQEPVL-FATTIAANIAYG-------CEATQEEIEKAAEQANAHNFIASFeegYQTqvgergvkLSGGQKQRVAIAR 691
Cdd:PRK13548 79 AVLPQHSSLsFPFTVEEVVAMGraphglsRAEDDALVAAALAQVDLAHLAGRD---YPQ--------LSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 692 AL--LMNPD----VLLLDEATSALD-AESEHFVKEAIDRAMV-NRTVLVIAHRLS-TVRNADQVLVIDKGHIVERGTHET 762
Cdd:PRK13548 148 VLaqLWEPDgpprWLLLDEPTSALDlAHQHHVLRLARQLAHErGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAE 227
|
..
gi 1005434824 763 LL 764
Cdd:PRK13548 228 VL 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
558-759 |
1.83e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 111.10 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFW----------------LRRKIAL 621
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHelitnpyskkiknfkeLRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 622 VSQEP--VLFATTIAANIAYGCEATQEEIEKAAEQANAHNFIASFEEGYQtqvgERG-VKLSGGQKQRVAIARALLMNPD 698
Cdd:PRK13631 121 VFQFPeyQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSYL----ERSpFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1005434824 699 VLLLDEATSALDAESEHFVKEAI-DRAMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGT 759
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLIlDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTGT 259
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
562-765 |
2.42e-26 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 108.13 E-value: 2.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 562 MSFEL--KPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIG-----RTNLAeldlfwlRRKIALVSQEPVLFA-TTI 633
Cdd:PRK10771 16 MRFDLtvERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNgqdhtTTPPS-------RRPVSMLFQENNLFShLTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 634 AANIAYGC-------EATQEEIEKAAEQANAHNFIASFEEgyqtqvgergvKLSGGQKQRVAIARALLMNPDVLLLDEAT 706
Cdd:PRK10771 89 AQNIGLGLnpglklnAAQREKLHAIARQMGIEDLLARLPG-----------QLSGGQRQRVALARCLVREQPILLLDEPF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1005434824 707 SALDAESEHFVKEAIDRAMVNR--TVLVIAHRLS-TVRNADQVLVIDKGHIVERGTHETLLA 765
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
297-808 |
3.02e-26 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 116.16 E-value: 3.02e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 297 RIRKQLFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLafmFSLSAKLTGVLISVVPIV 376
Cdd:TIGR01271 959 RLHEQMLHSVLQAPMAVLNTMKAGRILNRFTKDMAIIDDMLPLTLFDFIQLTLIVLGAI---FVVSVLQPYIFIAAIPVA 1035
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 377 GIGAQRYGSFVQGLRKRFQDELAAASSTAEEAIANIR---TVRSFSQE-------RKSMNSYdTDIDKSYKSGAKlalas 446
Cdd:TIGR01271 1036 VIFIMLRAYFLRTSQQLKQLESEARSPIFSHLITSLKglwTIRAFGRQsyfetlfHKALNLH-TANWFLYLSTLR----- 1109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 447 gFFNGVIGIIGQGAVVLVLWYGGSLVNKHELDVGILTAFMLYTLNVaMAFAFLSSVYGD-FMQAVGASVRMFELMDRIPS 525
Cdd:TIGR01271 1110 -WFQMRIDIIFVFFFIAVTFIAIGTNQDGEGEVGIILTLAMNILST-LQWAVNSSIDVDgLMRSVSRVFKFIDLPQEEPR 1187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 526 IDLEGGKKLSTVNQVIQFQDVYFAYPSRPDSDV--------------LKGMSFELKPGETVALVGPSGGGKSTVISLLER 591
Cdd:TIGR01271 1188 PSGGGGKYQLSTVLVIENPHAQKCWPSGGQMDVqgltakyteagravLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLR 1267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 592 FYDPKsGVISIGRTNLAELDLFWLRRKIALVSQEPVLFATTIAANIAYGCEATQEEIEKAAEQANAHNFIASFEEGYQTQ 671
Cdd:TIGR01271 1268 LLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLDFV 1346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 672 VGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDK 751
Cdd:TIGR01271 1347 LVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEG 1426
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1005434824 752 GHIVERGTHETLLAKAGVYKKLVLR----QLSVSQHENLSAGDLDPNLLGSEQPSVEEVEE 808
Cdd:TIGR01271 1427 SSVKQYDSIQKLLNETSLFKQAMSAadrlKLFPLHRRNSSKRKPQPKITALREEAEEEVQN 1487
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
552-805 |
4.69e-26 |
|
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: 115.43 E-value: 4.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 552 SRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLerfydpksgvisigrtnLAELDLF----WLRRKIALVSQEPV 627
Cdd:TIGR00957 647 ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSAL-----------------LAEMDKVeghvHMKGSVAYVPQQAW 709
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 628 LFATTIAANIAYGCeATQEEIEKAAEQANAhnFIASFE---EGYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDE 704
Cdd:TIGR00957 710 IQNDSLRENILFGK-ALNEKYYQQVLEACA--LLPDLEilpSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 705 ATSALDAE-SEHFVKEAI--DRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHETLLAKAGVYKKLvLRQLSVS 781
Cdd:TIGR00957 787 PLSAVDAHvGKHIFEHVIgpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEF-LRTYAPD 865
|
250 260
....*....|....*....|....
gi 1005434824 782 QHEnlsaGDLDPNLLGSEQPSVEE 805
Cdd:TIGR00957 866 EQQ----GHLEDSWTALVSGEGKE 885
|
|
| ABC_6TM_Pgp_ABCB1 |
cd18558 |
Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ... |
219-513 |
7.33e-26 |
|
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: 108.90 E-value: 7.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 219 AKPELCVLFIASVALLASSGSQIAAPYFFGRVIQASMEEGMSHLNKTIVLLSLIYLAGAL-AALVRSWLFTLAGQRLVAR 297
Cdd:cd18558 14 LLPAFMVIFGDMTDSFTNGGMTNITGNSSGLNSSAGPFEKLEEEMTLYAYYYLIIGAIVLiTAYIQGSFWGLAAGRQTKK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 298 IRKQLFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVG 377
Cdd:cd18558 94 IRYKFFHAIMRQEIGWFDVNDTGELNTRLADDVSKINEGIGDKIGVIFQNIATFGTGFIIGFIRGWKLTLVILAISPVLG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 378 IGAQRYGSFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIG 457
Cdd:cd18558 174 LSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLEIAKRNGIKKAITFNISMGAAFLLI 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 458 QGAVVLVLWYGGSLVNKHELDVG-ILTAFMLYTLNVAMAFAFLSSVYGdFMQAVGAS 513
Cdd:cd18558 254 YASYALAFWYGTYLVTQQEYSIGeVLTVFFSVLIGAFSAGQQVPSIEA-FANARGAA 309
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
226-765 |
1.17e-25 |
|
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: 112.20 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 226 LFIASVALLASSGSQIAAPYFFGRVIQASMEEGMSHLnKTIVLLSLIYLAGALAALVrswLFTLAGQRLVARIRKQLFAS 305
Cdd:COG4615 15 LLLALLLGLLSGLANAGLIALINQALNATGAALARLL-LLFAGLLVLLLLSRLASQL---LLTRLGQHAVARLRLRLSRR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 306 VVEQEVAFFDSNRTGELINRLSSDTQVIQNALtVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAQRYGS 385
Cdd:COG4615 91 ILAAPLERLERIGAARLLAALTEDVRTISQAF-VRLPELLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLGVAGYRLLVR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 386 FVQGLRKR---FQDELaaasstaeeaianIRTVRSFSQERK--SMNS------YDTDIDKSYKSGAKLALASGFFNGVIG 454
Cdd:COG4615 170 RARRHLRRareAEDRL-------------FKHFRALLEGFKelKLNRrrrrafFDEDLQPTAERYRDLRIRADTIFALAN 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 455 IIGQ----GAVVLVLWYGGSLVnkhELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGASVRMFELMDRIPSIDLEG 530
Cdd:COG4615 237 NWGNllffALIGLILFLLPALG---WADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKIEELELALAAAEPAA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 531 GKKLSTVN----QVIQFQDVYFAYPSRPDSD--VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGR 604
Cdd:COG4615 314 ADAAAPPApadfQTLELRGVTYRYPGEDGDEgfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 605 TNLAELDLFWLRRKIALVSQEPVLFATTiaaniaYGceatqeeIEKAAEQANAHNFIASFEEGYQTQVgERG----VKLS 680
Cdd:COG4615 394 QPVTADNREAYRQLFSAVFSDFHLFDRL------LG-------LDGEADPARARELLERLELDHKVSV-EDGrfstTDLS 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 681 GGQKQRVAIARALLMNPDVLLLDEATSALDAE-SEHFVKEAID--RAMvNRTVLVIAH--RLSTVrnADQVLVIDKGHIV 755
Cdd:COG4615 460 QGQRKRLALLVALLEDRPILVFDEWAADQDPEfRRVFYTELLPelKAR-GKTVIAISHddRYFDL--ADRVLKMDYGKLV 536
|
570
....*....|
gi 1005434824 756 ERGTHETLLA 765
Cdd:COG4615 537 ELTGPAALAA 546
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
540-734 |
1.28e-25 |
|
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: 105.25 E-value: 1.28e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWlRRKI 619
Cdd:COG4133 2 MLEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY-RRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 620 ALVSQEPVLFAT-TIAANIA-----YGCEATQEEIEKAAEQANahnfIASFEEgyqTQVGergvKLSGGQKQRVAIARAL 693
Cdd:COG4133 78 AYLGHADGLKPElTVRENLRfwaalYGLRADREAIDEALEAVG----LAGLAD---LPVR----QLSAGQKRRVALARLL 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1005434824 694 LMNPDVLLLDEATSALDAESEHFVKEAIdRAMVNRTVLVIA 734
Cdd:COG4133 147 LSPAPLWLLDEPFTALDAAGVALLAELI-AAHLARGGAVLL 186
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
543-754 |
3.53e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 110.54 E-value: 3.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 543 FQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRtnlaeldlfwlRRKIALV 622
Cdd:COG0488 1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-----------GLRIGYL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 623 SQEPVLFAT-TIAANIAYG------CEATQEEIEKA--------AEQANAHNFIASF-------------------EEGY 668
Cdd:COG0488 67 PQEPPLDDDlTVLDTVLDGdaelraLEAELEELEAKlaepdedlERLAELQEEFEALggweaearaeeilsglgfpEEDL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 669 QTQVGErgvkLSGGQKQRVAIARALLMNPDVLLLDEATSALDAES----EHFVKeaidramvNR--TVLVIAH-R--LST 739
Cdd:COG0488 147 DRPVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESiewlEEFLK--------NYpgTVLVVSHdRyfLDR 214
|
250
....*....|....*
gi 1005434824 740 VrnADQVLVIDKGHI 754
Cdd:COG0488 215 V--ATRILELDRGKL 227
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
558-765 |
5.21e-25 |
|
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: 110.16 E-value: 5.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKS----TVISLLERFYDPKSGVISIGRTNLAELDLFWLRR----KIALVSQEPV-- 627
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELRRirgnRIAMIFQEPMts 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 628 ---LFatTIAANIAygcEATQ--EEIEKAAEQANAhnfIASFEegyqtQVG----ERGVK-----LSGGQKQRVAIARAL 693
Cdd:COG4172 105 lnpLH--TIGKQIA---EVLRlhRGLSGAAARARA---LELLE-----RVGipdpERRLDayphqLSGGQRQRVMIAMAL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 694 LMNPDVLLLDEATSALDAEsehfVKEAI---------DRAMvnrTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHETL 763
Cdd:COG4172 172 ANEPDLLIADEPTTALDVT----VQAQIldllkdlqrELGM---ALLLITHDLGVVRRfADRVAVMRQGEIVEQGPTAEL 244
|
..
gi 1005434824 764 LA 765
Cdd:COG4172 245 FA 246
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
538-775 |
5.25e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 105.55 E-value: 5.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 538 NQVIQFQDVYFAYPSRPDSD---VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSG-VISIGRTNLAELDLF 613
Cdd:PRK13633 2 NEMIKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGkVYVDGLDTSDEENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 614 WLRRKIALVSQEP--VLFATTIAANIAYGCE---ATQEEIEKAAEQAnahnfiasfeegyQTQVGERGVK------LSGG 682
Cdd:PRK13633 82 DIRNKAGMVFQNPdnQIVATIVEEDVAFGPEnlgIPPEEIRERVDES-------------LKKVGMYEYRrhaphlLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 683 QKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRamVNR----TVLVIAHRLSTVRNADQVLVIDKGHIVERG 758
Cdd:PRK13633 149 QKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKE--LNKkygiTIILITHYMEEAVEADRIIVMDSGKVVMEG 226
|
250
....*....|....*..
gi 1005434824 759 THETLLAKAGVYKKLVL 775
Cdd:PRK13633 227 TPKEIFKEVEMMKKIGL 243
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
540-764 |
5.30e-25 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 104.86 E-value: 5.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYPsrpDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYD--PK---SGVISIGRTNL--AELDL 612
Cdd:PRK14239 5 ILQVSDLSVYYN---KKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIysPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 613 FWLRRKIALVSQEPVLFATTIAANIAYGC--------EATQEEIEKAAEQAnahnfiaSFEEGYQTQVGERGVKLSGGQK 684
Cdd:PRK14239 82 VDLRKEIGMVFQQPNPFPMSIYENVVYGLrlkgikdkQVLDEAVEKSLKGA-------SIWDEVKDRLHDSALGLSGGQQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 685 QRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTV-RNADQVLVIDKGHIVERG-THET 762
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNdTKQM 234
|
..
gi 1005434824 763 LL 764
Cdd:PRK14239 235 FM 236
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
541-758 |
6.30e-25 |
|
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: 103.49 E-value: 6.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFwlRRKIA 620
Cdd:cd03301 1 VELENVTKRFGNVT---ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 621 LVSQEPVLFA-TTIAANIAYGCE---ATQEEIEKAAEQANAHNFIASFEEGYQTQvgergvkLSGGQKQRVAIARALLMN 696
Cdd:cd03301 76 MVFQNYALYPhMTVYDNIAFGLKlrkVPKDEIDERVREVAELLQIEHLLDRKPKQ-------LSGGQRQRVALGRAIVRE 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005434824 697 PDVLLLDEATSALDAESEHFVKEAIDR--AMVNRTVLVIAH-RLSTVRNADQVLVIDKGHIVERG 758
Cdd:cd03301 149 PKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
541-759 |
8.11e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 105.21 E-value: 8.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPS-RP-DSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAEL----DLFW 614
Cdd:PRK13649 3 INLQNVSYTYQAgTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 615 LRRKIALVSQ--EPVLFATTIAANIAYGCE---ATQEEIEKAAEQANAHNFIAsfEEGYQTQVGErgvkLSGGQKQRVAI 689
Cdd:PRK13649 83 IRKKVGLVFQfpESQLFEETVLKDVAFGPQnfgVSQEEAEALAREKLALVGIS--ESLFEKNPFE----LSGGQMRRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005434824 690 ARALLMNPDVLLLDEATSALDA----ESEHFVKEAIDRAMvnrTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGT 759
Cdd:PRK13649 157 AGILAMEPKILVLDEPTAGLDPkgrkELMTLFKKLHQSGM---TIVLVTHLMDDVANyADFVYVLEKGKLVLSGK 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
558-759 |
9.57e-25 |
|
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: 103.67 E-value: 9.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWL-RRKIALVSQEPVLFAT-TIAA 635
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIaRLGIGRTFQIPRLFPElTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 636 NIAYGCEATQEEI--------EKAAEQANAHNFIASF--EEGYQTQVGErgvkLSGGQKQRVAIARALLMNPDVLLLDEA 705
Cdd:cd03219 95 NVMVAAQARTGSGlllararrEEREARERAEELLERVglADLADRPAGE----LSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1005434824 706 TSALDAESEHFVKEAIDR-AMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGT 759
Cdd:cd03219 171 AAGLNPEETEELAELIRElRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGT 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
541-766 |
1.13e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 104.86 E-value: 1.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAY-PSRP-DSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLA----ELDLFW 614
Cdd:PRK13646 3 IRFDNVSYTYqKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 615 LRRKIALVSQ--EPVLFATTIAANIAYGCEATQEEIEKAAEQAnahnFIASFEEGYQTQVGERG-VKLSGGQKQRVAIAR 691
Cdd:PRK13646 83 VRKRIGMVFQfpESQLFEDTVEREIIFGPKNFKMNLDEVKNYA----HRLLMDLGFSRDVMSQSpFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 692 ALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMV--NRTVLVIAHRLSTV-RNADQVLVIDKGHIVERGTHETLLAK 766
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTdeNKTIILVSHDMNEVaRYADEVIVMKEGSIVSQTSPKELFKD 236
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
541-758 |
1.20e-24 |
|
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: 102.66 E-value: 1.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRpdsDVLKGMSFELKPGETvALVGPSGGGKSTVISLLERFYDPKSGVISI-GRTNLAELDlfWLRRKI 619
Cdd:cd03264 1 LQLENLTKRYGKK---RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIdGQDVLKQPQ--KLRRRI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 620 ALVSQEPVLFAT-TIAANIAY-----GCEATQE--EIEKAAEQANAHNFiasfeegyqtqVGERGVKLSGGQKQRVAIAR 691
Cdd:cd03264 75 GYLPQEFGVYPNfTVREFLDYiawlkGIPSKEVkaRVDEVLELVNLGDR-----------AKKKIGSLSGGMRRRVGIAQ 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 692 ALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERG 758
Cdd:cd03264 144 ALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
541-772 |
1.22e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 104.91 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAY-PSRP-DSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISI---------GRTNLAE 609
Cdd:PRK13641 3 IKFENVDYIYsPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIagyhitpetGNKNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 610 LdlfwlRRKIALVSQ--EPVLFATTIAANIAYGCE---ATQEEIEKAAEQanahnFIASFeeGYQTQVGERG-VKLSGGQ 683
Cdd:PRK13641 83 L-----RKKVSLVFQfpEAQLFENTVLKDVEFGPKnfgFSEDEAKEKALK-----WLKKV--GLSEDLISKSpFELSGGQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 684 KQRVAIARALLMNPDVLLLDEATSALDAESEH-FVKEAIDRAMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHE 761
Cdd:PRK13641 151 MRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKeMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIKHASPK 230
|
250
....*....|.
gi 1005434824 762 TLLAKAGVYKK 772
Cdd:PRK13641 231 EIFSDKEWLKK 241
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
540-759 |
1.26e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 104.82 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAY-PSRP-DSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIG----RTNLAELDLF 613
Cdd:PRK13643 1 MIKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGdivvSSTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 614 WLRRKIALVSQEP--VLFATTIAANIAYGCE---ATQEEIEK-AAEQANAHNFIASFEEgyqtqvgERGVKLSGGQKQRV 687
Cdd:PRK13643 81 PVRKKVGVVFQFPesQLFEETVLKDVAFGPQnfgIPKEKAEKiAAEKLEMVGLADEFWE-------KSPFELSGGQMRRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1005434824 688 AIARALLMNPDVLLLDEATSALDAESE-HFVKEAIDRAMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGT 759
Cdd:PRK13643 154 AIAGILAMEPEVLVLDEPTAGLDPKARiEMMQLFESIHQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGT 227
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
538-747 |
1.35e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.87 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 538 NQVIQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRR 617
Cdd:PRK10247 5 SPLLQLQNVGYLAGDAK---ILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 618 KIALVSQEPVLFATTIAANIAYGCEATQEEIEKAAEQAnahnFIASFEEGyQTQVGERGVKLSGGQKQRVAIARALLMNP 697
Cdd:PRK10247 82 QVSYCAQTPTLFGDTVYDNLIFPWQIRNQQPDPAIFLD----DLERFALP-DTILTKNIAELSGGEKQRISLIRNLQFMP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1005434824 698 DVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVI--AHRLSTVRNADQVL 747
Cdd:PRK10247 157 KVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLwvTHDKDEINHADKVI 208
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
558-755 |
1.38e-24 |
|
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: 100.97 E-value: 1.38e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGrtnlaeldlfwlrrkialvsQEPVLFATTIAAnI 637
Cdd:cd03216 15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVD--------------------GKEVSFASPRDA-R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 638 AYGceatqeeiekaaeqanahnfIASFeegYQtqvgergvkLSGGQKQRVAIARALLMNPDVLLLDEATSAL-DAESEHF 716
Cdd:cd03216 74 RAG--------------------IAMV---YQ---------LSVGERQMVEIARALARNARLLILDEPTAALtPAEVERL 121
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1005434824 717 ---VKEAIDRamvNRTVLVIAHRLSTVRN-ADQVLVIDKGHIV 755
Cdd:cd03216 122 fkvIRRLRAQ---GVAVIFISHRLDEVFEiADRVTVLRDGRVV 161
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
555-758 |
1.39e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 103.45 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 555 DSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYD--PK---SGVISIGRTNLAELDLFWLRRKIALVSQEPVLF 629
Cdd:PRK14247 15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 630 AT-TIAANIAYGCEAT---------QEEIEKAAEQANahnfiasFEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPDV 699
Cdd:PRK14247 95 PNlSIFENVALGLKLNrlvkskkelQERVRWALEKAQ-------LWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEV 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 700 LLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAH-RLSTVRNADQVLVIDKGHIVERG 758
Cdd:PRK14247 168 LLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWG 227
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
541-752 |
1.68e-24 |
|
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: 102.41 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPsrPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVI----SIGRTNLAELDLFWLR 616
Cdd:cd03290 1 VQVTNGYFSWG--SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 617 RKIALVSQEPVLFATTIAANIAYGCEATQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALLMN 696
Cdd:cd03290 79 YSVAYAAQKPWLLNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQN 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1005434824 697 PDVLLLDEATSALDAE-SEHFVKEAIDRAMVN--RTVLVIAHRLSTVRNADQVLVIDKG 752
Cdd:cd03290 159 TNIVFLDDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
555-769 |
3.47e-24 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 101.98 E-value: 3.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 555 DSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWL-RRKIALVSQEPVLFAT-T 632
Cdd:COG0410 15 GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRLGIGYVPEGRRIFPSlT 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 633 IAANIAYGCEATQEEIEKAAeqanahnfiaSFEEGYQT--QVGER----GVKLSGGQKQRVAIARALLMNPDVLLLDEAT 706
Cdd:COG0410 95 VEENLLLGAYARRDRAEVRA----------DLERVYELfpRLKERrrqrAGTLSGGEQQMLAIGRALMSRPKLLLLDEPS 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 707 SALdaeSEHFVKE---AIDRamVNR---TVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHETLLAKAGV 769
Cdd:COG0410 165 LGL---APLIVEEifeIIRR--LNRegvTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELLADPEV 229
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
559-750 |
3.52e-24 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 101.02 E-value: 3.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 559 LKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPK---SGVISIGRTNLAELDLfwLRRKIALVSQEPVLFA-TTIA 634
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPA--EQRRIGILFQDDLLFPhLSVG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 635 ANIAYGCEAT------QEEIEKAAEQANAHNFiasfeegyqtqvGERGVK-LSGGQKQRVAIARALLMNPDVLLLDEATS 707
Cdd:COG4136 95 ENLAFALPPTigraqrRARVEQALEEAGLAGF------------ADRDPAtLSGGQRARVALLRALLAEPRALLLDEPFS 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1005434824 708 ALDA----ESEHFVKEAIDRAmvNRTVLVIAHRLSTVRNADQVLVID 750
Cdd:COG4136 163 KLDAalraQFREFVFEQIRQR--GIPALLVTHDEEDAPAAGRVLDLG 207
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
558-752 |
4.10e-24 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 101.74 E-value: 4.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISI----GRTNLAELD---LFWLRRK-IALVSQ----- 624
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQASpreILALRRRtIGYVSQflrvi 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 625 ----------EPvLFATTIAANIAYgceatqeeiEKAAE--------QANAHNFIASFeegyqtqvgergvklSGGQKQR 686
Cdd:COG4778 106 prvsaldvvaEP-LLERGVDREEAR---------ARAREllarlnlpERLWDLPPATF---------------SGGEQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 687 VAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLV-IAHRLSTV-RNADQVLVIDKG 752
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFHDEEVReAVADRVVDVTPF 228
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
514-756 |
4.13e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.07 E-value: 4.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 514 VRMFELMDRI--------PSIDLEGGKKLStvNQVIQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTV 585
Cdd:COG0488 283 IKALEKLEREepprrdktVEIRFPPPERLG--KKVLELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 586 ISLLERFYDPKSGVISIGrTNLaeldlfwlrrKIALVSQEPVLFAT--TIAANIAYGCEATQEeiekaaeqANAHNFIAS 663
Cdd:COG0488 358 LKLLAGELEPDSGTVKLG-ETV----------KIGYFDQHQEELDPdkTVLDELRDGAPGGTE--------QEVRGYLGR 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 664 F----EEGYqTQVGergvKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESehfvKEAIDRAMVN--RTVLVIAH-R 736
Cdd:COG0488 419 FlfsgDDAF-KPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIET----LEALEEALDDfpGTVLLVSHdR 489
|
250 260
....*....|....*....|..
gi 1005434824 737 --LSTVrnADQVLVIDKGHIVE 756
Cdd:COG0488 490 yfLDRV--ATRILEFEDGGVRE 509
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
558-762 |
4.72e-24 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 106.64 E-value: 4.72e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISI-GR------TNLAEldlfwlRRKIALVSQEPVLFA 630
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdGEpvrfrsPRDAQ------AAGIAIIHQELNLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 631 T-TIAANIAYGCEAT------QEEIEKAAEQAnahnfIASFEEGY--QTQVGErgvkLSGGQKQRVAIARALLMNPDVLL 701
Cdd:COG1129 93 NlSVAENIFLGREPRrgglidWRAMRRRAREL-----LARLGLDIdpDTPVGD----LSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1005434824 702 LDEATSAL-DAESEHF---VKEAIDRamvNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVerGTHET 762
Cdd:COG1129 164 LDEPTASLtEREVERLfriIRRLKAQ---GVAIIYISHRLDEVFEiADRVTVLRDGRLV--GTGPV 224
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
558-754 |
4.82e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 102.06 E-value: 4.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELdlfwlRRKIALVSQEPVLFA-TTIAAN 636
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLMFQDARLLPwKKVIDN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 637 IAYGCEATQEEiekAAEQANAhnfiasfEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHF 716
Cdd:PRK11247 102 VGLGLKGQWRD---AALQALA-------AVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1005434824 717 VKEAIDRAMVNR--TVLVIAHRLS-TVRNADQVLVIDKGHI 754
Cdd:PRK11247 172 MQDLIESLWQQHgfTVLLVTHDVSeAVAMADRVLLIEEGKI 212
|
|
| ABC_6TM_PCAT1_LagD_like |
cd18570 |
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ... |
220-502 |
8.91e-24 |
|
Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette transporters; This group includes the 6-TMD of the peptidase-containing ATP-binding cassette transporters (PCATs) such as Clostridium thermocellum PCAT1, a polypeptide processing and secretion transporter, and LagD, a bacteriocin ABC transporter from Lactococcus lactis. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs. The transporters involved in protein secretion often contain additional peptidase domains essential for substrate processing. These peptidase domains belong to the cysteine protease superfamily, classified as family C39, bacteriocin-processing peptidase. LagD is highly similar to the peptidase-containing ATP-binding cassette transporters (PCATs). In Gram-positive bacteria, the PCATs are responsible for exporting quorum-sensing or antimicrobial peptides called bacteriocins.
Pssm-ID: 350014 [Multi-domain] Cd Length: 294 Bit Score: 102.52 E-value: 8.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 220 KPELCVLFIASVALLASSgsqIAAPYFFG----RVIQASMeegMSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLV 295
Cdd:cd18570 1 KKLLILILLLSLLITLLG---IAGSFFFQilidDIIPSGD---INLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 296 ARIRKQLFASVVEQEVAFFDSNRTGELINRLSsDTQVIQNALT-VNVSMLLRYIIqIIGSLAFMFSLSAKLTGVLISVVP 374
Cdd:cd18570 75 IRLILGYFKHLLKLPLSFFETRKTGEIISRFN-DANKIREAISsTTISLFLDLLM-VIISGIILFFYNWKLFLITLLIIP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 375 IVGIgaqRYGSFVQGLRKRFQDELAAASSTAEE---AIANIRTVRSFSQERKSMNS----YDTDIDKSYKSGaKLALASG 447
Cdd:cd18570 153 LYIL---IILLFNKPFKKKNREVMESNAELNSYlieSLKGIETIKSLNAEEQFLKKiekkFSKLLKKSFKLG-KLSNLQS 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1005434824 448 FFNGVIGIIGQgavVLVLWYGGSLVNKHELDVGILTAFmlYTLnvaMAFaFLSSV 502
Cdd:cd18570 229 SIKGLISLIGS---LLILWIGSYLVIKGQLSLGQLIAF--NAL---LGY-FLGPI 274
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
540-765 |
1.09e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 101.60 E-value: 1.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYPSrpDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELD-LFWLRRK 618
Cdd:PRK13644 1 MIRLENVSYSYPD--GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSkLQGIRKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 619 IALVSQEP--VLFATTIAANIAYGCE---ATQEEIEKAAEQANAhnfiasfEEGYQTQVGERGVKLSGGQKQRVAIARAL 693
Cdd:PRK13644 79 VGIVFQNPetQFVGRTVEEDLAFGPEnlcLPPIEIRKRVDRALA-------EIGLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1005434824 694 LMNPDVLLLDEATSALDAESEHFVKEAIDRAMVN-RTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHETLLA 765
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKgKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVLS 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
559-782 |
1.18e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 104.34 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 559 LKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLR----RKIALVSQEPVLFA-TTI 633
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPhMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 634 AANIAYGCE----ATQEEIEKAAEqANAHNFIASFEEGYQTQvgergvkLSGGQKQRVAIARALLMNPDVLLLDEATSAL 709
Cdd:PRK10070 124 LDNTAFGMElagiNAEERREKALD-ALRQVGLENYAHSYPDE-------LSGGMRQRVGLARALAINPDILLMDEAFSAL 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 710 DAESEHFVKEAIDR--AMVNRTVLVIAHRL-STVRNADQVLVIDKGHIVERGTHETLLAK-AGVYKKLVLRQLSVSQ 782
Cdd:PRK10070 196 DPLIRTEMQDELVKlqAKHQRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEILNNpANDYVRTFFRGVDISQ 272
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
558-808 |
1.58e-23 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 101.08 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKsGVISIGRTNLAELDLFWLRRKIALVSQEPVLFATTIAANI 637
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTFRKNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 638 -AYGCEaTQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHF 716
Cdd:cd03289 98 dPYGKW-SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 717 VKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHETLLAKAGVYKKLVLR----QLSVSQHENLSAGDLD 792
Cdd:cd03289 177 IRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAISPsdrlKLFPRRNSSKSKRKPR 256
|
250
....*....|....*.
gi 1005434824 793 PNLLGSEQPSVEEVEE 808
Cdd:cd03289 257 PQIQALQEETEEEVQD 272
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
534-740 |
2.14e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 100.50 E-value: 2.14e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 534 LSTVNQVIQFQDVYFAYPSRpdsDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRT-----NLA 608
Cdd:PRK14258 1 MSKLIPAIKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVeffnqNIY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 609 E--LDLFWLRRKIALVSQEPVLFATTIAANIAYGCEAT----QEEIEKAAEQANAHnfiASFEEGYQTQVGERGVKLSGG 682
Cdd:PRK14258 78 ErrVNLNRLRRQVSMVHPKPNLFPMSVYDNVAYGVKIVgwrpKLEIDDIVESALKD---ADLWDEIKHKIHKSALDLSGG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1005434824 683 QKQRVAIARALLMNPDVLLLDEATSALDAES----EHFVKEAIDRAMVnrTVLVIAHRLSTV 740
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIAsmkvESLIQSLRLRSEL--TMVIVSHNLHQV 214
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
558-759 |
2.47e-23 |
|
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: 100.11 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWL-RRKIALVSQEPVLFAT-TIAA 635
Cdd:COG0411 19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIaRLGIARTFQNPRLFPElTVLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 636 NIAYGCEATQEE-------------IEKAAEQANAHNFIASFeeGYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLL 702
Cdd:COG0411 99 NVLVAAHARLGRgllaallrlprarREEREARERAEELLERV--GLADRADEPAGNLSYGQQRRLEIARALATEPKLLLL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1005434824 703 DEATSAL-DAESEHFVkEAID--RAMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGT 759
Cdd:COG0411 177 DEPAAGLnPEETEELA-ELIRrlRDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGT 236
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
558-773 |
2.66e-23 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 106.79 E-value: 2.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVI-SLLERFYdpksgvISIGRTnlaeldlfWLRRKIALVSQEPVLFATTIAAN 636
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLqSLLSQFE------ISEGRV--------WAERSIAYVPQQAWIMNATVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 637 IAYGCEATQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAE-SEH 715
Cdd:PTZ00243 741 ILFFDEEDAARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGER 820
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 716 FVKEAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHETlLAKAGVYKKL 773
Cdd:PTZ00243 821 VVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSAD-FMRTSLYATL 877
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
535-756 |
2.71e-23 |
|
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: 99.43 E-value: 2.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 535 STVNQVIQFQDVYFAYPSRPDS-DVLKGMSFELKPGETVALVGPSGGGKSTVISL---LERfydPKSGVISIGRTNLAEL 610
Cdd:COG4181 3 SSSAPIIELRGLTKTVGTGAGElTILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 611 D----LFWLRRKIALVSQEPVLFAT-TIAANIAYGCE-ATQEEIEKAAEQANAhnfiasfeegyqtQVG--ERG----VK 678
Cdd:COG4181 80 DedarARLRARHVGFVFQSFQLLPTlTALENVMLPLElAGRRDARARARALLE-------------RVGlgHRLdhypAQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 679 LSGGQKQRVAIARALLMNPDVLLLDEATSALDAESehfvKEAIDRAM--VNR---TVLVIA-HRLSTVRNADQVLVIDKG 752
Cdd:COG4181 147 LSGGEQQRVALARAFATEPAILFADEPTGNLDAAT----GEQIIDLLfeLNRergTTLVLVtHDPALAARCDRVLRLRAG 222
|
....
gi 1005434824 753 HIVE 756
Cdd:COG4181 223 RLVE 226
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
563-765 |
3.62e-23 |
|
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: 101.73 E-value: 3.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 563 SFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAE----LDLFWLRRKIALVSQEPVLFA-TTIAANI 637
Cdd:TIGR02142 17 DFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgIFLPPEKRRIGYVFQEARLFPhLSVRGNL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 638 AYG---CEATQEEIekaaeqanahnfiaSFEE-----GYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSAL 709
Cdd:TIGR02142 97 RYGmkrARPSERRI--------------SFERviellGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAAL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1005434824 710 DAESEHFVKEAIDR--AMVNRTVLVIAHRLSTV-RNADQVLVIDKGHIVERGTHETLLA 765
Cdd:TIGR02142 163 DDPRKYEILPYLERlhAEFGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
534-737 |
4.30e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 99.47 E-value: 4.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 534 LSTVNQ---VIQFQDVYFAYPSrpdSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYD-----PKSGVISIGRT 605
Cdd:PRK14243 1 TSTLNGtetVLRTENLNVYYGS---FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 606 NL--AELDLFWLRRKIALVSQEPVLFATTIAANIAYGCEAT------QEEIEKAAEQAnahnfiASFEEgYQTQVGERGV 677
Cdd:PRK14243 78 NLyaPDVDPVEVRRRIGMVFQKPNPFPKSIYDNIAYGARINgykgdmDELVERSLRQA------ALWDE-VKDKLKQSGL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 678 KLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRL 737
Cdd:PRK14243 151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
538-755 |
4.63e-23 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 104.81 E-value: 4.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 538 NQVIQFQDVYFAYPSRPDS-DVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELD---LF 613
Cdd:PRK10535 2 TALLELKDIRRSYPSGEEQvEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDadaLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 614 WLRRK-IALVSQEPVLFA-TTIAANIAygCEATQEEIEKAAEQANAHNFIASFeeGYQTQVGERGVKLSGGQKQRVAIAR 691
Cdd:PRK10535 82 QLRREhFGFIFQRYHLLShLTAAQNVE--VPAVYAGLERKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1005434824 692 ALLMNPDVLLLDEATSALDAESEHFVKeAIDRAMVNR--TVLVIAHRLSTVRNADQVLVIDKGHIV 755
Cdd:PRK10535 158 ALMNGGQVILADEPTGALDSHSGEEVM-AILHQLRDRghTVIIVTHDPQVAAQAERVIEIRDGEIV 222
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18782 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
220-509 |
5.22e-23 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 99.97 E-value: 5.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 220 KPELCVLFIASVALlasSGSQIAAPYFFGRVIQA-SMEEGMSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARI 298
Cdd:cd18782 1 RRALIEVLALSFVV---QLLGLANPLLFQVIIDKvLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 299 RKQLFASVVEQEVAFFDSNRTGELINRLSsDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGI 378
Cdd:cd18782 78 GGTIIDHLLRLPLGFFDKRPVGELSTRIS-ELDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 379 GAQRYGSFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQ 458
Cdd:cd18782 157 LTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEGFKLTVLGTTSGSLSQFLNK 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1005434824 459 GAVVLVLWYGGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQA 509
Cdd:cd18782 237 LSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLSTLWQQFQEL 287
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
549-749 |
6.79e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 96.92 E-value: 6.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 549 AYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTnlaeldlfwlrRKIALVSQ---E 625
Cdd:NF040873 1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-----------ARVAYVPQrseV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 626 PVLFATTIAANIAYGCEATQ-------EEIEKAAEQANAHNFIASFEEgyqTQVGErgvkLSGGQKQRVAIARALLMNPD 698
Cdd:NF040873 67 PDSLPLTVRDLVAMGRWARRglwrrltRDDRAAVDDALERVGLADLAG---RQLGE----LSGGQRQRALLAQGLAQEAD 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1005434824 699 VLLLDEATSALDAESEHFVKEAIDRAMV-NRTVLVIAHRLSTVRNADQVLVI 749
Cdd:NF040873 140 LLLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
541-758 |
7.51e-23 |
|
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: 97.44 E-value: 7.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAY-PSRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIG--RTNLAELDLfwlRR 617
Cdd:cd03266 2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfDVVKEPAEA---RR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 618 KIALVSQEPVLFA-TTIAANIAY--------GCEATQEeIEKAAEQANAHNFIAsfeegyqtqvgERGVKLSGGQKQRVA 688
Cdd:cd03266 79 RLGFVSDSTGLYDrLTARENLEYfaglyglkGDELTAR-LEELADRLGMEELLD-----------RRVGGFSTGMRQKVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1005434824 689 IARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAM-VNRTVLVIAHRLSTV-RNADQVLVIDKGHIVERG 758
Cdd:cd03266 147 IARALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRaLGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
558-765 |
1.02e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 99.01 E-value: 1.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSG------VISIGRTNLAELDLFWLRRKIALVSQEPVLFAT 631
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgdVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFPM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 632 TIAANIAYGCEATQEEIEKAAEQ-ANAHNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALD 710
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVPRKEFRGvAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 711 AESEHFVKEAIdRAMVNR-TVLVIAHRLS-TVRNADQVLVIDKGHIVERGTHETLLA 765
Cdd:PRK14271 196 PTTTEKIEEFI-RSLADRlTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLFS 251
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
540-761 |
2.10e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.95 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYpsRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKI 619
Cdd:PRK13652 3 LIETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 620 ALVSQEP--VLFATTIAANIAYGCEATQEEIEKAAEQANAHNFIASFEEgYQTQVGERgvkLSGGQKQRVAIARALLMNP 697
Cdd:PRK13652 81 GLVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEE-LRDRVPHH---LSGGEKKRVAIAGVIAMEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 698 DVLLLDEATSALDAESehfVKEAID--RAMVNR---TVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHE 761
Cdd:PRK13652 157 QVLVLDEPTAGLDPQG---VKELIDflNDLPETygmTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVE 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
540-776 |
2.66e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 97.61 E-value: 2.66e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYPSrpDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNL--AELDLFWLRR 617
Cdd:PRK13636 5 ILKVEELNYNYSD--GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdySRKGLMKLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 618 KIALVSQEP--VLFATTIAANIAYGC---EATQEEIEKAAEQANAHNFIASFEEGyQTQVgergvkLSGGQKQRVAIARA 692
Cdd:PRK13636 83 SVGMVFQDPdnQLFSASVYQDVSFGAvnlKLPEDEVRKRVDNALKRTGIEHLKDK-PTHC------LSFGQKKRVAIAGV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 693 LLMNPDVLLLDEATSALD----AESEHFVKEAIDRamVNRTVLVIAHRLSTVR-NADQVLVIDKGHIVERGTHETLLAKA 767
Cdd:PRK13636 156 LVMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQKE--LGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQGNPKEVFAEK 233
|
....*....
gi 1005434824 768 GVYKKLVLR 776
Cdd:PRK13636 234 EMLRKVNLR 242
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
557-765 |
3.22e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 96.96 E-value: 3.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 557 DVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIG-------RTNLAELDLF------WLRRKIALVS 623
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNgqtinlvRDKDGQLKVAdknqlrLLRTRLTMVF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 624 QEPVLFA-TTIAANIAygcEATQE--EIEKAAEQANAHNFIASFEEGYQTQvGERGVKLSGGQKQRVAIARALLMNPDVL 700
Cdd:PRK10619 99 QHFNLWShMTVLENVM---EAPIQvlGLSKQEARERAVKYLAKVGIDERAQ-GKYPVHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1005434824 701 LLDEATSALDAEsehFVKEAIdRAMVN-----RTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHETLLA 765
Cdd:PRK10619 175 LFDEPTSALDPE---LVGEVL-RIMQQlaeegKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQLFG 241
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
541-759 |
3.24e-22 |
|
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: 95.65 E-value: 3.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPDSdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAElDLFWLRRKIA 620
Cdd:cd03263 1 LQIRNLTKTYKKGTKP-AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 621 LVSQEPVLFAT-TIAANIAYGCEATQeeIEKAAEQANAHNFIASFE-EGYQ-TQVGErgvkLSGGQKQRVAIARALLMNP 697
Cdd:cd03263 79 YCPQFDALFDElTVREHLRFYARLKG--LPKSEIKEEVELLLRVLGlTDKAnKRART----LSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1005434824 698 DVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGT 759
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGS 215
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
556-780 |
3.87e-22 |
|
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: 96.05 E-value: 3.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 556 SDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWL-RRKIALVSQEPVLFAT-TI 633
Cdd:TIGR03410 13 SHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERaRAGIAYVPQGREIFPRlTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 634 AANIAYGCEAtqeeiekaaeQANAHNFIAsfEEGY------QTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATS 707
Cdd:TIGR03410 93 EENLLTGLAA----------LPRRSRKIP--DEIYelfpvlKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005434824 708 ALDAEsehFVKE---AID--RAMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGThetllaKAGVYKKLVLRQLSV 780
Cdd:TIGR03410 161 GIQPS---IIKDigrVIRrlRAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGA------GDELDEDKVRRYLAV 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
559-763 |
5.28e-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: 95.13 E-value: 5.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 559 LKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSgvisiGRTNLAELDLFW----LRRKIALVSQEPVL-FATTI 633
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTS-----GRATVAGHDVVRepreVRRRIGIVFQDLSVdDELTG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 634 AANIA-----YGCEAtQEEIEKAAEqanahnFIASFEEGyqtQVGERGVK-LSGGQKQRVAIARALLMNPDVLLLDEATS 707
Cdd:cd03265 91 WENLYiharlYGVPG-AERRERIDE------LLDFVGLL---EAADRLVKtYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 708 ALDAESEHFVKEAIdRAMVNR---TVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHETL 763
Cdd:cd03265 161 GLDPQTRAHVWEYI-EKLKEEfgmTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
540-710 |
9.05e-22 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 98.10 E-value: 9.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISI-GR--TNL-AEldlfwl 615
Cdd:PRK09452 14 LVELRGISKSFDGKE---VISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLdGQdiTHVpAE------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 616 RRKIALVSQEPVLFA-TTIAANIAYG--CEAT-QEEIEKAAEQANAHNFIASFEEGYQTQvgergvkLSGGQKQRVAIAR 691
Cdd:PRK09452 85 NRHVNTVFQSYALFPhMTVFENVAFGlrMQKTpAAEITPRVMEALRMVQLEEFAQRKPHQ-------LSGGQQQRVAIAR 157
|
170
....*....|....*....
gi 1005434824 692 ALLMNPDVLLLDEATSALD 710
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALD 176
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
558-758 |
9.34e-22 |
|
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: 94.21 E-value: 9.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISI---GRTNLAELdlfwLRRKIALVSqEPVLFAT-TI 633
Cdd:cd03268 15 VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFdgkSYQKNIEA----LRRIGALIE-APGFYPNlTA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 634 AANIAYGCEATQ---EEIEKAAEQANAHNfiasfeegyqtqVGERGVK-LSGGQKQRVAIARALLMNPDVLLLDEATSAL 709
Cdd:cd03268 90 RENLRLLARLLGirkKRIDEVLDVVGLKD------------SAKKKVKgFSLGMKQRLGIALALLGNPDLLILDEPTNGL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1005434824 710 DAESEHFVKEAI-DRAMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERG 758
Cdd:cd03268 158 DPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
553-756 |
1.34e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 95.52 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 553 RPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELD-----LFwlRRKIALVSQEP- 626
Cdd:PRK10419 22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqrkAF--RRDIQMVFQDSi 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 627 --VLFATTIAANIA-----------YGCEATQEEIEKAAEQANAHnfiasfeegyqtqVGERGVKLSGGQKQRVAIARAL 693
Cdd:PRK10419 100 saVNPRKTVREIIReplrhllsldkAERLARASEMLRAVDLDDSV-------------LDKRPPQLSGGQLQRVCLARAL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005434824 694 LMNPDVLLLDEATSALDAeseHFVKEAID-----RAMVNRTVLVIAHRLSTV-RNADQVLVIDKGHIVE 756
Cdd:PRK10419 167 AVEPKLLILDEAVSNLDL---VLQAGVIRllkklQQQFGTACLFITHDLRLVeRFCQRVMVMDNGQIVE 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
558-765 |
1.80e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 99.01 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRT--NLAELDLFWLRRKIALVSQEPV------LF 629
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIWFDGQPlhNLNRRQLLPVRHRIQVVFQDPNsslnprLN 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 630 ATTIaanIAYGCEATQEEIEKAAEQANAhnfIASFEE-GYQTQVGER-GVKLSGGQKQRVAIARALLMNPDVLLLDEATS 707
Cdd:PRK15134 381 VLQI---IEEGLRVHQPTLSAAQREQQV---IAVMEEvGLDPETRHRyPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1005434824 708 ALDAESEHFVKeAIDRAMVNR---TVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHETLLA 765
Cdd:PRK15134 455 SLDKTVQAQIL-ALLKSLQQKhqlAYLFISHDLHVVRAlCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
558-758 |
1.91e-21 |
|
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: 93.94 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGrtnlaelDLFWLRRKIALVSQEPVLFA--TTIAA 635
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVA-------GLVPWKRRKKFLRRIGVVFGqkTQLWW 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 636 NI----AYGCEATQEEIEKAAEQANAHNFIASFEEGYQTQVGERgvKLSGGQKQRVAIARALLMNPDVLLLDEATSALDA 711
Cdd:cd03267 109 DLpvidSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVR--QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1005434824 712 ESEHFVKEAIDRAMVNR--TVLVIAHRLSTV-RNADQVLVIDKGHIVERG 758
Cdd:cd03267 187 VAQENIRNFLKEYNRERgtTVLLTSHYMKDIeALARRVLVIDKGRLLYDG 236
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
541-751 |
1.99e-21 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 91.83 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAypsRPDSDVL-KGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRtnlaeldlfwlRRKI 619
Cdd:cd03223 1 IELENLSLA---TPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-----------GEDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 620 ALVSQEPVLFATTIAANIAYGCEATqeeiekaaeqanahnfiasfeegyqtqvgergvkLSGGQKQRVAIARALLMNPDV 699
Cdd:cd03223 67 LFLPQRPYLPLGTLREQLIYPWDDV----------------------------------LSGGEQQRLAFARLLLHKPKF 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1005434824 700 LLLDEATSALDAESEHFVKEAIDRAMVnrTVLVIAHRLSTVRNADQVLVIDK 751
Cdd:cd03223 113 VFLDEATSALDEESEDRLYQLLKELGI--TVISVGHRPSLWKFHDRVLDLDG 162
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
555-779 |
2.10e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 94.73 E-value: 2.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 555 DSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERF---YDPK----SGVISIGRtNLAELDLFWLRRKIALVSQEPV 627
Cdd:PRK14246 22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSKikvdGKVLYFGK-DIFQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 628 LFA-TTIAANIAYGCEA----TQEEIEKAAEQANAHnfIASFEEGYQtQVGERGVKLSGGQKQRVAIARALLMNPDVLLL 702
Cdd:PRK14246 101 PFPhLSIYDNIAYPLKShgikEKREIKKIVEECLRK--VGLWKEVYD-RLNSPASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 703 DEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTV-RNADQVLVIDKGHIVERGTHETLLA--KAGVYKKLVLRQLS 779
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIFTspKNELTEKYVIGRIS 257
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
558-758 |
3.02e-21 |
|
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: 92.73 E-value: 3.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDlfwlRRKIALVSQEPVLF-ATTIAAN 636
Cdd:cd03269 15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA----RNRIGYLPEERGLYpKMKVIDQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 637 IAYgcEATQEEIEKAAEQANAHNFIASFE-EGYQTQVGErgvKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEH 715
Cdd:cd03269 91 LVY--LAQLKGLKKEEARRRIDEWLERLElSEYANKRVE---ELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVE 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1005434824 716 FVKEAI-DRAMVNRTVLVIAHRLSTV-RNADQVLVIDKGHIVERG 758
Cdd:cd03269 166 LLKDVIrELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
|
|
| ABC_6TM_exporter_like |
cd18565 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
265-489 |
3.38e-21 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 95.33 E-value: 3.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 265 TIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQLFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSML 344
Cdd:cd18565 56 LGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFLDDGANSI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 345 LRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAQRYGSFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQE--- 421
Cdd:cd18565 136 IRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEdfe 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005434824 422 ----RKSMNSY-DTDIDksyksGAKLalaSGFFNGVIGIIGQGAVVLVLWYGGSLV------NKHELDVGILTAFMLYT 489
Cdd:cd18565 216 rervADASEEYrDANWR-----AIRL---RAAFFPVIRLVAGAGFVATFVVGGYWVldgpplFTGTLTVGTLVTFLFYT 286
|
|
| ABC_6TM_exporter_like |
cd18540 |
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ... |
226-509 |
3.87e-21 |
|
Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 94.47 E-value: 3.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 226 LFIASVALLASSGSQIAAPYFFGRVIQASMEEGmshLNKTIVLLSLIYLAGALAALVRSWLF-TLAGQ---RLVARIRKQ 301
Cdd:cd18540 4 LILLIILMLLVALLDAVFPLLTKYAIDHFITPG---TLDGLTGFILLYLGLILIQALSVFLFiRLAGKiemGVSYDLRKK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 302 LFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVP-IVGIG- 379
Cdd:cd18540 81 AFEHLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPvLAVVSi 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 380 --------AQRY---------GSFVQGlrkrfqdelaaasstaeeaIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKL 442
Cdd:cd18540 161 yfqkkilkAYRKvrkinsritGAFNEG-------------------ITGAKTTKTLVREEKNLREFKELTEEMRRASVRA 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 443 ALASGFFNGVIGIIGQGAVVLVLWYGGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQA 509
Cdd:cd18540 222 ARLSALFLPIVLFLGSIATALVLWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSA 288
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
558-756 |
4.21e-21 |
|
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: 93.72 E-value: 4.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELD---LFWLRRKIALVSQE---PVLFAT 631
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDrkqRRAFRRDVQLVFQDspsAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 632 TIAANIAYGCEATqEEIEKAAEQANAHNFIAsfEEGYQTQVGER-GVKLSGGQKQRVAIARALLMNPDVLLLDEATSALD 710
Cdd:TIGR02769 106 TVRQIIGEPLRHL-TSLDESEQKARIAELLD--MVGLRSEDADKlPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1005434824 711 AESEHFVKEAID--RAMVNRTVLVIAHRLSTV-RNADQVLVIDKGHIVE 756
Cdd:TIGR02769 183 MVLQAVILELLRklQQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVE 231
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
552-774 |
4.99e-21 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 93.75 E-value: 4.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 552 SRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIALVSQ------- 624
Cdd:COG4167 22 RRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKYRCKHIRMIFQdpntsln 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 625 ----------EPVLFATTIAAniaygcEATQEEIEKA-------AEQANahnfiasfeegYQTQVgergvkLSGGQKQRV 687
Cdd:COG4167 102 prlnigqileEPLRLNTDLTA------EEREERIFATlrlvgllPEHAN-----------FYPHM------LSSGQKQRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 688 AIARALLMNPDVLLLDEATSALDAesehfvkeAIDRAMVNRTV----------LVIAHRLSTVRN-ADQVLVIDKGHIVE 756
Cdd:COG4167 159 ALARALILQPKIIIADEALAALDM--------SVRSQIINLMLelqeklgisyIYVSQHLGIVKHiSDKVLVMHQGEVVE 230
|
250 260
....*....|....*....|
gi 1005434824 757 RGTHETLLA--KAGVYKKLV 774
Cdd:COG4167 231 YGKTAEVFAnpQHEVTKRLI 250
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
555-761 |
5.03e-21 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 93.15 E-value: 5.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 555 DSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIALVSQEPVL-FATTI 633
Cdd:PRK11231 14 TKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHLTpEGITV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 634 AANIAYG-----------CEATQEEIEKAAEqanahnfiasfeegyQTQVGERGVK----LSGGQKQRVAIARALLMNPD 698
Cdd:PRK11231 94 RELVAYGrspwlslwgrlSAEDNARVNQAME---------------QTRINHLADRrltdLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 699 VLLLDEATSALDAesEHFVkEAID--RAMVN--RTVLVIAHRLSTV-RNADQVLVIDKGHIVERGTHE 761
Cdd:PRK11231 159 VVLLDEPTTYLDI--NHQV-ELMRlmRELNTqgKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQGTPE 223
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
541-711 |
1.14e-20 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 92.62 E-value: 1.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYP-SRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNL----AEldlfwl 615
Cdd:COG4525 4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVtgpgAD------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 616 rRkiALVSQEPVLFA-TTIAANIAYGCEATQeeIEKAAEQANAHNFIAsfeegyqtQVGERGV------KLSGGQKQRVA 688
Cdd:COG4525 78 -R--GVVFQKDALLPwLNVLDNVAFGLRLRG--VPKAERRARAEELLA--------LVGLADFarrriwQLSGGMRQRVG 144
|
170 180
....*....|....*....|...
gi 1005434824 689 IARALLMNPDVLLLDEATSALDA 711
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDA 167
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
558-759 |
1.82e-20 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 94.00 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAEL---DlfwlrRKIALVSQEPVLFA-TTI 633
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLharD-----RKVGFVFQHYALFRhMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 634 AANIAYGCEA-------TQEEIEKAAEQANAHNFIASFEEGYQTQvgergvkLSGGQKQRVAIARALLMNPDVLLLDEAT 706
Cdd:PRK10851 92 FDNIAFGLTVlprrerpNAAAIKAKVTQLLEMVQLAHLADRYPAQ-------LSGGQKQRVALARALAVEPQILLLDEPF 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 707 SALDAEsehfVKEAIDRAMVN-------RTVLVIAHRLSTVRNADQVLVIDKGHIVERGT 759
Cdd:PRK10851 165 GALDAQ----VRKELRRWLRQlheelkfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGT 220
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
558-763 |
2.06e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 92.84 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISI------GRTNLAELDLFW----------------- 614
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdekNKKKTKEKEKVLeklviqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 615 -LRRKIALVSQ--EPVLFATTIAANIAYGCEATQEEIEKAAEQANAHNFIASFEEGYQtqvgERG-VKLSGGQKQRVAIA 690
Cdd:PRK13651 102 eIRRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESYL----QRSpFELSGGQKRRVALA 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005434824 691 RALLMNPDVLLLDEATSALDAESehfVKEAID----RAMVNRTVLVIAHRLSTV-RNADQVLVIDKGHIVERG-THETL 763
Cdd:PRK13651 178 GILAMEPDFLVFDEPTAGLDPQG---VKEILEifdnLNKQGKTIILVTHDLDNVlEWTKRTIFFKDGKIIKDGdTYDIL 253
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
558-777 |
2.54e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 90.91 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISI-GR-TNLAEL------DLfwlrrkialvsqepvlf 629
Cdd:COG1134 41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVnGRvSALLELgagfhpEL----------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 630 atTIAANIAYGCEA---TQEEIEKAAEqanahnFIASFEEgyqtqVGE---RGVK-LSGGQKQRVAIARALLMNPDVLLL 702
Cdd:COG1134 104 --TGRENIYLNGRLlglSRKEIDEKFD------EIVEFAE-----LGDfidQPVKtYSSGMRARLAFAVATAVDPDILLV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 703 DEATSALDAeseHFVKEAIDR--AMVN--RTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHETLLAKagvYKKLVLRQ 777
Cdd:COG1134 171 DEVLAVGDA---AFQKKCLARirELREsgRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIAA---YEALLAGR 244
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
540-768 |
2.81e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.18 E-value: 2.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYPsrpDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISI------GRTNLAeldlf 613
Cdd:PRK13537 7 PIDFRNVEKRYG---DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLcgepvpSRARHA----- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 614 wlRRKIALVSQ----EPVLfatTIAANIA-----YGCEATQ--EEIEKAAEqanahnfIASFEEGYQTQVGErgvkLSGG 682
Cdd:PRK13537 79 --RQRVGVVPQfdnlDPDF---TVRENLLvfgryFGLSAAAarALVPPLLE-------FAKLENKADAKVGE----LSGG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 683 QKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIdRAMVNR--TVLVIAHRLSTV-RNADQVLVIDKGH-IVERG 758
Cdd:PRK13537 143 MKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLMWERL-RSLLARgkTILLTTHFMEEAeRLCDRLCVIEEGRkIAEGA 221
|
250
....*....|
gi 1005434824 759 THETLLAKAG 768
Cdd:PRK13537 222 PHALIESEIG 231
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
540-755 |
4.74e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 89.55 E-value: 4.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYPSrpDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAEL---DLFWLR 616
Cdd:PRK10908 1 MIRFEHVSKAYLG--GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrEVPFLR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 617 RKIALVSQEP-VLFATTIAANIAYG---CEATQEEIEKAAEQA--------NAHNFiasfeegyqtqvgerGVKLSGGQK 684
Cdd:PRK10908 79 RQIGMIFQDHhLLMDRTVYDNVAIPliiAGASGDDIRRRVSAAldkvglldKAKNF---------------PIQLSGGEQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005434824 685 QRVAIARALLMNPDVLLLDEATSALD-AESEHFVK--EAIDRAMVnrTVLVIAHRLSTV-RNADQVLVIDKGHIV 755
Cdd:PRK10908 144 QRVGIARAVVNKPAVLLADEPTGNLDdALSEGILRlfEEFNRVGV--TVLMATHDIGLIsRRSYRMLTLSDGHLH 216
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
541-761 |
4.90e-20 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.20 E-value: 4.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISI------GRTNLAeldlfw 614
Cdd:PRK13536 42 IDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlgvpvpARARLA------ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 615 lRRKIALVSQEPVL-FATTIAAN-IAYG--CEATQEEIEkaAEQANAHNFiASFEEGYQTQVGErgvkLSGGQKQRVAIA 690
Cdd:PRK13536 113 -RARIGVVPQFDNLdLEFTVRENlLVFGryFGMSTREIE--AVIPSLLEF-ARLESKADARVSD----LSGGMKRRLTLA 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005434824 691 RALLMNPDVLLLDEATSALDAESEHFVKEAIdRAMVNR--TVLVIAHRLSTV-RNADQVLVIDKGH-IVERGTHE 761
Cdd:PRK13536 185 RALINDPQLLILDEPTTGLDPHARHLIWERL-RSLLARgkTILLTTHFMEEAeRLCDRLCVLEAGRkIAEGRPHA 258
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
541-753 |
7.03e-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: 86.73 E-value: 7.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNlaeldlfwlrrKIA 620
Cdd:cd03221 1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTV-----------KIG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 621 LVSQepvlfattiaaniaygceatqeeiekaaeqanahnfiasfeegyqtqvgergvkLSGGQKQRVAIARALLMNPDVL 700
Cdd:cd03221 67 YFEQ------------------------------------------------------LSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 701 LLDEATSALDAESehfvKEAIDRAMVN--RTVLVIAH-R--LSTVrnADQVLVIDKGH 753
Cdd:cd03221 93 LLDEPTNHLDLES----IEALEEALKEypGTVILVSHdRyfLDQV--ATKIIELEDGK 144
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
555-758 |
9.54e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 89.52 E-value: 9.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 555 DSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPK-----SGVISIGRTNL--AELDLFWLRRKIALVSQEPV 627
Cdd:PRK14267 16 SNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEVRREVGMVFQYPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 628 LFA-TTIAANIAYGCE-----ATQEEIEKAAEQANAHnfiASFEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLL 701
Cdd:PRK14267 96 PFPhLTIYDNVAIGVKlnglvKSKKELDERVEWALKK---AALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 702 LDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHR-LSTVRNADQVLVIDKGHIVERG 758
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVG 230
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
546-763 |
1.05e-19 |
|
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: 90.30 E-value: 1.05e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 546 VYFAYPSRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVIS-IGRtnlaeldlfwlrrkIALVSQ 624
Cdd:cd03291 40 LFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKhSGR--------------ISFSSQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 625 EPVLFATTIAANIAYGCEATQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDE 704
Cdd:cd03291 106 FSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDS 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 705 ATSALDAESEHFVKEA-IDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHETL 763
Cdd:cd03291 186 PFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
541-757 |
1.26e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 89.37 E-value: 1.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNL----AEldlfwlr 616
Cdd:PRK11248 2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVegpgAE------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 617 rKIALVSQEPVLFATTIAANIAYGCE---ATQEEIEKAAEQANAHNFIASFEEGYQTQvgergvkLSGGQKQRVAIARAL 693
Cdd:PRK11248 72 -RGVVFQNEGLLPWRNVQDNVAFGLQlagVEKMQRLEIAHQMLKKVGLEGAEKRYIWQ-------LSGGQRQRVGIARAL 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1005434824 694 LMNPDVLLLDEATSALDAesehFVKEAIDRAMVN------RTVLVIAHRL-STVRNADQVLVI--DKGHIVER 757
Cdd:PRK11248 144 AANPQLLLLDEPFGALDA----FTREQMQTLLLKlwqetgKQVLLITHDIeEAVFMATELVLLspGPGRVVER 212
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
558-775 |
1.38e-19 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 94.59 E-value: 1.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVIS-IGRtnlaeldlfwlrrkIALVSQEPVLFATTIAAN 636
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKhSGR--------------ISFSPQTSWIMPGTIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 637 IAYGCEATQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHF 716
Cdd:TIGR01271 507 IIFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 717 VKEA-IDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHETLLAKAGVYKKLVL 775
Cdd:TIGR01271 587 IFEScLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRPDFSSLLL 646
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
558-758 |
1.53e-19 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 87.97 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIgrtnlaeldlfwlRRKIALVsqepvlfattIAANI 637
Cdd:cd03220 37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV-------------RGRVSSL----------LGLGG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 638 AYGCEATQEE-IE--------KAAEQANAHNFIASF---EEGYQTQVGErgvkLSGGQKQRVAIARALLMNPDVLLLDEA 705
Cdd:cd03220 94 GFNPELTGREnIYlngrllglSRKEIDEKIDEIIEFselGDFIDLPVKT----YSSGMKARLAFAIATALEPDILLIDEV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 706 TSALDAeseHFVKEAIDR--AMVN--RTVLVIAHRLSTVRN-ADQVLVIDKGHIVERG 758
Cdd:cd03220 170 LAVGDA---AFQEKCQRRlrELLKqgKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
559-762 |
1.58e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 92.78 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 559 LKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVI-------SIGRTNLAeldlfwLRRKIALVSQEPVLFAT 631
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEIlidgkpvRIRSPRDA------IALGIGMVHQHFMLVPN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 632 -TIAANIAYGCEATQEEI---EKAAEQanahnfIASFEEGY------QTQVGErgvkLSGGQKQRVAIARALLMNPDVLL 701
Cdd:COG3845 95 lTVAENIVLGLEPTKGGRldrKAARAR------IRELSERYgldvdpDAKVED----LSVGEQQRVEILKALYRGARILI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005434824 702 LDEATSAL-DAESEHFVkeAIDRAMVN--RTVLVIAHRLSTVR-NADQVLVIDKGHIVerGTHET 762
Cdd:COG3845 165 LDEPTAVLtPQEADELF--EILRRLAAegKSIIFITHKLREVMaIADRVTVLRRGKVV--GTVDT 225
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
541-758 |
2.46e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 90.86 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPsrpDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIG--RTNlaelDLFWLRRK 618
Cdd:PRK11000 4 VTLRNVTKAYG---DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGekRMN----DVPPAERG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 619 IALVSQEPVLFA-TTIAANIAYGCE---ATQEEIEKAAEQAN-----AHnfiasfeegyqtqVGERGVK-LSGGQKQRVA 688
Cdd:PRK11000 77 VGMVFQSYALYPhLSVAENMSFGLKlagAKKEEINQRVNQVAevlqlAH-------------LLDRKPKaLSGGQRQRVA 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1005434824 689 IARALLMNPDVLLLDEATSALDAESEHFVKEAIDR--AMVNRTVLVIAH-RLSTVRNADQVLVIDKGHIVERG 758
Cdd:PRK11000 144 IGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRlhKRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
552-770 |
3.51e-19 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 90.67 E-value: 3.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 552 SRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIALVSQEPVL-FA 630
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSLsFE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 631 TTIAANIAYG-----------CEATQEEIEKAAEQANAHNFIAsfeegyqtqvgeRGV-KLSGGQKQRVAIARALLMNPD 698
Cdd:PRK09536 92 FDVRQVVEMGrtphrsrfdtwTETDRAAVERAMERTGVAQFAD------------RPVtSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 699 VLLLDEATSALDAesEHFVKE-AIDRAMVN--RTVLVIAHRLS-TVRNADQVLVIDKGHIVERG------THETLLAKAG 768
Cdd:PRK09536 160 VLLLDEPTASLDI--NHQVRTlELVRRLVDdgKTAVAAIHDLDlAARYCDELVLLADGRVRAAGppadvlTADTLRAAFD 237
|
..
gi 1005434824 769 VY 770
Cdd:PRK09536 238 AR 239
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
562-761 |
4.28e-19 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 89.89 E-value: 4.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 562 MSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFwlRRKIALVSQEPVLFA-TTIAANIAYG 640
Cdd:PRK11607 38 VSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY--QRPINMMFQSYALFPhMTVEQNIAFG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 641 CEatQEEIEKAAEQANAHNFIASFEegYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAE----SEHF 716
Cdd:PRK11607 116 LK--QDKLPKAEIASRVNEMLGLVH--MQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlrdrMQLE 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1005434824 717 VKEAIDRamVNRTVLVIAH-RLSTVRNADQVLVIDKGHIVERGTHE 761
Cdd:PRK11607 192 VVDILER--VGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPE 235
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
555-766 |
4.39e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 87.43 E-value: 4.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 555 DSDVLKGMSFELKPGETVALVGPSGGGKST---VISLLERfYDPKSGVISIGRTNLAELD--------LFwlrrkiaLVS 623
Cdd:COG0396 12 GKEILKGVNLTIKPGEVHAIMGPNGSGKSTlakVLMGHPK-YEVTSGSILLDGEDILELSpderaragIF-------LAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 624 QEPV--------LFATTIAANIAYGCEATQEEIEKAAEQANAHNFIASFeegyqtqvGERGV--KLSGGQKQRVAIARAL 693
Cdd:COG0396 84 QYPVeipgvsvsNFLRTALNARRGEELSAREFLKLLKEKMKELGLDEDF--------LDRYVneGFSGGEKKRNEILQML 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1005434824 694 LMNPDVLLLDEATSALDAESEHFVKEAIDRAMV-NRTVLVIAH--RLSTVRNADQVLVIDKGHIVERGTHEtlLAK 766
Cdd:COG0396 156 LLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKE--LAL 229
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
556-754 |
1.28e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 85.64 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 556 SDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSG-VISIGR-------TNLAELDlfwlRRKIALVSQ-EP 626
Cdd:PRK11629 22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGdVIFNGQpmsklssAAKAELR----NQKLGFIYQfHH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 627 VLFATTIAANIAY----GCEATQEEIEKAAEQANAhnfiasfeEGYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLL 702
Cdd:PRK11629 98 LLPDFTALENVAMplliGKKKPAEINSRALEMLAA--------VGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1005434824 703 DEATSALDAESEHFVKEAIDRAMVNR--TVLVIAHRLSTVRNADQVLVIDKGHI 754
Cdd:PRK11629 170 DEPTGNLDARNADSIFQLLGELNRLQgtAFLVVTHDLQLAKRMSRQLEMRDGRL 223
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
557-755 |
1.56e-18 |
|
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: 85.40 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 557 DVLKGMSFELKPGETVALVGPSGGGKST---VISLLERFYDPKSGVISIgrtNLAELDLFWLRRKIALVSQEPVLFAT-- 631
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTlldAISGRVEGGGTTSGQILF---NGQPRKPDQFQKCVAYVRQDDILLPGlt 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 632 -----TIAANIAYGCEATQEEIEKAAEqanahnfIASFEEGYQTQVGERGVK-LSGGQKQRVAIARALLMNPDVLLLDEA 705
Cdd:cd03234 98 vretlTYTAILRLPRKSSDAIRKKRVE-------DVLLRDLALTRIGGNLVKgISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1005434824 706 TSALDAESEH-FVKEAIDRAMVNRTVLVIAH--RLSTVRNADQVLVIDKGHIV 755
Cdd:cd03234 171 TSGLDSFTALnLVSTLSQLARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIV 223
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
545-777 |
1.63e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.21 E-value: 1.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 545 DVYFAYPsrpDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSG-VISIGRT-NLAELDLFWLRRKIALV 622
Cdd:PRK13638 6 DLWFRYQ---DEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGaVLWQGKPlDYSKRGLLALRQQVATV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 623 SQEP--VLFATTIAANIAYGCE---ATQEEIEKAAEQA----NAHNFiasFEEGYQTqvgergvkLSGGQKQRVAIARAL 693
Cdd:PRK13638 83 FQDPeqQIFYTDIDSDIAFSLRnlgVPEAEITRRVDEAltlvDAQHF---RHQPIQC--------LSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 694 LMNPDVLLLDEATSALDAESEHFVKEAIDR-AMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHETLLAKAGVYK 771
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHGAPGEVFACTEAME 231
|
....*.
gi 1005434824 772 KLVLRQ 777
Cdd:PRK13638 232 QAGLTQ 237
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
558-772 |
2.03e-18 |
|
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: 85.29 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRK-IALVSQEPVLFAT-TIAA 635
Cdd:cd03218 15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYLPQEASIFRKlTVEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 636 NIAYGCEATQEEIEKAAEQANAhnFIASFeeGYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALD----A 711
Cdd:cd03218 95 NILAVLEIRGLSKKEREEKLEE--LLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDpiavQ 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1005434824 712 ESEHFVKEAIDRAMvnrTVLVIAHRLS-TVRNADQVLVIDKGHIVERGTHETLLAKAGVYKK 772
Cdd:cd03218 171 DIQKIIKILKDRGI---GVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIAANELVRKV 229
|
|
| ABC_6TM_YwjA_like |
cd18549 |
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ... |
226-489 |
2.53e-18 |
|
Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar proteins; This group represents the six-transmembrane helical domain of an uncharacterized ABC transporter YwjA from Bacillus subtilis and similar proteins. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.
Pssm-ID: 349993 [Multi-domain] Cd Length: 295 Bit Score: 86.35 E-value: 2.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 226 LFIASVAL-LASSGSQIAAPYFFGRVIQASMEEG-MSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQLF 303
Cdd:cd18549 3 LFFLDLFCaVLIAALDLVFPLIVRYIIDDLLPSKnLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 304 ASVVEQEVAFFDSNRTGELINRLSSDTQviqnaltvNVS--------MLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPI 375
Cdd:cd18549 83 EHLQKLSFSFFDNNKTGQLMSRITNDLF--------DISelahhgpeDLFISIITIIGSFIILLTINVPLTLIVFALLPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 376 VGIGAQRY-GSFVQGLRK----------RFQDelaaasstaeeAIANIRTVRSFSQERKSMNSYDTDID-------KSYK 437
Cdd:cd18549 155 MIIFTIYFnKKMKKAFRRvrekigeinaQLED-----------SLSGIRVVKAFANEEYEIEKFDEGNDrfleskkKAYK 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1005434824 438 SGAKLALASGFFNGVIgiigqgaVVLVLWYGGSLVNKHELDVGILTAFMLYT 489
Cdd:cd18549 224 AMAYFFSGMNFFTNLL-------NLVVLVAGGYFIIKGEITLGDLVAFLLYV 268
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
535-763 |
2.93e-18 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 88.95 E-value: 2.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 535 STVNQVIQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFW 614
Cdd:PRK15439 6 TTAPPLLCARSISKQYSGVE---VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 615 LRR-KIALVSQEPVLFAT-TIAANIAYGCEATQEEIEKAAE-------QANAHNFIASFEegyqtqVGERgvklsggqkQ 685
Cdd:PRK15439 83 AHQlGIYLVPQEPLLFPNlSVKENILFGLPKRQASMQKMKQllaalgcQLDLDSSAGSLE------VADR---------Q 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 686 RVAIARALLMNPDVLLLDEATSALD-AESEHFVKEAidRAMVNRTV--LVIAHRLSTVRN-ADQVLVIDKGHIVERGTHE 761
Cdd:PRK15439 148 IVEILRGLMRDSRILILDEPTASLTpAETERLFSRI--RELLAQGVgiVFISHKLPEIRQlADRISVMRDGTIALSGKTA 225
|
..
gi 1005434824 762 TL 763
Cdd:PRK15439 226 DL 227
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
559-776 |
3.21e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 86.68 E-value: 3.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 559 LKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIG-------RTNLAeldlfwlrRKIALV----SQ--- 624
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLgyvpfkrRKEFA--------RRIGVVfgqrSQlww 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 625 -EPVLFATTIAANIaYgceatqeEIEKAAEQANAHNFIASFEEG--YQTQVgeRgvKLSGGQKQRVAIARALLMNPDVLL 701
Cdd:COG4586 110 dLPAIDSFRLLKAI-Y-------RIPDAEYKKRLDELVELLDLGelLDTPV--R--QLSLGQRMRCELAAALLHRPKILF 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 702 LDEATSALDAESEHFVKEAIDRamVNR----TVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHETLLAKAGVYKKLVLR 776
Cdd:COG4586 178 LDEPTIGLDVVSKEAIREFLKE--YNRergtTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKERFGPYKTIVLE 255
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
558-765 |
4.99e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 88.22 E-value: 4.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKS-TVISLLERFYDPK----SGVISIGRTNLAELDLFWLRR----KIALVSQEPVL 628
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRGvrgnKIAMIFQEPMV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 629 -----------FATTIAANIAYGCEATQEEIEKAAEQA---NAHNFIASFEEgyqtqvgergvKLSGGQKQRVAIARALL 694
Cdd:PRK15134 104 slnplhtlekqLYEVLSLHRGMRREAARGEILNCLDRVgirQAAKRLTDYPH-----------QLSGGERQRVMIAMALL 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1005434824 695 MNPDVLLLDEATSALD----AESEHFVKEAidRAMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHETLLA 765
Cdd:PRK15134 173 TRPELLIADEPTTALDvsvqAQILQLLREL--QQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLFS 246
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
555-761 |
6.60e-18 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 82.57 E-value: 6.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 555 DSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKsgvISIGRTNLAELDLFWL------RRKIALVSQEPVl 628
Cdd:cd03217 12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYE---VTEGEILFKGEDITDLppeeraRLGIFLAFQYPP- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 629 fattiaaniaygceatqeEIE--KAAeqanahNFIASFEEGyqtqvgergvkLSGGQKQRVAIARALLMNPDVLLLDEAT 706
Cdd:cd03217 88 ------------------EIPgvKNA------DFLRYVNEG-----------FSGGEKKRNEILQLLLLEPDLAILDEPD 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 707 SALDAESEHFVKEAIDR-AMVNRTVLVIAH--RLSTVRNADQVLVIDKGHIVERGTHE 761
Cdd:cd03217 133 SGLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGDKE 190
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
558-808 |
6.99e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 85.16 E-value: 6.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDlfwlRRKIALVSQEPVLFAT-TIAAN 636
Cdd:COG4152 16 AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIGYLPEERGLYPKmKVGEQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 637 IAY-----GceatqeeIEKAAEQANAHNFIASFEegyqtqVGERGVK----LSGGQKQRVAIARALLMNPDVLLLDEATS 707
Cdd:COG4152 92 LVYlarlkG-------LSKAEAKRRADEWLERLG------LGDRANKkveeLSKGNQQKVQLIAALLHDPELLILDEPFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 708 ALDAESEHFVKEAI-DRAMVNRTVLVIAHRLSTV-RNADQVLVIDKGHIVERGTHETLLAKAGvYKKLVLRqlsvsqhen 785
Cdd:COG4152 159 GLDPVNVELLKDVIrELAAKGTTVIFSSHQMELVeELCDRIVIINKGRKVLSGSVDEIRRQFG-RNTLRLE--------- 228
|
250 260
....*....|....*....|...
gi 1005434824 786 lsaGDLDPNLLgSEQPSVEEVEE 808
Cdd:COG4152 229 ---ADGDAGWL-RALPGVTVVEE 247
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
541-711 |
7.36e-18 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 86.05 E-value: 7.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSrpDSDVLKGMSFELKPGETVALVGPSGGGKSTV---ISLLERFydpKSGVISIGRTNLAEL---Dlfw 614
Cdd:PRK11650 4 LKLQAVRKSYDG--KTQVIKGIDLDVADGEFIVLVGPSGCGKSTLlrmVAGLERI---TSGEIWIGGRVVNELepaD--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 615 lrRKIALVSQEPVLFA-TTIAANIAYGC-------EATQEEIEKAAEqanahnfIASFEEGYQtqvgERGVKLSGGQKQR 686
Cdd:PRK11650 76 --RDIAMVFQNYALYPhMSVRENMAYGLkirgmpkAEIEERVAEAAR-------ILELEPLLD----RKPRELSGGQRQR 142
|
170 180
....*....|....*....|....*
gi 1005434824 687 VAIARALLMNPDVLLLDEATSALDA 711
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEPLSNLDA 167
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
555-766 |
7.83e-18 |
|
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: 87.55 E-value: 7.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 555 DSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERF--YDPKSGVI-----------------SIGR------TNLAE 609
Cdd:TIGR03269 12 GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpsKVGEpcpvcgGTLEP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 610 LDL-FW---------LRRKIAlvsqepVLFATTIAAniaYGCEATQEEIEKAAEQANAHNFIA---SFEEGYQTQVGER- 675
Cdd:TIGR03269 92 EEVdFWnlsdklrrrIRKRIA------IMLQRTFAL---YGDDTVLDNVLEALEEIGYEGKEAvgrAVDLIEMVQLSHRi 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 676 ---GVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNR--TVLVIAHRLSTVRN-ADQVLVI 749
Cdd:TIGR03269 163 thiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASgiSMVLTSHWPEVIEDlSDKAIWL 242
|
250
....*....|....*..
gi 1005434824 750 DKGHIVERGTHETLLAK 766
Cdd:TIGR03269 243 ENGEIKEEGTPDEVVAV 259
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
559-759 |
7.99e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 84.67 E-value: 7.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 559 LKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGR----TNLAEL-DLFWLRRKIALVSQEP--VLFAT 631
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIkEVKRLRKEIGLVFQFPeyQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 632 TIAANIAYGCEATQEEIEKAAEQANAHNFIASFEEGYqtqVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDA 711
Cdd:PRK13645 107 TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDY---VKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDP 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1005434824 712 ESEH-FVK--EAIDRAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGT 759
Cdd:PRK13645 184 KGEEdFINlfERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
553-759 |
9.20e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.80 E-value: 9.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 553 RPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLErFYDPKSGVISIGRT-NLAELDLFWLRRKIALVSQEPVLFAT 631
Cdd:TIGR00955 35 RPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKGVKGSGSVLlNGMPIDAKEMRAISAYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 632 -------TIAANIAYGCEATQEEIEKAAEQ-------ANAHNFIasfeegyqTQVGERGVKLSGGQKQRVAIARALLMNP 697
Cdd:TIGR00955 114 ltvrehlMFQAHLRMPRRVTKKEKRERVDEvlqalglRKCANTR--------IGVPGRVKGLSGGERKRLAFASELLTDP 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005434824 698 DVLLLDEATSALDAESEHFVKEAIDR-AMVNRTVLVIAHRLST--VRNADQVLVIDKGHIVERGT 759
Cdd:TIGR00955 186 PLLFCDEPTSGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGS 250
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
553-765 |
1.60e-17 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 83.30 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 553 RPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIALVSQEPV----- 627
Cdd:PRK15112 23 RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPStslnp 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 628 ------LFATTIAANIAYGCEATQEEIEKAAEQANAHNFIASFeegYQTQvgergvkLSGGQKQRVAIARALLMNPDVLL 701
Cdd:PRK15112 103 rqrisqILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASY---YPHM-------LAPGQKQRLGLARALILRPKVII 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1005434824 702 LDEATSALDAES---------EHFVKEAIDRAMVNRTVLVIAHRlstvrnADQVLVIDKGHIVERGTHETLLA 765
Cdd:PRK15112 173 ADEALASLDMSMrsqlinlmlELQEKQGISYIYVTQHLGMMKHI------SDQVLVMHQGEVVERGSTADVLA 239
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
559-711 |
1.99e-17 |
|
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: 82.13 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 559 LKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISI-GRtnlaELDLFWLRRKIalVSQEPVLFA-TTIAAN 636
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILeGK----QITEPGPDRMV--VFQNYSLLPwLTVREN 74
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005434824 637 IAYGCEATQEEIEKAAEQANAHNFIASFeeGYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDA 711
Cdd:TIGR01184 75 IALAVDRVLPDLSKSERRAIVEEHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDA 147
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
560-763 |
2.96e-17 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 83.99 E-value: 2.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 560 KGMSFELKPGETVALVGPSGGGKST----VISLLErfydPKSGVIS-IGR--TNLAELDLFWLRRKIALVSQEPVlfAT- 631
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTfaraIIGLVK----ATDGEVAwLGKdlLGMKDDEWRAVRSDIQMIFQDPL--ASl 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 632 ----TIAANIA-----YGCEATQEEIEKAAEQANAH-----NFIASFEEgyqtqvgergvKLSGGQKQRVAIARALLMNP 697
Cdd:PRK15079 112 nprmTIGEIIAeplrtYHPKLSRQEVKDRVKAMMLKvgllpNLINRYPH-----------EFSGGQCQRIGIARALILEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1005434824 698 DVLLLDEATSALD----AESEHFVKEaIDRAMvNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHETL 763
Cdd:PRK15079 181 KLIICDEPVSALDvsiqAQVVNLLQQ-LQREM-GLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
525-761 |
5.28e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 85.29 E-value: 5.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 525 SIDLEGGKKLSTVNQVIQFQDvyfaypSRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGR 604
Cdd:PRK10261 4 SDELDARDVLAVENLNIAFMQ------EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 605 ----------TNLAELDLFWLRR----KIALVSQEPV-----LFAT--TIAANIAYGCEATQEEIEKAAEQANAHNFIAS 663
Cdd:PRK10261 78 mllrrrsrqvIELSEQSAAQMRHvrgaDMAMIFQEPMtslnpVFTVgeQIAESIRLHQGASREEAMVEAKRMLDQVRIPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 664 feegYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAI-----DRAMvnrTVLVIAHRLS 738
Cdd:PRK10261 158 ----AQTILSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIkvlqkEMSM---GVIFITHDMG 230
|
250 260
....*....|....*....|....
gi 1005434824 739 TVRN-ADQVLVIDKGHIVERGTHE 761
Cdd:PRK10261 231 VVAEiADRVLVMYQGEAVETGSVE 254
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
573-761 |
1.03e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 82.61 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 573 ALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDL-FWL---RRKIALVSQEPVLFA-TTIAANIAYGCeatqee 647
Cdd:PRK11144 28 AIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKgICLppeKRRIGYVFQDARLFPhYKVRGNLRYGM------ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 648 iekaAEQANAHnfiasfeegYQTQVGERGVK---------LSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVK 718
Cdd:PRK11144 102 ----AKSMVAQ---------FDKIVALLGIEplldrypgsLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1005434824 719 EAIDR--AMVNRTVLVIAHRLSTV-RNADQVLVIDKGHIVERGTHE 761
Cdd:PRK11144 169 PYLERlaREINIPILYVSHSLDEIlRLADRVVVLEQGKVKAFGPLE 214
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
556-754 |
1.44e-16 |
|
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: 78.24 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 556 SDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELD-LFWLRRKIALVSQEPV---LFAT 631
Cdd:cd03215 13 KGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIAYVPEDRKregLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 632 -TIAANIAygceatqeeiekaaeqanahnfIASFeegyqtqvgergvkLSGGQKQRVAIARALLMNPDVLLLDEATSALD 710
Cdd:cd03215 93 lSVAENIA----------------------LSSL--------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVD 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1005434824 711 AESEHFVKEAIDR-AMVNRTVLVIAHRLSTV-RNADQVLVIDKGHI 754
Cdd:cd03215 137 VGAKAEIYRLIRElADAGKAVLLISSELDELlGLCDRILVMYEGRI 182
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
561-761 |
2.12e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 79.65 E-value: 2.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 561 GMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIA-------------------L 621
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVvrtfqhvrlfremtvienlL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 622 VSQE--------PVLFATTiaaniAYgCEATQEEIEKAA---EQANAHNFiASFEEGyqtqvgergvKLSGGQKQRVAIA 690
Cdd:PRK11300 103 VAQHqqlktglfSGLLKTP-----AF-RRAESEALDRAAtwlERVGLLEH-ANRQAG----------NLAYGQQRRLEIA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1005434824 691 RALLMNPDVLLLDEATSALDAESEHFVKEAID--RAMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHE 761
Cdd:PRK11300 166 RCMVTQPEILMLDEPAAGLNPKETKELDELIAelRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPE 239
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
552-713 |
2.33e-16 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 78.17 E-value: 2.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 552 SRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWlRRKIALVSQEPVLFAT 631
Cdd:TIGR01189 9 SRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP-HENILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 632 -TIAANIAYGCE---ATQEEIEKAAEQANahnfIASFEegyQTQVGErgvkLSGGQKQRVAIARALLMNPDVLLLDEATS 707
Cdd:TIGR01189 88 lSALENLHFWAAihgGAQRTIEDALAAVG----LTGFE---DLPAAQ----LSAGQQRRLALARLWLSRRPLWILDEPTT 156
|
....*.
gi 1005434824 708 ALDAES 713
Cdd:TIGR01189 157 ALDKAG 162
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
549-753 |
3.55e-16 |
|
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: 82.29 E-value: 3.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 549 AYPsrPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLerfydpkSGVIS--IGRTNLAEldlfwlRRKIALVSQEP 626
Cdd:TIGR03719 13 VVP--PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AGVDKdfNGEARPQP------GIKVGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 627 VLFAT-TIAANIAYGCE---------------------------ATQEEIEKAAEQANAHNFIASFE---EGYQTQVGER 675
Cdd:TIGR03719 78 QLDPTkTVRENVEEGVAeikdaldrfneisakyaepdadfdklaAEQAELQEIIDAADAWDLDSQLEiamDALRCPPWDA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 676 GV-KLSGGQKQRVAIARALLMNPDVLLLDEATSALDAES----EHFVKEaidramVNRTVLVIAH-R--LSTVrnADQVL 747
Cdd:TIGR03719 158 DVtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE------YPGTVVAVTHdRyfLDNV--AGWIL 229
|
....*.
gi 1005434824 748 VIDKGH 753
Cdd:TIGR03719 230 ELDRGR 235
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
549-769 |
4.92e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 78.40 E-value: 4.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 549 AYPSRpdsDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFW-LRRKIALVSQEPV 627
Cdd:PRK10895 12 AYKGR---RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEAS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 628 LFATTIAANIAYGCEATQEEIEKAAEQANAHNFIASFE-EGYQTQVGErgvKLSGGQKQRVAIARALLMNPDVLLLDEAT 706
Cdd:PRK10895 89 IFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHiEHLRDSMGQ---SLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 707 SALDAESEHFVKEAI----DRAMvnrTVLVIAHRL-STVRNADQVLVIDKGHIVERGTHETLLAKAGV 769
Cdd:PRK10895 166 AGVDPISVIDIKRIIehlrDSGL---GVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEILQDEHV 230
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
558-761 |
9.88e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.85 E-value: 9.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISigRTnlAELDLFWLRRKIALVSQEPVlfatTIAANI 637
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--RN--GKLRIGYVPQKLYLDTTLPL----TVNRFL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 638 AYGCEATQEEIEKAAEQANAHNFIasfEEGYQtqvgergvKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFV 717
Cdd:PRK09544 91 RLRPGTKKEDILPALKRVQAGHLI---DAPMQ--------KLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1005434824 718 KEAID--RAMVNRTVLVIAHRLSTVR-NADQVLVIDkGHIVERGTHE 761
Cdd:PRK09544 160 YDLIDqlRRELDCAVLMVSHDLHLVMaKTDEVLCLN-HHICCSGTPE 205
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
558-755 |
9.95e-16 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 77.82 E-value: 9.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISI-GR--TNLAEldlfWLR-RKIALVSQEPVL---FA 630
Cdd:COG1101 21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIdGKdvTKLPE----YKRaKYIGRVFQDPMMgtaPS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 631 TTIAAN--IAY--------GCEATQEEIEKAAEQanahnfIASFEEGY----QTQVGergvKLSGGQKQrvaiARALLM- 695
Cdd:COG1101 97 MTIEENlaLAYrrgkrrglRRGLTKKRRELFREL------LATLGLGLenrlDTKVG----LLSGGQRQ----ALSLLMa 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 696 ---NPDVLLLDEATSALDAESEHFVKEAIDRaMVNR---TVLVIAHRLS-TVRNADQVLVIDKGHIV 755
Cdd:COG1101 163 tltKPKLLLLDEHTAALDPKTAALVLELTEK-IVEEnnlTTLMVTHNMEqALDYGNRLIMMHEGRII 228
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
541-759 |
1.39e-15 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 77.43 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIA 620
Cdd:COG4604 2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 621 LVSQEPVlFAT--TIAANIAYG---------CEATQEEIEKAAEQANahnfIASFEEGYQTQvgergvkLSGGQKQRVAI 689
Cdd:COG4604 79 ILRQENH-INSrlTVRELVAFGrfpyskgrlTAEDREIIDEAIAYLD----LEDLADRYLDE-------LSGGQRQRAFI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 690 ARALLMNPDVLLLDEATSALDaesehfVKEAID-----RAMV---NRTVLVIAHRLstvrN-----ADQVLVIDKGHIVE 756
Cdd:COG4604 147 AMVLAQDTDYVLLDEPLNNLD------MKHSVQmmkllRRLAdelGKTVVIVLHDI----NfascyADHIVAMKDGRVVA 216
|
...
gi 1005434824 757 RGT 759
Cdd:COG4604 217 QGT 219
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
550-765 |
2.61e-15 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 76.22 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 550 YPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVisllerFY------DPKSGVISIGRTNLAELDLfWLR-RK-IAL 621
Cdd:COG1137 13 YGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHLPM-HKRaRLgIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 622 VSQEPVLFAT-TIAANIAygceATQEEIEKAAEQANA--HNFIASFeegyqtQVGE----RGVKLSGGQKQRVAIARALL 694
Cdd:COG1137 83 LPQEASIFRKlTVEDNIL----AVLELRKLSKKEREErlEELLEEF------GITHlrksKAYSLSGGERRRVEIARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1005434824 695 MNPDVLLLDEATSALD----AESEHFVKEAIDRAMvnrTVLVIAHRlstVRNA----DQVLVIDKGHIVERGTHETLLA 765
Cdd:COG1137 153 TNPKFILLDEPFAGVDpiavADIQKIIRHLKERGI---GVLITDHN---VRETlgicDRAYIISEGKVLAEGTPEEILN 225
|
|
| ABC_6TM_CvaB_RaxB_like |
cd18567 |
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ... |
220-488 |
2.85e-15 |
|
Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 secretion systems, CvaB and RaxB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the peptidase-containing ABC transporter subunit of T1SS (Type 1 secretion systems), such as Escherichia coli colicin V secretion/processing ATP-binding protein CvaB and putative ABC transporter RaxB. These ABC-transporter proteins carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion. RaxB is part of the T1SS RaxABC, which is responsible for the type 1-dependent secretion of the bacterial quorum-sensing molecule AvrXa21. Both CvaB and RaxB belong to a subgroup of T1SS ABC transporters that contain a C39 peptidase domain. T1SS are found in pathogenic Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium.
Pssm-ID: 350011 [Multi-domain] Cd Length: 294 Bit Score: 77.12 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 220 KPELCVLFIASVALLASSgsqIAAPYFFGRVI-QASMEEGMSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARI 298
Cdd:cd18567 1 KRALLQILLLSLALELFA---LASPLYLQLVIdEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 299 RKQLFASVVEQEVAFFDSNRTGELINRLSSdTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTG-VLISVVPIVG 377
Cdd:cd18567 78 TSNLFRHLLRLPLSYFEKRHLGDIVSRFGS-LDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALiVLAAVALYAL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 378 IgaqRYGSFVQgLRKRFQDELAAASSTAEEAIANIR---TVRSFSQE--RKS--MNSYDTDIDKSYKSGaKLALASGFFN 450
Cdd:cd18567 157 L---RLALYPP-LRRATEEQIVASAKEQSHFLETIRgiqTIKLFGREaeREArwLNLLVDAINADIRLQ-RLQILFSAAN 231
|
250 260 270
....*....|....*....|....*....|....*...
gi 1005434824 451 GVIGIIGQgavVLVLWYGGSLVNKHELDVGILTAFMLY 488
Cdd:cd18567 232 GLLFGLEN---ILVIYLGALLVLDGEFTVGMLFAFLAY 266
|
|
| ABC_6TM_HetC_like |
cd18568 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ... |
226-510 |
3.00e-15 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.
Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 77.22 E-value: 3.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 226 LFIASVaLLASSGsqIAAPYFfgrvIQASMEEGMSHLNKTIVLLSLIYLAGA-----LAALVRSWLFTLAGQRLVARIRK 300
Cdd:cd18568 7 ILLASL-LLQLLG--LALPLF----TQIILDRVLVHKNISLLNLILIGLLIVgifqiLLSAVRQYLLDYFANRIDLSLLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 301 QLFASVVEQEVAFFDSNRTGELINRLSsDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGA 380
Cdd:cd18568 80 DFYKHLLSLPLSFFASRKVGDIITRFQ-ENQKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 381 QRYGSFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQER----KSMNSYDTDIDKSYKsGAKLALASGFFNGVIGII 456
Cdd:cd18568 159 LLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERpirwRWENKFAKALNTRFR-GQKLSIVLQLISSLINHL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1005434824 457 GQgavVLVLWYGGSLVNKHELDVGILTAF-MLYTlNVAMAFAFLSSVYGDFMQAV 510
Cdd:cd18568 238 GT---IAVLWYGAYLVISGQLTIGQLVAFnMLFG-SVINPLLALVGLWDELQETR 288
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
562-758 |
3.69e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.51 E-value: 3.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 562 MSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRT---NLAELDLFWLRRKIALVSQEPvlFAT-----TI 633
Cdd:PRK10261 343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridTLSPGKLQALRRDIQFIFQDP--YASldprqTV 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 634 AANIAygceatqeeiekaaEQANAHNFIASfeEGYQTQVG---ER-GVK----------LSGGQKQRVAIARALLMNPDV 699
Cdd:PRK10261 421 GDSIM--------------EPLRVHGLLPG--KAAAARVAwllERvGLLpehawrypheFSGGQRQRICIARALALNPKV 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1005434824 700 LLLDEATSALDAEsehfVKEAIDRAMVNR------TVLVIAHRLSTV-RNADQVLVIDKGHIVERG 758
Cdd:PRK10261 485 IIADEAVSALDVS----IRGQIINLLLDLqrdfgiAYLFISHDMAVVeRISHRVAVMYLGQIVEIG 546
|
|
| ABC_6TM_CyaB_HlyB_like |
cd18588 |
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ... |
233-509 |
3.95e-15 |
|
Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunits of T1SS, such as CyaG and HlyB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. Additionally, CyaB is part of the three T1SS complex proteins for adenylate cyclase toxin CyaA, which is a primary virulence factor in Bordetella pertussis: CyaB (an ABC transporter) CyaD (a membrane fusion protein), and CyaE (an outer membrane protein).
Pssm-ID: 350032 [Multi-domain] Cd Length: 294 Bit Score: 76.77 E-value: 3.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 233 LLASSGSQI---AAPYFFGRVI-QASMEEGMSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQLFASVVE 308
Cdd:cd18588 8 LLASLFLQLfalVTPLFFQVIIdKVLVHRSLSTLDVLAIGLLVVALFEAVLSGLRTYLFSHTTNRIDAELGARLFRHLLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 309 QEVAFFDSNRTGELINR---LSSdtqvIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTG-VLISVVPIVGIgaqryg 384
Cdd:cd18588 88 LPLSYFESRQVGDTVARvreLES----IRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLiVLASLPLYALL------ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 385 SFVQG--LRKRFQDELAAASSTAEE---AIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQG 459
Cdd:cd18588 158 SLLVTpiLRRRLEEKFQRGAENQSFlveTVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIVQLIQKL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1005434824 460 AVVLVLWYGGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQA 509
Cdd:cd18588 238 TTLAILWFGAYLVMDGELTIGQLIAFNMLAGQVSQPVLRLVQLWQDFQQA 287
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
527-765 |
1.10e-14 |
|
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: 77.54 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 527 DLEGGKKLSTVNQVIQFQDVYFAYPSrPDSDVLK---GMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVIS-- 601
Cdd:TIGR03269 266 EVEKECEVEVGEPIIKVRNVSKRYIS-VDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvr 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 602 -----IGRTNLAELDLFWLRRKIALVSQEPVLFA-TTIAANIAygcEATQEEI--EKAAEQANAHNFIASFEEGYQTQVG 673
Cdd:TIGR03269 345 vgdewVDMTKPGPDGRGRAKRYIGILHQEYDLYPhRTVLDNLT---EAIGLELpdELARMKAVITLKMVGFDEEKAEEIL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 674 ER-GVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAI--DRAMVNRTVLVIAHRLSTVRN-ADQVLVI 749
Cdd:TIGR03269 422 DKyPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVLDvCDRAALM 501
|
250
....*....|....*.
gi 1005434824 750 DKGHIVERGTHETLLA 765
Cdd:TIGR03269 502 RDGKIVKIGDPEEIVE 517
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
552-714 |
2.30e-14 |
|
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: 72.53 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 552 SRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIALVSQEPVLFAT 631
Cdd:cd03231 9 ERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPGIKTTL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 632 TIAANIAYGCE-ATQEEIEKAAEQANahnfIASFEEGYQTQvgergvkLSGGQKQRVAIARALLMNPDVLLLDEATSALD 710
Cdd:cd03231 89 SVLENLRFWHAdHSDEQVEEALARVG----LNGFEDRPVAQ-------LSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
....
gi 1005434824 711 AESE 714
Cdd:cd03231 158 KAGV 161
|
|
| ABC_6TM_ATM1_ABCB7 |
cd18582 |
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ... |
231-510 |
2.34e-14 |
|
Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1/ABCB7 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia.
Pssm-ID: 350026 [Multi-domain] Cd Length: 292 Bit Score: 74.46 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 231 VALLASSGSQIAAPYFFGRVIQAsMEEGMSHLNKTIVLLSLIY----LAGALAALVRSWLFTLAGQRLVARIRKQLFASV 306
Cdd:cd18582 3 LLLVLAKLLNVAVPFLLKYAVDA-LSAPASALLAVPLLLLLAYglarILSSLFNELRDALFARVSQRAVRRLALRVFRHL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 307 VEQEVAFFDSNRTGELinrlssdTQVI---QNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAqrY 383
Cdd:cd18582 82 HSLSLRFHLSRKTGAL-------SRAIergTRGIEFLLRFLLFNILPTILELLLVCGILWYLYGWSYALITLVTVAL--Y 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 384 GSF---VQGLRKRFQDELAAASSTAEEAI----ANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGII 456
Cdd:cd18582 153 VAFtikVTEWRTKFRREMNEADNEANAKAvdslLNYETVKYFNNEEYEAERYDKALAKYEKAAVKSQTSLALLNIGQALI 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1005434824 457 GQGAVVLVLWYGGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAV 510
Cdd:cd18582 233 ISLGLTAIMLLAAQGVVAGTLTVGDFVLVNTYLLQLYQPLNFLGFVYREIRQSL 286
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
538-739 |
4.10e-14 |
|
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: 75.74 E-value: 4.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 538 NQVIQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTnlaeldlfwlrR 617
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET-----------V 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 618 KIALVSQ--EPVLFATTIAANIAYGceatQEEIEKAAEQANAHNFIASFE---EGYQTQVGErgvkLSGGQKQRVAIARA 692
Cdd:TIGR03719 386 KLAYVDQsrDALDPNKTVWEEISGG----LDIIKLGKREIPSRAYVGRFNfkgSDQQKKVGQ----LSGGERNRVHLAKT 457
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1005434824 693 LLMNPDVLLLDEATSALDAESEHFVKEAIDRamVNRTVLVIAH------RLST 739
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLDVETLRALEEALLN--FAGCAVVISHdrwfldRIAT 508
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
559-761 |
4.99e-14 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 73.12 E-value: 4.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 559 LKGMSFELKPGETVALVGPSGGGKSTVISLLERFYD----PKSGVISIGRT-----NLAElDLFWLRRKIALVSQEPVLF 629
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGSHIELLGRTvqregRLAR-DIRKSRANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 630 -ATTIAANI---AYGCEA---------TQEEIEKAAeQANAHNFIASFEEgyqtqvgERGVKLSGGQKQRVAIARALLMN 696
Cdd:PRK09984 99 nRLSVLENVligALGSTPfwrtcfswfTREQKQRAL-QALTRVGMVHFAH-------QRVSTLSGGQQQRVAIARALMQQ 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 697 PDVLLLDEATSALDAESEHFVKEAIDRAMVNR--TVLVIAHRLS-TVRNADQVLVIDKGHIVERGTHE 761
Cdd:PRK09984 171 AKVILADEPIASLDPESARIVMDTLRDINQNDgiTVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQ 238
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
541-759 |
5.03e-14 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 72.57 E-value: 5.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVyfAYPSRpdsdvLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYdPKSGVISIGRTNLAELDLFWLRRKIA 620
Cdd:COG4138 1 LQLNDV--AVAGR-----LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 621 -LVSQEPVLFATTIAANIAYGceatQEEIEKAAEQANAHNFIASF---EEGYQTQVGergvKLSGGQKQRVAIARALL-- 694
Cdd:COG4138 73 yLSQQQSPPFAMPVFQYLALH----QPAGASSEAVEQLLAQLAEAlglEDKLSRPLT----QLSGGEWQRVRLAAVLLqv 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 695 ---MNPD--VLLLDEATSALD-AEsehfvKEAIDR-----AMVNRTVLVIAHRLS-TVRNADQVLVIDKGHIVERGT 759
Cdd:COG4138 145 wptINPEgqLLLLDEPMNSLDvAQ-----QAALDRllrelCQQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGE 216
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
547-755 |
5.47e-14 |
|
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: 71.52 E-value: 5.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 547 YFAYPSRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVI----SLLERFYDPkSGVISIGRTNLAELDLFWlRRKIALV 622
Cdd:cd03233 11 FTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLkalaNRTEGNVSV-EGDIHYNGIPYKEFAEKY-PGEIIYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 623 SQEPVLFATTiaaniaygceaTQEEIEKAAEQANAHNFIasfeegyqtqvgeRGVklSGGQKQRVAIARALLMNPDVLLL 702
Cdd:cd03233 89 SEEDVHFPTL-----------TVRETLDFALRCKGNEFV-------------RGI--SGGERKRVSIAEALVSRASVLCW 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1005434824 703 DEATSALDAESE-HFVKeaIDRAMV---NRTVLVIAHRLS--TVRNADQVLVIDKGHIV 755
Cdd:cd03233 143 DNSTRGLDSSTAlEILK--CIRTMAdvlKTTTFVSLYQASdeIYDLFDKVLVLYEGRQI 199
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
538-765 |
6.19e-14 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 72.42 E-value: 6.19e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 538 NQVIQFQDVYfAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKS-TVISLLerfydpksGVISIGRTNLA-------- 608
Cdd:PRK10418 2 PQQIELRNIA-LQAAQP---LVHGVSLTLQRGRVLALVGGSGSGKSlTCAAAL--------GILPAGVRQTAgrvlldgk 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 609 ELDLFWLR-RKIALVSQEP-VLF--ATTIAANIAYGCEATqeeiekaAEQANAHNFIASFEEgyqtqVG----ERGVKL- 679
Cdd:PRK10418 70 PVAPCALRgRKIATIMQNPrSAFnpLHTMHTHARETCLAL-------GKPADDATLTAALEA-----VGlenaARVLKLy 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 680 ----SGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRT--VLVIAHRLSTV-RNADQVLVIDKG 752
Cdd:PRK10418 138 pfemSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVaRLADDVAVMSHG 217
|
250
....*....|...
gi 1005434824 753 HIVERGTHETLLA 765
Cdd:PRK10418 218 RIVEQGDVETLFN 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
558-734 |
9.72e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 70.67 E-value: 9.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLF----WLRRKIALvsqEPVLfatTI 633
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAeachYLGHRNAM---KPAL---TV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 634 AANIA-----YGceATQEEIEKAAEQANAHNfIASFEEGYqtqvgergvkLSGGQKQRVAIARALLMNPDVLLLDEATSA 708
Cdd:PRK13539 91 AENLEfwaafLG--GEELDIAAALEAVGLAP-LAHLPFGY----------LSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180
....*....|....*....|....*.
gi 1005434824 709 LDAESEHFVKEAIdRAMVNRTVLVIA 734
Cdd:PRK13539 158 LDAAAVALFAELI-RAHLAQGGIVIA 182
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
542-764 |
1.03e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.13 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 542 QFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIAL 621
Cdd:PRK10575 13 ALRNVSFRVPGRT---LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 622 VSQE-PVLFATTIAANIAYG-----------CEATQEEIEKAAEQAN----AHNFIASfeegyqtqvgergvkLSGGQKQ 685
Cdd:PRK10575 90 LPQQlPAAEGMTVRELVAIGrypwhgalgrfGAADREKVEEAISLVGlkplAHRLVDS---------------LSGGERQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 686 RVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIA--HRLS-TVRNADQVLVIDKGHIVERGTHET 762
Cdd:PRK10575 155 RAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAvlHDINmAARYCDYLVALRGGEMIAQGTPAE 234
|
..
gi 1005434824 763 LL 764
Cdd:PRK10575 235 LM 236
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
558-710 |
2.36e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 70.19 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELD---LFWLR-RKIALVSQEPVLFATTI 633
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeeaRAKLRaKHVGFVFQSFMLIPTLN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 634 A-ANIAYGCEATQEEIEKAAEQAnahnfIASFEegyQTQVGER----GVKLSGGQKQRVAIARALLMNPDVLLLDEATSA 708
Cdd:PRK10584 105 AlENVELPALLRGESSRQSRNGA-----KALLE---QLGLGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADEPTGN 176
|
..
gi 1005434824 709 LD 710
Cdd:PRK10584 177 LD 178
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
558-756 |
2.50e-13 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 69.99 E-value: 2.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFY--DPKSGVISIGRTNLAeldlfwlrRKIALVsqEPVLFATTIAA 635
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFG--------REASLI--DAIGRKGDFKD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 636 NIaygceatqeEIEKAAEQANAHNFIASFEEgyqtqvgergvkLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEH 715
Cdd:COG2401 115 AV---------ELLNAVGLSDAVLWLRRFKE------------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1005434824 716 FVKEAIDRAM--VNRTVLVIAHRlSTVRNA---DQVLVIDKGHIVE 756
Cdd:COG2401 174 RVARNLQKLArrAGITLVVATHH-YDVIDDlqpDLLIFVGYGGVPE 218
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
532-759 |
2.59e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 72.06 E-value: 2.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 532 KKLSTVNQVIQFQDVYFAYpSRPDSDV--LKGMSFELKPGETVALVGPSGGGKS-TVISLLERFydPKSGVIS-----IG 603
Cdd:PRK09473 4 LAQQQADALLDVKDLRVTF-STPDGDVtaVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLL--AANGRIGgsatfNG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 604 RT--NLAELDLFWLR-RKIALVSQEPVlfaTTIAANIAYGcEATQE--EIEKAAEQANAhnfiasFEEGYQTQvgeRGVK 678
Cdd:PRK09473 81 REilNLPEKELNKLRaEQISMIFQDPM---TSLNPYMRVG-EQLMEvlMLHKGMSKAEA------FEESVRML---DAVK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 679 L--------------SGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAID--RAMVNRTVLVIAHRLSTVRN 742
Cdd:PRK09473 148 MpearkrmkmyphefSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNelKREFNTAIIMITHDLGVVAG 227
|
250
....*....|....*...
gi 1005434824 743 -ADQVLVIDKGHIVERGT 759
Cdd:PRK09473 228 iCDKVLVMYAGRTMEYGN 245
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
563-758 |
7.26e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.57 E-value: 7.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 563 SFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWL----RRKIA-----LVSQEP---VLFA 630
Cdd:PRK11701 26 SFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALseaeRRRLLrtewgFVHQHPrdgLRMQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 631 TTIAANIA----------YG---CEATQ--EEIEKAAEQanahnfiasfeegyqtqVGERGVKLSGGQKQRVAIARALLM 695
Cdd:PRK11701 106 VSAGGNIGerlmavgarhYGdirATAGDwlERVEIDAAR-----------------IDDLPTTFSGGMQQRLQIARNLVT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 696 NPDVLLLDEATSALDAESEHFVKEAIdRAMVNR---TVLVIAHRLSTVRN-ADQVLVIDKGHIVERG 758
Cdd:PRK11701 169 HPRLVFMDEPTGGLDVSVQARLLDLL-RGLVRElglAVVIVTHDLAVARLlAHRLLVMKQGRVVESG 234
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
549-735 |
7.73e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 71.69 E-value: 7.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 549 AYPsrPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLerfydpkSGV--ISIGRTNLAEldlfwlRRKIALVSQEP 626
Cdd:PRK11819 15 VVP--PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AGVdkEFEGEARPAP------GIKVGYLPQEP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 627 VLFAT-TIAANIAYGCEATQ------EEI------------EKAAEQA---------NAHNFIASFE---EGYQTQVGER 675
Cdd:PRK11819 80 QLDPEkTVRENVEEGVAEVKaaldrfNEIyaayaepdadfdALAAEQGelqeiidaaDAWDLDSQLEiamDALRCPPWDA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005434824 676 GV-KLSGGQKQRVAIARALLMNPDVLLLDEATSALDAES----EHFVKEaidramVNRTVLVIAH 735
Cdd:PRK11819 160 KVtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESvawlEQFLHD------YPGTVVAVTH 218
|
|
| ABC_6TM_MRP7_D2_like |
cd18605 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and ... |
224-383 |
9.69e-13 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 7, and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 7 (MRP7), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350049 [Multi-domain] Cd Length: 300 Bit Score: 69.87 E-value: 9.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 224 CVLFIASVALLasSGSQIAAPYFFGRVIQASMEEGMSHLNKTIV--LLSLIYLAGA--LAALVRSWLFTLAGQRLVARIR 299
Cdd:cd18605 1 LILILLSLILM--QASRNLIDFWLSYWVSHSNNSFFNFINDSFNffLTVYGFLAGLnsLFTLLRAFLFAYGGLRAARRLH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 300 KQLFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFM-FSLSAkltgVLISVVPIVGI 378
Cdd:cd18605 79 NKLLSSILFAKMSFFDKTPVGRILNRFSSDVYTIDDSLPFILNILLAQLFGLLGYLVVIcYQLPW----LLLLLLPLAFI 154
|
....*..
gi 1005434824 379 GA--QRY 383
Cdd:cd18605 155 YYriQRY 161
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18566 |
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ... |
226-487 |
1.53e-12 |
|
Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350010 [Multi-domain] Cd Length: 294 Bit Score: 69.15 E-value: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 226 LFIASVAL--LAssgsqIAAPYFF----GRVIQAsmeEGMSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIR 299
Cdd:cd18566 7 VLLASLFIniLA-----LATPLFIlqvyDRVIPN---ESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 300 KQLFASVVEQEVAFFDSNRTGELINRLSSDTQvIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTgvlisVVPIVGIG 379
Cdd:cd18566 79 NAAFEHLLSLPLSFFEREPSGAHLERLNSLEQ-IREFLTGQALLALLDLPFVLIFLGLIWYLGGKLV-----LVPLVLLG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 380 AQRYGSFVQG--LRKRFQDELAAASSTAEEAI---ANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIG 454
Cdd:cd18566 153 LFVLVAILLGpiLRRALKERSRADERRQNFLIetlTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQ 232
|
250 260 270
....*....|....*....|....*....|...
gi 1005434824 455 IIGQGAVVLVLWYGGSLVNKHELDVGILTAFML 487
Cdd:cd18566 233 LFSQVSMVAVVAFGALLVINGDLTVGALIACTM 265
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
227-765 |
1.56e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.77 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 227 FIASVAL-LASSGSQIAAPYFFGRVIQASMEEGMSHLNKTIVLLsLIYLAGALAA-LVRSWLftlaGQRLVARIRKQLFA 304
Cdd:PRK10522 15 FISVMALsLASAALGIGLIAFINQRLIETADTSLLVLPEFLGLL-LLLMAVTLGSqLALTTL----GHHFVYRLRSEFIK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 305 SVVEQEVAFFDSNRTGELINRLSSDTQVIQNALtVNVSMLLRYIIQIIGSLAFMFSLSAKL---TGVLISVVPIVG---- 377
Cdd:PRK10522 90 RILDTHVERIEQLGSASLLASLTSDVRNITIAF-VRLPELVQGIILTLGSAAYLAWLSPKMllvTAIWMAVTIWGGfvlv 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 378 ------IGAQR---------YGSFVQGlRKrfqdELAaasstaeeaIANIRTVRSFSQErksmnsYDTDIdKSYKSGAKL 442
Cdd:PRK10522 169 arvykhMATLRetedklyndYQTVLEG-RK----ELT---------LNRERAEYVFENE------YEPDA-QEYRHHIIR 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 443 A-LASGFFNGVIGIIGQGAVVLVLWyggsLVNKHEL-DVGILTAFMLYTLnvamafaFLSSvygDFMQAVGA-------- 512
Cdd:PRK10522 228 AdTFHLSAVNWSNIMMLGAIGLVFY----MANSLGWaDTNVAATYSLTLL-------FLRT---PLLSAVGAlptllsaq 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 513 ----SVRMFELMDRIPsiDLEGGKKLSTVnQVIQFQDVYFAYPSRPDSdvLKGMSFELKPGETVALVGPSGGGKSTVISL 588
Cdd:PRK10522 294 vafnKLNKLALAPYKA--EFPRPQAFPDW-QTLELRNVTFAYQDNGFS--VGPINLTIKRGELLFLIGGNGSGKSTLAML 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 589 LERFYDPKSGVISIGRTNLAELDLFWLRRKIALVSQEPVLFATTIAANiayGCEATQEEIEKAAEQANAHNFIaSFEEGY 668
Cdd:PRK10522 369 LTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLLGPE---GKPANPALVEKWLERLKMAHKL-ELEDGR 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 669 QTQvgergVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAeseHFVKE------AIDRAMvNRTVLVIAHRLSTVRN 742
Cdd:PRK10522 445 ISN-----LKLSKGQKKRLALLLALAEERDILLLDEWAADQDP---HFRREfyqvllPLLQEM-GKTIFAISHDDHYFIH 515
|
570 580
....*....|....*....|...
gi 1005434824 743 ADQVLVIDKGHIVERGTHETLLA 765
Cdd:PRK10522 516 ADRLLEMRNGQLSELTGEERDAA 538
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
540-752 |
1.62e-12 |
|
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: 66.88 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYPSRPDS-DVLKGMSFELKPGETVALVGPSGGGKSTVISLL-ERfydPKSGVISigrtnlAELDLFWLRR 617
Cdd:cd03232 3 VLTWKNLNYTVPVKGGKrQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGR---KTAGVIT------GEILINGRPL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 618 KIalvsqepvlfatTIAANIAYgceatqeeiekaAEQANAHNFIASFEEGYQTQVGERGvkLSGGQKQRVAIARALLMNP 697
Cdd:cd03232 74 DK------------NFQRSTGY------------VEQQDVHSPNLTVREALRFSALLRG--LSVEQRKRLTIGVELAAKP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 698 DVLLLDEATSALDAESEHFVKEAIDR-AMVNRTVLVIAHRLSTV--RNADQVLVIDKG 752
Cdd:cd03232 128 SILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSASifEKFDRLLLLKRG 185
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
559-784 |
2.46e-12 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 67.99 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 559 LKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGR--TNLAeldlfwLRRK-IALVSQE-------PVL 628
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGqpTRQA------LQKNlVAYVPQSeevdwsfPVL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 629 FATTIAANiAYGcEATQEEIEKAAEQANAHNFIASFE--EGYQTQVGErgvkLSGGQKQRVAIARALLMNPDVLLLDEAT 706
Cdd:PRK15056 97 VEDVVMMG-RYG-HMGWLRRAKKRDRQIVTAALARVDmvEFRHRQIGE----LSGGQKKRVFLARAIAQQGQVILLDEPF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 707 SALDAESE----HFVKEAIDRAmvnRTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHETLLAKAGVYKKL--VLRQLSV 780
Cdd:PRK15056 171 TGVDVKTEariiSLLRELRDEG---KTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAENLELAFsgVLRHVAL 247
|
....
gi 1005434824 781 SQHE 784
Cdd:PRK15056 248 NGSE 251
|
|
| ABC_6TM_ABCC_D2 |
cd18580 |
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ... |
226-520 |
2.46e-12 |
|
Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 2 (TMD2) of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. All ABC transporters share a common architecture of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350024 [Multi-domain] Cd Length: 294 Bit Score: 68.30 E-value: 2.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 226 LFIASVALLASSGSQIAAPYFFGRVIQASMEEGMSHLNKTIVLLSLIYLAGALA-ALVRSWLFTLAGQRLVARIRKQLFA 304
Cdd:cd18580 1 VLLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLlVLLRWLLFVLAGLRASRRLHDKLLR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 305 SVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSaklTGVLISVVPIVGIGA--QR 382
Cdd:cd18580 81 SVLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVS---PYFLIVLPPLLVVYYllQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 383 YgsFVQGLR--KR------------FQDelaaasstaeeAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGF 448
Cdd:cd18580 158 Y--YLRTSRqlRRlesesrsplyshFSE-----------TLSGLSTIRAFGWQERFIEENLRLLDASQRAFYLLLAVQRW 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1005434824 449 FNGVIGIIGQGAVVLVLwyGGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGASVRMFELM 520
Cdd:cd18580 225 LGLRLDLLGALLALVVA--LLAVLLRSSISAGLVGLALTYALSLTGSLQWLVRQWTELETSMVSVERILEYT 294
|
|
| ABC_6TM_Sav1866_like |
cd18554 |
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ... |
245-523 |
2.89e-12 |
|
Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar proteins; This group represents the homodimeric bacterial ABC multidrug exporter Sav1866, which is homologous to the lipid flippase MsbA, and both of which are functionally related to the human P-glycoprotein multidrug transporter (ABCB1 or MDR1). This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.
Pssm-ID: 349998 [Multi-domain] Cd Length: 299 Bit Score: 68.21 E-value: 2.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 245 YFFGRVIQA---SMEEGMSHLNKTIVLLSLIYLAGALAA-LVRSWLFTLAGQRLVARIRKQLFASVVEQEVAFFDSNRTG 320
Cdd:cd18554 24 YIVDDVIQGsslTLDEKVYKLFTIIGIMFFIFLILRPPVeYYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYANNRSG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 321 ELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAQRYGSFVQGLRKRFQDELAA 400
Cdd:cd18554 104 EIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQALAE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 401 ASSTAEEAIANIRTVRSFSQERKSMNSYDTD----IDKSYKSGAKLALASGFFNGVIGIigqgAVVLVLWYGGSLVNKHE 476
Cdd:cd18554 184 VQGFLHERIQGMSVIKSFALEKHEQKQFDKRnghfLTRALKHTRWNAKTFSAVNTITDL----APLLVIGFAAYLVIEGN 259
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1005434824 477 LDVGILTAFmlytlnvamaFAFLSSVYGDFMQAVGASVRM---FELMDRI 523
Cdd:cd18554 260 LTVGTLVAF----------VGYMERMYSPLRRLVNSFTTLtqsFASMDRV 299
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
563-764 |
3.29e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.27 E-value: 3.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 563 SFELKPGETVALVGPSGGGKSTVIS----LLerfydPKSGVISIGRTNLAELDLFWL-RRKIALVSQEPVLFATTI---- 633
Cdd:PRK03695 16 SAEVRAGEILHLVGPNGAGKSTLLArmagLL-----PGSGSIQFAGQPLEAWSAAELaRHRAYLSQQQTPPFAMPVfqyl 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 634 AANIAYGC--EATQEEIEKAAEQANAHNFIasfeegyqtqvgERGV-KLSGGQKQRVAIARALL-----MNPD--VLLLD 703
Cdd:PRK03695 91 TLHQPDKTrtEAVASALNEVAEALGLDDKL------------GRSVnQLSGGEWQRVRLAAVVLqvwpdINPAgqLLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 704 EATSALDAESEhfvkEAIDR-----AMVNRTVLVIAHRLS-TVRNADQVLVIDKGHIVERGTHETLL 764
Cdd:PRK03695 159 EPMNSLDVAQQ----AALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
553-789 |
3.33e-12 |
|
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: 70.81 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 553 RPDSDVLKGMSFElkpGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLaELDLFWLRRKIALVSQEPVLFA-T 631
Cdd:TIGR01257 943 RPAVDRLNITFYE---NQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHhL 1018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 632 TIAANIAY-------GCEATQEEIEKAAEQANAHNfiasfeegyqtQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDE 704
Cdd:TIGR01257 1019 TVAEHILFyaqlkgrSWEEAQLEMEAMLEDTGLHH-----------KRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDE 1087
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 705 ATSALDAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTheTLLAK----AGVYKKLVLRQLS 779
Cdd:TIGR01257 1088 PTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT--PLFLKncfgTGFYLTLVRKMKN 1165
|
250
....*....|
gi 1005434824 780 VSQHENLSAG 789
Cdd:TIGR01257 1166 IQSQRGGCEG 1175
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
535-763 |
4.23e-12 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 67.48 E-value: 4.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 535 STVNQVIQFQDVYFaypSRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELD--- 611
Cdd:PRK11831 2 QSVANLVDMRGVSF---TRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 612 LFWLRRKIALVSQEPVLFA-TTIAANIAYGC-EATQ--EEIEKAAeqanahnFIASFEegyqtQVGERGV------KLSG 681
Cdd:PRK11831 79 LYTVRKRMSMLFQSGALFTdMNVFDNVAYPLrEHTQlpAPLLHST-------VMMKLE-----AVGLRGAaklmpsELSG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 682 GQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDR--AMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERG 758
Cdd:PRK11831 147 GMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISElnSALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHG 226
|
....*
gi 1005434824 759 THETL 763
Cdd:PRK11831 227 SAQAL 231
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
559-757 |
6.81e-12 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 68.80 E-value: 6.81e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 559 LKGMSFELKPGETVALVGPSGGGKSTVISLLerfydpkSGVISIGRTnlaELDLFWL-------------RRKIALVSQE 625
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVL-------SGVYPHGTY---EGEIIFEgeelqasnirdteRAGIAIIHQE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 626 PVLFAT-TIAANIAYGCEATQE-EIEKAAEQANAHNFIAsfEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLD 703
Cdd:PRK13549 91 LALVKElSVLENIFLGNEITPGgIMDYDAMYLRAQKLLA--QLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 704 EATSALdAESEHFVKEAIDRAMVNRTV--LVIAHRLSTVRN-ADQVLVIDKG-HIVER 757
Cdd:PRK13549 169 EPTASL-TESETAVLLDIIRDLKAHGIacIYISHKLNEVKAiSDTICVIRDGrHIGTR 225
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
559-758 |
7.89e-12 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 68.66 E-value: 7.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 559 LKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELD-LFWLRRKIALVSQE-PVLFATTIAAN 636
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhKLAAQLGIGIIYQElSVIDELTVLEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 637 IAYGCEATQE-------EIEKAAEQANAHNFIASFEEGYQTQVGErgvkLSGGQKQRVAIARALLMNPDVLLLDEATSAL 709
Cdd:PRK09700 101 LYIGRHLTKKvcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVAN----LSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1005434824 710 -DAESEHFVkeAIDRAMVN--RTVLVIAHRLSTVRN-ADQVLVIDKGHIVERG 758
Cdd:PRK09700 177 tNKEVDYLF--LIMNQLRKegTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
561-775 |
1.03e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 64.83 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 561 GMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAEL------DLFWLRR----KIALVSQEPVLFA 630
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrdeyhqDLLYLGHqpgiKTELTALENLRFY 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 631 TTIAAniaygcEATQEEIEKAAEQANahnfIASFEE---GYqtqvgergvkLSGGQKQRVAIARALLMNPDVLLLDEATS 707
Cdd:PRK13538 99 QRLHG------PGDDEALWEALAQVG----LAGFEDvpvRQ----------LSAGQQRRVALARLWLTRAPLWILDEPFT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 708 ALDAESehfvkeaidramvnrtVLVIAHRLStvRNADQvlvidkGHIVERGTHETLLAKAGVYKKLVL 775
Cdd:PRK13538 159 AIDKQG----------------VARLEALLA--QHAEQ------GGMVILTTHQDLPVASDKVRKLRL 202
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
559-763 |
1.08e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.01 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 559 LKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGR-----TNLAELdlfwLRRKIALVSQE----PVLf 629
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqemrfASTTAA----LAAGVAIIYQElhlvPEM- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 630 atTIAANIAYG--------------CEATQEEIEKAAEQANAhnfiasfeegyQTQVGErgvkLSGGQKQRVAIARALLM 695
Cdd:PRK11288 95 --TVAENLYLGqlphkggivnrrllNYEAREQLEHLGVDIDP-----------DTPLKY----LSIGQRQMVEIAKALAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1005434824 696 NPDVLLLDEATSALDA-ESEHFVKeAID--RAMvNRTVLVIAHRLSTV-RNADQVLVIDKGHIVErgTHETL 763
Cdd:PRK11288 158 NARVIAFDEPTSSLSArEIEQLFR-VIRelRAE-GRVILYVSHRMEEIfALCDAITVFKDGRYVA--TFDDM 225
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
557-767 |
1.56e-11 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 67.35 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 557 DVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISI-GRtnlaELDLF----WLRRKIALVS----QEPV 627
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLdGK----PVRIRsprdAIRAGIAYVPedrkGEGL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 628 LFATTIAANIAYgceATQEE------IEKAAEQANAHNFIASFE---EGYQTQVGErgvkLSGGQKQRVAIARALLMNPD 698
Cdd:COG1129 342 VLDLSIRENITL---ASLDRlsrgglLDRRRERALAEEYIKRLRiktPSPEQPVGN----LSGGNQQKVVLAKWLATDPK 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 699 VLLLDEATSALD--AESE--HFVKEAIDRAMvnrTVLVIahrlST-----VRNADQVLVIDKGHIV-----ERGTHETLL 764
Cdd:COG1129 415 VLILDEPTRGIDvgAKAEiyRLIRELAAEGK---AVIVI----SSelpelLGLSDRILVMREGRIVgeldrEEATEEAIM 487
|
...
gi 1005434824 765 AKA 767
Cdd:COG1129 488 AAA 490
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
558-769 |
1.77e-11 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 64.90 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAEldlfW-----LRRKIALVSQEPVLFA-T 631
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITD----WqtakiMREAVAIVPEGRRVFSrM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 632 TIAANIAYGC-----EATQEEIEKAAEQanahnFIASFEEGYQtqvgeRGVKLSGGQKQRVAIARALLMNPDVLLLDEAT 706
Cdd:PRK11614 96 TVEENLAMGGffaerDQFQERIKWVYEL-----FPRLHERRIQ-----RAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005434824 707 SALDAESEHFVKEAID--RAMVNRTVLVIAHRLSTVRNADQVLVIDKGHIVERGTHETLLAKAGV 769
Cdd:PRK11614 166 LGLAPIIIQQIFDTIEqlREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAV 230
|
|
| ABC_6TM_PrtD_LapB_HlyB_like |
cd18783 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ... |
227-516 |
2.51e-11 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.
Pssm-ID: 350056 [Multi-domain] Cd Length: 294 Bit Score: 65.23 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 227 FIASVALlasSGSQIAAPYFFGRVIQASM-EEGMSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQLFAS 305
Cdd:cd18783 8 AIASLIL---HVLALAPPIFFQIVIDKVLvHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 306 VVEQEVAFFDSNRTGELINRLSSdTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIGAqryGS 385
Cdd:cd18783 85 LLSLPIDFFERTPAGVLTKHMQQ-IERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALII---LA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 386 FVQGLRKRFQ---DELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQGAVV 462
Cdd:cd18783 161 FLPPFRRRLQalyRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMTV 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1005434824 463 LVLWYGGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFmQAVGASVRM 516
Cdd:cd18783 241 GVIWVGAYLVFAGSLTVGALIAFNMLAGRVAGPLVQLAGLVQEY-QEARLSVRM 293
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
486-750 |
2.56e-11 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 67.08 E-value: 2.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 486 MLYTLnvAMAFAFLSSVYGDFMQAVGASVRMFELMD-------------RIPSID-----------LEGGKKLSTVNQVI 541
Cdd:TIGR00954 375 LLLKA--ADALGRLMLAGRDMTRLAGFTARVDTLLQvlddvksgnfkrpRVEEIEsgreggrnsnlVPGRGIVEYQDNGI 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 542 QFQDVYFAYPSrpdSDVL-KGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNlaeldlfwlrrKIA 620
Cdd:TIGR00954 453 KFENIPLVTPN---GDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKG-----------KLF 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 621 LVSQEPVLFATTIAANIAY--GCEATQE------EIEKAAEQANAHNFIAsfEEGYQTQVGERGVKLSGGQKQRVAIARA 692
Cdd:TIGR00954 519 YVPQRPYMTLGTLRDQIIYpdSSEDMKRrglsdkDLEQILDNVQLTHILE--REGGWSAVQDWMDVLSGGEKQRIAMARL 596
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 693 LLMNPDVLLLDEATSALDAESEHFVKEAIDRamVNRTVLVIAHRLSTVRNADQVLVID 750
Cdd:TIGR00954 597 FYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHRKSLWKYHEYLLYMD 652
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
558-752 |
2.60e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.21 E-value: 2.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKS--GVISIGRTNLAELDLfwlrRKIALVSQEPVLFATTIAA 635
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQIL----KRTGFVTQDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 636 NIAYGC-------EATQEEIEKAAEQANAHNFIASFEegyQTQVGE---RGVklSGGQKQRVAIARALLMNPDVLLLDEA 705
Cdd:PLN03211 159 ETLVFCsllrlpkSLTKQEKILVAESVISELGLTKCE---NTIIGNsfiRGI--SGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1005434824 706 TSALDAESEH-FVKEAIDRAMVNRTVLVIAHRLST--VRNADQVLVIDKG 752
Cdd:PLN03211 234 TSGLDATAAYrLVLTLGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEG 283
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
565-750 |
3.13e-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: 64.35 E-value: 3.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 565 ELKPGETVALVGPSGGGKSTVISLLERFYDPKSGvisigrtnlaelDLFWLRRKIALVSQE-PVLFATTIAA------NI 637
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG------------DIEIELDTVSYKPQYiKADYEGTVRDllssitKD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 638 AYGCEATQEEIEKAAEqanahnfiasFEEGYQTQVGErgvkLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFV 717
Cdd:cd03237 89 FYTHPYFKTEIAKPLQ----------IEQILDREVPE----LSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA 154
|
170 180 190
....*....|....*....|....*....|....*.
gi 1005434824 718 KEAIDRAMVN--RTVLVIAHRLSTVRN-ADQVLVID 750
Cdd:cd03237 155 SKVIRRFAENneKTAFVVEHDIIMIDYlADRLIVFE 190
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
558-759 |
3.25e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.85 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLE-RFYDPK-------SGVISIGRTNLAELDLFWLRRKIALVSQ--EPV 627
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQaaQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 628 lFATTIAANIAYGCeatQEEIEKAAEQANAHNFIASFE---EGYQTQVGERGVKLSGGQKQRVAIARAL---------LM 695
Cdd:PRK13547 96 -FAFSAREIVLLGR---YPHARRAGALTHRDGEIAWQAlalAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 696 NPDVLLLDEATSALDAESEHFVKEAIdRAMV---NRTVLVIAHRLS-TVRNADQVLVIDKGHIVERGT 759
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTV-RRLArdwNLGVLAIVHDPNlAARHADRIAMLADGAIVAHGA 238
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
565-735 |
5.40e-11 |
|
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: 65.96 E-value: 5.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 565 ELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVIsigrtnlaELDLfwlrrKIALVSQEpvlfattIAANIaygcEAT 644
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV--------DEDL-----KISYKPQY-------ISPDY----DGT 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 645 QEEIekaAEQANAHNFIASFeegYQTQVG---------ERGVK-LSGGQKQRVAIARALLMNPDVLLLDEATSALDAESE 714
Cdd:COG1245 418 VEEF---LRSANTDDFGSSY---YKTEIIkplglekllDKNVKdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQR 491
|
170 180
....*....|....*....|...
gi 1005434824 715 HFVKEAIDRAMVNR--TVLVIAH 735
Cdd:COG1245 492 LAVAKAIRRFAENRgkTAMVVDH 514
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
568-751 |
1.35e-10 |
|
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: 60.08 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 568 PGETVALVGPSGGGKSTVISLLERFYDPKS-GVISIGRTNLAELDLFWLRrkialvsqepvlfattiaaniaygceatqe 646
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGgGVIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 647 eiekaaeqanahnfiasfeegyQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAM- 725
Cdd:smart00382 51 ----------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLl 108
|
170 180 190
....*....|....*....|....*....|..
gi 1005434824 726 ------VNRTVLVIAHRLSTVRNADQVLVIDK 751
Cdd:smart00382 109 lllkseKNLTVILTTNDEKDLGPALLRRRFDR 140
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
538-712 |
1.56e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.37 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 538 NQVIQFQDVYFAYPSRpdsdVL-KGMSFELKPGETVALVGPSGGGKSTV---ISLLERfydPKSGVISIGRTnlaeldlf 613
Cdd:PRK11819 322 DKVIEAENLSKSFGDR----LLiDDLSFSLPPGGIVGIIGPNGAGKSTLfkmITGQEQ---PDSGTIKIGET-------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 614 wlrRKIALVSQ-----EPvlfATTIAANIAYGceatQEEIEKAAEQANAHNFIASFeeGY-----QTQVGErgvkLSGGQ 683
Cdd:PRK11819 387 ---VKLAYVDQsrdalDP---NKTVWEEISGG----LDIIKVGNREIPSRAYVGRF--NFkggdqQKKVGV----LSGGE 450
|
170 180
....*....|....*....|....*....
gi 1005434824 684 KQRVAIARALLMNPDVLLLDEATSALDAE 712
Cdd:PRK11819 451 RNRLHLAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| ABC_6TM_T1SS_like |
cd18555 |
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ... |
226-502 |
1.66e-10 |
|
Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 62.91 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 226 LFIASVAL-LASSGSQIAAPYFFGRVI-QASMEEGMSHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQLF 303
Cdd:cd18555 3 LLISILLLsLLLQLLTLLIPILTQYVIdNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSDFF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 304 ASVVEQEVAFFDSNRTGELINRLSSDTQvIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLTG-VLISVVPIVGIGAqr 382
Cdd:cd18555 83 EHLLKLPYSFFENRSSGDLLFRANSNVY-IRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLiVLLLGLLIVLLLL-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 383 YGSFVqgLRKRFQDELAAASSTAEE---AIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQG 459
Cdd:cd18555 160 LTRKK--IKKLNQEEIVAQTKVQSYlteTLYGIETIKSLGSEKNIYKKWENLFKKQLKAFKKKERLSNILNSISSSIQFI 237
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1005434824 460 AVVLVLWYGGSLVNKHELDVGILTAFmlytlnVAMAFAFLSSV 502
Cdd:cd18555 238 APLLILWIGAYLVINGELTLGELIAF------SSLAGSFLTPI 274
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
558-758 |
1.97e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 62.31 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLFWLRRKIALVSQEpvlfATT----- 632
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN----ATTpgdit 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 633 ---IAANIAYGCEATQEEIEKAAEQANAHNFIASfeeGYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSAL 709
Cdd:PRK10253 98 vqeLVARGRYPHQPLFTRWRKEDEEAVTKAMQAT---GITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1005434824 710 DAESEHFVKEAIDRamVNR----TVLVIAHRLS-TVRNADQVLVIDKGHIVERG 758
Cdd:PRK10253 175 DISHQIDLLELLSE--LNRekgyTLAAVLHDLNqACRYASHLIALREGKIVAQG 226
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
565-735 |
2.83e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.67 E-value: 2.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 565 ELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISigrtnlAELdlfwlrrKIALVSQEpvlfattIAANIaygcEAT 644
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD------PEL-------KISYKPQY-------IKPDY----DGT 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 645 QEE-IEKAAEqanahNFIASFeegYQTQVG---------ERGVK-LSGGQKQRVAIARALLMNPDVLLLDEATSALDAES 713
Cdd:PRK13409 417 VEDlLRSITD-----DLGSSY---YKSEIIkplqlerllDKNVKdLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQ 488
|
170 180
....*....|....*....|....
gi 1005434824 714 EHFVKEAIDRAMVNR--TVLVIAH 735
Cdd:PRK13409 489 RLAVAKAIRRIAEEReaTALVVDH 512
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
557-755 |
4.96e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 62.74 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 557 DVLKGMSFELKPGETVALVGPSGGGKSTVISLL--ERfyDPKSGVISIGRTNLAELDLFWLRRK-IALVSQEPVLFAT-- 631
Cdd:COG3845 272 PALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPRERRRLgVAYIPEDRLGRGLvp 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 632 --TIAANIAYGcEATQEE------IEKAAEQANAHNFIASFE---EGYQTQVGergvKLSGGQKQRVAIARALLMNPDVL 700
Cdd:COG3845 350 dmSVAENLILG-RYRRPPfsrggfLDRKAIRAFAEELIEEFDvrtPGPDTPAR----SLSGGNQQKVILARELSRDPKLL 424
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 701 LLDEATSALDAESEHFVKEAIdRAMVNR--TVLVIAHRLSTVRN-ADQVLVIDKGHIV 755
Cdd:COG3845 425 IAAQPTRGLDVGAIEFIHQRL-LELRDAgaAVLLISEDLDEILAlSDRIAVMYEGRIV 481
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
559-754 |
7.76e-10 |
|
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: 62.15 E-value: 7.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 559 LKGMSFELKPGETVALVGPSGGGKSTVISLLERFYdPK---SGVISIGRTNLAELDLFWLRRK-IALVSQEPVLFAT-TI 633
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTERAgIVIIHQELTLVPElSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 634 AANIAYGCEATQE--EIEKAAEQANAHNFIASFE---EGYQTQVGERGvklsGGQKQRVAIARALLMNPDVLLLDEATSA 708
Cdd:TIGR02633 96 AENIFLGNEITLPggRMAYNAMYLRAKNLLRELQldaDNVTRPVGDYG----GGQQQLVEIAKALNKQARLLILDEPSSS 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1005434824 709 L-DAESEHFVKEAIDRAMVNRTVLVIAHRLSTVRN-ADQVLVIDKG-HI 754
Cdd:TIGR02633 172 LtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGqHV 220
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
524-769 |
1.48e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 61.45 E-value: 1.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 524 PSIDLEGGKKLStvNQVIQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISig 603
Cdd:PRK15064 305 PFIRFEQDKKLH--RNALEVENLTKGFDNGP---LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK-- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 604 rtnlaeldlfWlrrkialvsqepvlfatTIAANIAYgceatqeeiekaAEQANAHNF---IASFEEGYQ-TQVGE----- 674
Cdd:PRK15064 378 ----------W-----------------SENANIGY------------YAQDHAYDFendLTLFDWMSQwRQEGDdeqav 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 675 RG---------------VK-LSGGQKQRVAIARALLMNPDVLLLDEATSALDAESehfvKEAIDRAMVNR--TVLVIAHR 736
Cdd:PRK15064 419 RGtlgrllfsqddikksVKvLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMES----IESLNMALEKYegTLIFVSHD 494
|
250 260 270
....*....|....*....|....*....|....*
gi 1005434824 737 LSTVRN-ADQVLVIDKGHIVE-RGTHETLLAKAGV 769
Cdd:PRK15064 495 REFVSSlATRIIEITPDGVVDfSGTYEEYLRSQGI 529
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
552-760 |
1.74e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.03 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 552 SRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLL--ERFYDPKSGVISIGRTNLAELD-----------LFWLRRK 618
Cdd:PRK09580 10 SVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSpedragegifmAFQYPVE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 619 IALVSQEpVLFATTIAANIAYgceATQEEIEKAAEQANAHNFIASFEEGYQTQVGERGVKLSGGQKQRVAIARALLMNPD 698
Cdd:PRK09580 90 IPGVSNQ-FFLQTALNAVRSY---RGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVGFSGGEKKRNDILQMAVLEPE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005434824 699 VLLLDEATSALDAESEHFVKEAIDRAM-VNRTVLVIAH--RLSTVRNADQVLVIDKGHIVERGTH 760
Cdd:PRK09580 166 LCILDESDSGLDIDALKIVADGVNSLRdGKRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF 230
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
555-766 |
1.74e-09 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.27 E-value: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 555 DSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERF--YDPKSGVISIGRTNLAELD-----------LFWLRRKIAL 621
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEpeerahlgiflAFQYPIEIPG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 622 VSQEPVLFATTIAANIAYGCEATQ--EEIEKAAEQANAHNFIASF-----EEGYqtqvgergvklSGGQKQRVAIARALL 694
Cdd:CHL00131 99 VSNADFLRLAYNSKRKFQGLPELDplEFLEIINEKLKLVGMDPSFlsrnvNEGF-----------SGGEKKRNEILQMAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1005434824 695 MNPDVLLLDEATSALDAESEHFVKEAIDRAM-VNRTVLVIAH--RLSTVRNADQVLVIDKGHIVERGTHEtlLAK 766
Cdd:CHL00131 168 LDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAE--LAK 240
|
|
| ABC_6TM_ATM1_ABCB7_HMT1_ABCB6 |
cd18560 |
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ... |
229-510 |
2.05e-09 |
|
Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group represents the Atm1/ABCB7/HMT1/ABCB6 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Yeast ATM1 and human ABCB7 (ABC transporter subfamily B, member 7), which are involved in the assembly of cytosolic iron-sulfur (Fe/S) cluster-containing proteins by mediating export of Fe/S cluster precursors from mitochondria. In eukaryotes, the Atm1/ABCB7 is present in the inner membrane of mitochondria and is required for the formation of cytosolic iron sulfur cluster containing proteins; mutations of ABCB7 gene result in mitochondrial iron accumulation and are responsible for X-linked sideroblastic anemia. ABCB6 is originally identified as a porphyrin transporter present in the outer membrane of mitochondria. It is highly expressed in cells resistance to arsenic and protects against arsenic cytotoxicity. Moreover, Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster.
Pssm-ID: 350004 [Multi-domain] Cd Length: 292 Bit Score: 59.55 E-value: 2.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 229 ASVALLASSGSQIAAPYFFGRVIQASMEEGMSHLNKTIVLLSLIYLAGALAAL---VRSWLFTLAGQRLVARIRKQLFAS 305
Cdd:cd18560 1 SLLLLILGKACNVLAPLFLGRAVNALTLAKVKDLESAVTLILLYALLRFSSKLlkeLRSLLYRRVQQNAYRELSLKTFAH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 306 VVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIG-SLAFMFSLSAkltgvLISVVPIVGIGAqrYG 384
Cdd:cd18560 81 LHSLSLDWHLSKKTGEVVRIMDRGTESANTLLSYLVFYLVPTLLELIVvSVVFAFHFGA-----WLALIVFLSVLL--YG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 385 SF---VQGLRKRFQdELAAASSTAEEAIA-----NIRTVRSFSQERKSMNSYDTDIDKsYKSGAKLALAS-GFFNGVIGI 455
Cdd:cd18560 154 VFtikVTEWRTKFR-RAANKKDNEAHDIAvdsllNFETVKYFTNEKYEVDRYGEAVKE-YQKSSVKVQASlSLLNVGQQL 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1005434824 456 IGQGAVVLVLWYGGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAV 510
Cdd:cd18560 232 IIQLGLTLGLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQPLNFLGTIYRMIIQSL 286
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
549-755 |
2.15e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 549 AYPSRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLerfydpkSGVISI--GRTNLAElDLfwlrrKIALVSQEP 626
Cdd:PRK11147 9 AWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLddGRIIYEQ-DL-----IVARLQQDP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 627 VLFAT-TIAANIAYGCEATQE----------------------EIEKAAEQANAHNfIASFEEGYQTQVGERGV------ 677
Cdd:PRK11147 76 PRNVEgTVYDFVAEGIEEQAEylkryhdishlvetdpseknlnELAKLQEQLDHHN-LWQLENRINEVLAQLGLdpdaal 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 678 -KLSGGQKQRVAIARALLMNPDVLLLDEATSALDAES----EHFVKEaidramVNRTVLVIAHRLSTVRN-ADQVLVIDK 751
Cdd:PRK11147 155 sSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETiewlEGFLKT------FQGSIIFISHDRSFIRNmATRIVDLDR 228
|
....
gi 1005434824 752 GHIV 755
Cdd:PRK11147 229 GKLV 232
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
540-710 |
2.71e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 60.64 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 540 VIQFQDVYFAYPSRPDsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGviSIGRTNLAELDLFWLRRKI 619
Cdd:PLN03073 508 IISFSDASFGYPGGPL--LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSG--TVFRSAKVRMAVFSQHHVD 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 620 AL-VSQEPVLFAttiaaniaygceatqeeiekaaeqanAHNFIASFEEGYQTQVGERGVK----------LSGGQKQRVA 688
Cdd:PLN03073 584 GLdLSSNPLLYM--------------------------MRCFPGVPEQKLRAHLGSFGVTgnlalqpmytLSGGQKSRVA 637
|
170 180
....*....|....*....|..
gi 1005434824 689 IARALLMNPDVLLLDEATSALD 710
Cdd:PLN03073 638 FAKITFKKPHILLLDEPSNHLD 659
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
557-758 |
4.02e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.51 E-value: 4.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 557 DVLKGMSFELKPGETVALVGPSGGGKST----VISLLERFYDPKSGVISIGRTNLAELDLFwLRRKIALVSQEPVLFAT- 631
Cdd:TIGR00956 75 DILKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPEEIKKH-YRGDVVYNAETDVHFPHl 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 632 TIAANI--AYGCEATQEEIEKAAEQANA----HNFIASF--EEGYQTQVGE---RGVklSGGQKQRVAIARALLMNPDVL 700
Cdd:TIGR00956 154 TVGETLdfAARCKTPQNRPDGVSREEYAkhiaDVYMATYglSHTRNTKVGNdfvRGV--SGGERKRVSIAEASLGGAKIQ 231
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1005434824 701 LLDEATSALDAESE-HFVKEAIDRA-MVNRTVLVIAHRLStvRNA----DQVLVIDKGHIVERG 758
Cdd:TIGR00956 232 CWDNATRGLDSATAlEFIRALKTSAnILDTTPLVAIYQCS--QDAyelfDKVIVLYEGYQIYFG 293
|
|
| ABC_6TM_VMR1_D2_like |
cd18604 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
227-383 |
4.29e-09 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 2 (TMD2) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350048 [Multi-domain] Cd Length: 297 Bit Score: 58.63 E-value: 4.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 227 FIASVALLASSGSQIAAPYFFGRVIQASMEEGM-----SHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQ 301
Cdd:cd18604 2 ALLLLLFVLSQLLSVGQSWWLGIWASAYETSSAlppseVSVLYYLGIYALISLLSVLLGTLRYLLFFFGSLRASRKLHER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 302 LFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLtgvLISVVPIVGIG-- 379
Cdd:cd18604 82 LLHSVLRAPLRWLDTTPVGRILNRFSKDIETIDSELADSLSSLLESTLSLLVILIAIVVVSPAF---LLPAVVLAALYvy 158
|
....*
gi 1005434824 380 -AQRY 383
Cdd:cd18604 159 iGRLY 163
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
567-738 |
9.11e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 56.99 E-value: 9.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 567 KPGETVALVGPSGGGKSTVISLLE--------RFYDPKS--GVISIGRTNlaELDLFWLR---------RKIALVSQEPV 627
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAgklkpnlgKFDDPPDwdEILDEFRGS--ELQNYFTKllegdvkviVKPQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 628 LFATTIAANIaygceatqeeiEKAAEQANAHNFIASFEegyQTQVGERGV-KLSGGQKQRVAIARALLMNPDVLLLDEAT 706
Cdd:cd03236 102 AVKGKVGELL-----------KKKDERGKLDELVDQLE---LRHVLDRNIdQLSGGELQRVAIAAALARDADFYFFDEPS 167
|
170 180 190
....*....|....*....|....*....|....*....
gi 1005434824 707 SALDaesehfVKEAIDRAMV-------NRTVLVIAHRLS 738
Cdd:cd03236 168 SYLD------IKQRLNAARLirelaedDNYVLVVEHDLA 200
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
555-735 |
1.43e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 58.26 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 555 DSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRT----NLAELDLFWLRrkialVSQEPVLFA 630
Cdd:PRK10636 324 DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGiklgYFAQHQLEFLR-----ADESPLQHL 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 631 TTIAaniaygceatqeeiEKAAEQaNAHNFIASFeeGYQ-TQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSAL 709
Cdd:PRK10636 399 ARLA--------------PQELEQ-KLRDYLGGF--GFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHL 461
|
170 180
....*....|....*....|....*....
gi 1005434824 710 DAESEHFVKEAI---DRAMVnrtvlVIAH 735
Cdd:PRK10636 462 DLDMRQALTEALidfEGALV-----VVSH 485
|
|
| ABC_6TM_SUR1_D2_like |
cd18602 |
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group ... |
227-378 |
2.59e-08 |
|
Six-transmembrane helical domain 2 (TMD2) of the sulphonylurea receptors SUR1/2; This group represents the six-transmembrane domain 2 (TMD2) of the sulphonylurea receptors SUR1/2 (ABCC8), which function as a modulator of ATP-sensitive potassium channels and insulin release, and belong to the ABCC subfamily. The ATP-sensitive (K-ATP) channel is an octameric complex of four pore-forming Kir6.2 subunits and four regulatory SUR subunits. Thus, in contrast to other ABC transporters, the SUR serves as the regulatory subunit of an ion channel. Mutations and deficiencies in the SUR proteins have been observed in patients with hyperinsulinemic hypoglycemia of infancy, an autosomal recessive disorder of unregulated and high insulin secretion. Mutations have also been associated with non-insulin-dependent diabetes mellitus type 2, an autosomal dominant disease of defective insulin secretion.
Pssm-ID: 350046 [Multi-domain] Cd Length: 307 Bit Score: 56.46 E-value: 2.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 227 FIASVALLASSGSQIAAPYFFGRVIQASMEEGMSHLNKTIVLLS--------LIYLAGALAALVRSWLFTLAGQRLVARI 298
Cdd:cd18602 2 ALVLALALLKQGLRVATDFWLADWTEANHDVASVVFNITSSSLEddevsyyiSVYAGLSLGAVILSLVTNLAGELAGLRA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 299 RKQLFA----SVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFMFSLSAKLtgvLISVVP 374
Cdd:cd18602 82 ARRLHDrmlrNIVRAPMRFFDTTPIGRILNRFSSDTNVIDQKLPTTLERLLRFLLLCLSAIIVNAIVTPYF---LIALIP 158
|
....
gi 1005434824 375 IVGI 378
Cdd:cd18602 159 IIIV 162
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
648-767 |
3.18e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.94 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 648 IEKAAEQANAHNFIASFE---EGYQTQVGergvKLSGGQKQRVAIARALLMNPDVLLLDEATSALD--AESE------HF 716
Cdd:PRK10762 366 LKHADEQQAVSDFIRLFNiktPSMEQAIG----LLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDvgAKKEiyqlinQF 441
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1005434824 717 VKEAIDramvnrTVLVIAHRLSTVRNADQVLVIDKGHI-----VERGTHETLLAKA 767
Cdd:PRK10762 442 KAEGLS------IILVSSEMPEVLGMSDRILVMHEGRIsgeftREQATQEKLMAAA 491
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
559-756 |
3.29e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 56.72 E-value: 3.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 559 LKGMSFELKPGETVALVGPSGGGKSTVISLLerfydpkSGVISIG----------------RTNLAEldlfwlRRKIALV 622
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVL-------SGVYPHGsyegeilfdgevcrfkDIRDSE------ALGIVII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 623 SQE----PVLfatTIAANIAYGCEAT-------QEEIEKAAEqanahnFIA--SFEEGYQTQVGERGVklsgGQKQRVAI 689
Cdd:NF040905 84 HQElaliPYL---SIAENIFLGNERAkrgvidwNETNRRARE------LLAkvGLDESPDTLVTDIGV----GKQQLVEI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1005434824 690 ARALLMNPDVLLLDEATSAL-DAESEH-------FVKEAIdramvnrTVLVIAHRLSTVRN-ADQVLVIDKGHIVE 756
Cdd:NF040905 151 AKALSKDVKLLILDEPTAALnEEDSAAlldllleLKAQGI-------TSIIISHKLNEIRRvADSITVLRDGRTIE 219
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
563-739 |
3.64e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.10 E-value: 3.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 563 SFEL------KPGETVALVGPSGGGKSTVISLLerfydpkSGVIsigRTNLAELD--LFW---LRR-------------- 617
Cdd:COG1245 87 GFRLyglpvpKKGKVTGILGPNGIGKSTALKIL-------SGEL---KPNLGDYDeePSWdevLKRfrgtelqdyfkkla 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 618 --------KIALVSQEPVLFATTiaaniaygceaTQEEIEKAAEQANAHNFIASFEegyQTQVGERGVK-LSGGQKQRVA 688
Cdd:COG1245 157 ngeikvahKPQYVDLIPKVFKGT-----------VRELLEKVDERGKLDELAEKLG---LENILDRDISeLSGGELQRVA 222
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 689 IARALLMNPDVLLLDEATSALDaesehfVKEAIDRAMV-------NRTVLVIAHRLST 739
Cdd:COG1245 223 IAAALLRDADFYFFDEPSSYLD------IYQRLNVARLirelaeeGKYVLVVEHDLAI 274
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
552-712 |
4.39e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.47 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 552 SRPDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDlfwLRRKIALVSQEPVLFAT 631
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD---RSRFMAYLGHLPGLKAD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 632 TIA-ANIAYGCEATQEEIEKAAEQANAHNFIASFEEGYQTQvgergvkLSGGQKQRVAIARALLMNPDVLLLDEATSALD 710
Cdd:PRK13543 97 LSTlENLHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQ-------LSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
..
gi 1005434824 711 AE 712
Cdd:PRK13543 170 LE 171
|
|
| ABC_6TM_MRP5_8_9_D2 |
cd18599 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, ... |
223-395 |
6.49e-08 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 5, 8, and 9, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350043 [Multi-domain] Cd Length: 313 Bit Score: 55.26 E-value: 6.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 223 LCVLFIASVALLASSG-------SQIAAPYFFGRVIQASMEEGMSHlNKTIVLLSLIYLAGALA----ALVRSWLFTLAG 291
Cdd:cd18599 8 VLLLFILSVGSTVFSDwwlsywlKQGSGNTTNNVDNSTVDSGNISD-NPDLNFYQLVYGGSILVilllSLIRGFVFVKVT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 292 QRLVARIRKQLFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIGSLAFmfsLSAKLTGVLIS 371
Cdd:cd18599 87 LRASSRLHNKLFQKILRSPMSFFDTTPTGRILNRFSKDLDEVDVRLPFTLENFLQNVLLVVFSLII---IAIVFPWFLIA 163
|
170 180
....*....|....*....|....*.
gi 1005434824 372 VVPIVGIGAQRYGSFVQGLR--KRFQ 395
Cdd:cd18599 164 LIPLAIIFVFLSKIFRRAIRelKRLE 189
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
565-750 |
6.82e-08 |
|
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: 52.96 E-value: 6.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 565 ELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISigrtnlaeldlfWLRRKIALVSQEpvlfattiaaniaygceat 644
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDE------------WDGITPVYKPQY------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 645 qeeiekaaeqanahnfiasfeegyqtqvgergVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRA 724
Cdd:cd03222 70 --------------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRL 117
|
170 180
....*....|....*....|....*....
gi 1005434824 725 MVN--RTVLVIAHRLSTVRN-ADQVLVID 750
Cdd:cd03222 118 SEEgkKTALVVEHDLAVLDYlSDRIHVFE 146
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
554-730 |
1.64e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 554 PDSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGrTNL---------AELDLfwlrrkialvsq 624
Cdd:PRK11147 330 DGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG-TKLevayfdqhrAELDP------------ 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 625 epvlfATTIAANIAYGceatQEEIEKAAEQANAHNFIASFEegYQTQVGERGVK-LSGGQKQRVAIARALLMNPDVLLLD 703
Cdd:PRK11147 397 -----EKTVMDNLAEG----KQEVMVNGRPRHVLGYLQDFL--FHPKRAMTPVKaLSGGERNRLLLARLFLKPSNLLILD 465
|
170 180 190
....*....|....*....|....*....|....*....
gi 1005434824 704 EATSALDAESEHFVKEAI------------DRAMVNRTV 730
Cdd:PRK11147 466 EPTNDLDVETLELLEELLdsyqgtvllvshDRQFVDNTV 504
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
563-737 |
2.33e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.43 E-value: 2.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 563 SFEL------KPGETVALVGPSGGGKSTVISLLerfydpkSGVIsigRTNLAE----------LDLF-------WLRR-- 617
Cdd:PRK13409 87 GFKLyglpipKEGKVTGILGPNGIGKTTAVKIL-------SGEL---IPNLGDyeeepswdevLKRFrgtelqnYFKKly 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 618 --------KIALVSQEPVLFATTiaaniaygceaTQEEIEKAAEQANAHNFIASFEegyQTQVGERGVK-LSGGQKQRVA 688
Cdd:PRK13409 157 ngeikvvhKPQYVDLIPKVFKGK-----------VRELLKKVDERGKLDEVVERLG---LENILDRDISeLSGGELQRVA 222
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1005434824 689 IARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRTVLVIAHRL 737
Cdd:PRK13409 223 IAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDL 271
|
|
| ABC_6TM_YOR1_D2_like |
cd18606 |
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ... |
272-378 |
2.68e-07 |
|
Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Yor1p, an oligomycin resistance ABC transporter, and similar proteins. Members of this group belong to the MRP (multidrug resistance-associated protein) subfamily (ABCC). In addition to Yor1p, yeast ABCC (also termed MRP/CFTR) subfamily also comprises five other members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, and Vmr1p), which are not included in this group. Yor1p is a plasma membrane ATP-binding transporter that mediates export of many different organic anions including oligomycin. While Yor1p has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane.
Pssm-ID: 350050 [Multi-domain] Cd Length: 290 Bit Score: 52.86 E-value: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 272 IYLAGALAALVRSWLFTLAGQRLVARIRKQLFASVVEQ----EVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRY 347
Cdd:cd18606 40 IYAGLGVLQAIFLFLFGLLLAYLGIRASKRLHNKALKRvlraPMSFFDTTPLGRILNRFSKDTDVLDNELPDSLRMFLYT 119
|
90 100 110
....*....|....*....|....*....|.
gi 1005434824 348 IIQIIGSLAFMFSLsakLTGVLISVVPIVGI 378
Cdd:cd18606 120 LSSIIGTFILIIIY---LPWFAIALPPLLVL 147
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
558-752 |
3.22e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.34 E-value: 3.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLL-ERFydpKSGVISIGR--TNLAELDLFWLRRkIALVSQEPVLFAT-TI 633
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaERV---TTGVITGGDrlVNGRPLDSSFQRS-IGYVQQQDLHLPTsTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 634 AANIAYGCEATQ-EEIEKAAEQANAHNFIASFE-EGY-QTQVGERGVKLSGGQKQRVAIARALLMNPDVLL-LDEATSAL 709
Cdd:TIGR00956 854 RESLRFSAYLRQpKSVSKSEKMEYVEEVIKLLEmESYaDAVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGL 933
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1005434824 710 DAESEHFVKEAIdRAMVN--RTVLVIAHRLSTVRNA--DQVLVIDKG 752
Cdd:TIGR00956 934 DSQTAWSICKLM-RKLADhgQAILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
559-758 |
6.07e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 52.97 E-value: 6.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 559 LKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISI-GRTNLAELD--LFWLRRKIALVSQEPVLFATTIaa 635
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIkGSAALIAISsgLNGQLTGIENIELKGLMMGLTK-- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 636 niaygcEATQEEIEKAAEQANAHNFIASFEEGYqtqvgergvklSGGQKQRVAIARALLMNPDVLLLDEATSALDaesEH 715
Cdd:PRK13545 118 ------EKIKEIIPEIIEFADIGKFIYQPVKTY-----------SSGMKSRLGFAISVHINPDILVIDEALSVGD---QT 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1005434824 716 FVKEAIDR----AMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERG 758
Cdd:PRK13545 178 FTKKCLDKmnefKEQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYG 225
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
541-745 |
9.87e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 9.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 541 IQFQDVYFAYPSRPdsdVLKGMSFELKPGETVALVGPSGGGKSTVISLLerfydpkSGVISIGRTNlaELDLF------- 613
Cdd:PRK10938 261 IVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI-------TGDHPQGYSN--DLTLFgrrrgsg 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 614 ---W-LRRKIALVSQEPVL---FATTIAANIAYG-------CEATQEEIEKAAEQanahnFIASFeeGYQTQVGERGVK- 678
Cdd:PRK10938 329 etiWdIKKHIGYVSSSLHLdyrVSTSVRNVILSGffdsigiYQAVSDRQQKLAQQ-----WLDIL--GIDKRTADAPFHs 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 679 LSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVN-RTVLV------------IAHRLSTVRNADQ 745
Cdd:PRK10938 402 LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEgETQLLfvshhaedapacITHRLEFVPDGDI 481
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
562-754 |
1.09e-06 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 51.98 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 562 MSFELKPGETVALVGPSGGGKStviSLLERFY---DPKSGVISIGRTNLAELDLFwLRRKIALV-----SQEPVLFA-TT 632
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRT---ELAETLYglrPARGGRIMLNGKEINALSTA-QRLARGLVylpedRQSSGLYLdAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 633 IAANIaygCEATQEE----IEKAAEQANAhnfiasfeEGYQTQVG------ERGVK-LSGGQKQRVAIARALLMNPDVLL 701
Cdd:PRK15439 358 LAWNV---CALTHNRrgfwIKPARENAVL--------ERYRRALNikfnhaEQAARtLSGGNQQKVLIAKCLEASPQLLI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1005434824 702 LDEATSALDAESEHFVKEAIDR-AMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHI 754
Cdd:PRK15439 427 VDEPTRGVDVSARNDIYQLIRSiAAQNVAVLFISSDLEEIEQmADRVLVMHQGEI 481
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
673-768 |
1.33e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 51.27 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 673 GERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIdRAMV--NRTVLVIAHRLSTVRN-ADQVLVI 749
Cdd:NF000106 139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV-RSMVrdGATVLLTTQYMEEAEQlAHELTVI 217
|
90
....*....|....*....
gi 1005434824 750 DKGHIVERGTHETLLAKAG 768
Cdd:NF000106 218 DRGRVIADGKVDELKTKVG 236
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
555-787 |
1.67e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 555 DSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSG-----VISIGRTNLAEL----DLFWLRRKIALVSQE 625
Cdd:PRK10938 15 DTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGerqsqFSHITRLSFEQLqklvSDEWQRNNTDMLSPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 626 PVLFATTIAaniaygcEATQEEIEKAAE-QANAHNFiasfeeGYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDE 704
Cdd:PRK10938 95 EDDTGRTTA-------EIIQDEVKDPARcEQLAQQF------GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 705 ATSALDAESEHFVKEAIDR-AMVNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHETLLAKAgvykklVLRQLSVSq 782
Cdd:PRK10938 162 PFDGLDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQA------LVAQLAHS- 234
|
....*
gi 1005434824 783 hENLS 787
Cdd:PRK10938 235 -EQLE 238
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
563-767 |
2.19e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.08 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 563 SFELKPGETVALVGPSGGGKS-TVISLLERFYDPKSGVISI-GR----TNLAELdlfwLRRKIALVSQE-------PVLf 629
Cdd:PRK13549 282 SFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIdGKpvkiRNPQQA----IAQGIAMVPEDrkrdgivPVM- 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 630 atTIAANI---AYGCEATQEEIEKAAEQANAHNFIASFEegYQTQVGERGV-KLSGGQKQRVAIARALLMNPDVLLLDEA 705
Cdd:PRK13549 357 --GVGKNItlaALDRFTGGSRIDDAAELKTILESIQRLK--VKTASPELAIaRLSGGNQQKAVLAKCLLLNPKILILDEP 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 706 TSALD--AESE------HFVKEAIdramvnrTVLVIAHRLSTVRN-ADQVLVIDKGHIveRG-------THETLLAKA 767
Cdd:PRK13549 433 TRGIDvgAKYEiyklinQLVQQGV-------AIIVISSELPEVLGlSDRVLVMHEGKL--KGdlinhnlTQEQVMEAA 501
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
678-778 |
2.39e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 50.51 E-value: 2.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 678 KLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAID--RAMVNRTVLVIAHRLSTV-RNADQVLVIDKGHI 754
Cdd:PRK11022 153 QLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLelQQKENMALVLITHDLALVaEAAHKIIVMYAGQV 232
|
90 100
....*....|....*....|....*
gi 1005434824 755 VERGT-HETLLAKAGVYKKLVLRQL 778
Cdd:PRK11022 233 VETGKaHDIFRAPRHPYTQALLRAL 257
|
|
| ABC_6TM_AarD_CydDC_like |
cd18561 |
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ... |
231-513 |
2.42e-06 |
|
Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and similar proteins; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350005 [Multi-domain] Cd Length: 289 Bit Score: 49.97 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 231 VALLASSGSQIAAPYFFGRVIQASMeegmshLNKTIVLLSLIYLAGALAALVRSWLFTL-------AGQRLVARIRKQLF 303
Cdd:cd18561 3 LLGLLITALYIAQAWLLARALARIF------AGGPWEDIMPPLAGIAGVIVLRAALLWLrervahrAAQRVKQHLRRRLF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 304 ASVVEQEVAFFDSNRTGELINRLSSDTQVIQnaltvnvSMLLRYIIQIIGS----------LAFMFSLSAKLTGVLISVV 373
Cdd:cd18561 77 AKLLKLGPGYLEGERTGELQTTVVDGVEALE-------AYYGRYLPQLLVAllgplliliyLFFLDPLVALILLVFALLI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 374 PI----VGIGAQRYGSFVQGLRKRFQDELAAAsstaeeaIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFF 449
Cdd:cd18561 150 PLspalWDRLAKDTGRRHWAAYGRLSAQFLDS-------LQGMTTLKAFGASKRRGNELAARAEDLRQATMKVLAVSLLS 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1005434824 450 NGVIGIIGQGAVVLVLWYGGSLVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGAS 513
Cdd:cd18561 223 SGIMGLATALGTALALGVGALRVLGGQLTLSSLLLILFLSREFFRPLRDLGAYWHAGYQGISAA 286
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
542-755 |
3.11e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 50.68 E-value: 3.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 542 QFQDVYfAYPSRPDSDV------LKG------MSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSG-------VISI 602
Cdd:PRK11288 241 EIGDIY-GYRPRPLGEVrlrldgLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGqvyldgkPIDI 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 603 GRTNLAeldlfwLRRKIALV----SQEPVLFATTIAANIAYGCEATQEE----IEKAAEQANAHNFIASFEegYQTQVGE 674
Cdd:PRK11288 320 RSPRDA------IRAGIMLCpedrKAEGIIPVHSVADNINISARRHHLRagclINNRWEAENADRFIRSLN--IKTPSRE 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 675 RG-VKLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAI-DRAMVNRTVLVIAHRLSTVRN-ADQVLVIDK 751
Cdd:PRK11288 392 QLiMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIyELAAQGVAVLFVSSDLPEVLGvADRIVVMRE 471
|
....
gi 1005434824 752 GHIV 755
Cdd:PRK11288 472 GRIA 475
|
|
| ABC_6TM_ABCC_D1 |
cd18579 |
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group ... |
228-386 |
3.13e-06 |
|
Six-transmembrane helical domain 1 (TMD1) of the ABC transporters, subfamily C; This group represents the six-transmembrane domain 1 (TMD1)of the ABC transporters that belong to the ABCC subfamily, such as the sulphonylurea receptors SUR1/2 (ABCC8), the cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), Multidrug-Resistance associated Proteins (MRP1-9), VMR1 (vacuolar multidrug resistance protein 1), and YOR1 (yeast oligomycin resistance transporter protein). This TM subunit exhibits the type 3 ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The type 3 ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. By contrast, bacterial ABC exporters are typically assembled from dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are comprised of two identical TMDs and two identical NBDs.
Pssm-ID: 350023 [Multi-domain] Cd Length: 289 Bit Score: 49.79 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 228 IASVALLASSGSQIAAPYFFGRVIQASMEEGMSHLNKTIVLLSLIYLAGALAALVRSWLFTLaGQRLVARIRKQLFASVV 307
Cdd:cd18579 1 LAGLLKLLEDLLSLAQPLLLGLLISYLSSYPDEPLSEGYLLALALFLVSLLQSLLLHQYFFL-SFRLGMRVRSALSSLIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 308 E----QEVAFFDSNRTGELINRLSSDTQVIQNALtVNVSMLLRYIIQIIGSLAFMFSL---SAkLTG--VLISVVPIVGI 378
Cdd:cd18579 80 RkalrLSSSARQETSTGEIVNLMSVDVQRIEDFF-LFLHYLWSAPLQIIVALYLLYRLlgwAA-LAGlgVLLLLIPLQAF 157
|
....*...
gi 1005434824 379 GAQRYGSF 386
Cdd:cd18579 158 LAKLISKL 165
|
|
| ABC_6TM_MRP1_2_3_6_D2_like |
cd18603 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, ... |
274-383 |
3.20e-06 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated proteins (MRPs) 1, 2, 3 and 6, all of which are belonging to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350047 [Multi-domain] Cd Length: 296 Bit Score: 49.78 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 274 LAGALAALVRSWLFTLAGQRLVARIRKQLFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLLRYIIQIIG 353
Cdd:cd18603 52 LGQAIFVFLGSLALALGCVRASRNLHNKLLHNILRAPMSFFDTTPLGRILNRFSKDIDTVDNTLPQNIRSFLNCLFQVIS 131
|
90 100 110
....*....|....*....|....*....|
gi 1005434824 354 SLaFMFSLSAKLTGVLISVVPIVGIGAQRY 383
Cdd:cd18603 132 TL-VVISISTPIFLVVIIPLAILYFFIQRF 160
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
555-744 |
3.39e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 48.41 E-value: 3.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 555 DSDVLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAElDLFWLRRKIALVSQE----PVLfa 630
Cdd:PRK13540 13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFVGHRsginPYL-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 631 tTIAANIAYGCE--ATQEEIEKAAEQANAHNFIaSFEEGYqtqvgergvkLSGGQKQRVAIARALLMNPDVLLLDEATSA 708
Cdd:PRK13540 90 -TLRENCLYDIHfsPGAVGITELCRLFSLEHLI-DYPCGL----------LSSGQKRQVALLRLWMSKAKLWLLDEPLVA 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 1005434824 709 LDAESEHFVKEAID--RAMvNRTVLVIAHRLSTVRNAD 744
Cdd:PRK13540 158 LDELSLLTIITKIQehRAK-GGAVLLTSHQDLPLNKAD 194
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
678-767 |
6.76e-06 |
|
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: 49.44 E-value: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 678 KLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDR-AMVNRTVLVIAHRLSTVRN-ADQVLVID----K 751
Cdd:TIGR02633 403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGegklK 482
|
90
....*....|....*..
gi 1005434824 752 GHIVERG-THETLLAKA 767
Cdd:TIGR02633 483 GDFVNHAlTQEQVLAAA 499
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
648-759 |
9.00e-06 |
|
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: 47.99 E-value: 9.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 648 IEKAAE----QANAHNFIASFEE---GYqTQVGERGVKLSGGQKQRVAIARALLM---NPDVLLLDEATSALDAESEHFV 717
Cdd:cd03271 133 VEEALEffenIPKIARKLQTLCDvglGY-IKLGQPATTLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKL 211
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1005434824 718 KEAIDRaMVNR--TVLVIAHRLSTVRNADQvlVID--------KGHIVERGT 759
Cdd:cd03271 212 LEVLQR-LVDKgnTVVVIEHNLDVIKCADW--IIDlgpeggdgGGQVVASGT 260
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
646-710 |
9.29e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.47 E-value: 9.29e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 646 EEIEKAAEQANAHNFIA--SFEEGYQTQvgeRGVKLSGGQKQRVAIARALLMNPDVLLLDEATSALD 710
Cdd:PLN03073 313 ELIDAYTAEARAASILAglSFTPEMQVK---ATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
563-751 |
9.50e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 47.22 E-value: 9.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 563 SFELKPGETVaLVGPSGGGKSTVISLLE-------------RFYDPKsgVISIGrTNLAELDL-FWLRRKIAL-VSQEPV 627
Cdd:cd03240 17 EIEFFSPLTL-IVGQNGAGKTTIIEALKyaltgelppnskgGAHDPK--LIREG-EVRAQVKLaFENANGKKYtITRSLA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 628 LFAttiaaNIAYgCEatQEEIEKAAEQanahnfiasfeegyqtqvgERGvKLSGGQKQ------RVAIARALLMNPDVLL 701
Cdd:cd03240 93 ILE-----NVIF-CH--QGESNWPLLD-------------------MRG-RCSGGEKVlasliiRLALAETFGSNCGILA 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1005434824 702 LDEATSALDAES-EHFVKEAID--RAMVNRTVLVIAHRLSTVRNADQVLVIDK 751
Cdd:cd03240 145 LDEPTTNLDEENiEESLAEIIEerKSQKNFQLIVITHDEELVDAADHIYRVEK 197
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
568-753 |
1.06e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.20 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 568 PGETVALVGPSGGGKSTVIsllerfydpksgvisigrtnlaeldlfwlrrkialvsqEPVLFATTIAANIAYGCEATQEE 647
Cdd:cd03227 20 EGSLTIITGPNGSGKSTIL--------------------------------------DAIGLALGGAQSATRRRSGVKAG 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 648 IEKAAEQANAHNFIasfeegyqtqvgergVKLSGGQKQRVAIARAL---LMNPDVL-LLDEATSALDAESEHFVKEAI-D 722
Cdd:cd03227 62 CIVAAVSAELIFTR---------------LQLSGGEKELSALALILalaSLKPRPLyILDEIDRGLDPRDGQALAEAIlE 126
|
170 180 190
....*....|....*....|....*....|.
gi 1005434824 723 RAMVNRTVLVIAHRLSTVRNADQVLVIDKGH 753
Cdd:cd03227 127 HLVKGAQVIVITHLPELAELADKLIHIKKVI 157
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
562-765 |
1.48e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 47.87 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 562 MSFELKPGETVALVGPSGGGKSTVISLLerfydpkSGV------ISIGRTNLAELDLFWL----RRK-----IALVSQEP 626
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAI-------CGVtkdnwrVTADRMRFDDIDLLRLspreRRKlvghnVSMIFQEP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 627 vlfattiaaniaYGCEATQEEIEKAAEQAnahnfIA--SFEEGYQTQVGER-----------GVK------------LSG 681
Cdd:PRK15093 99 ------------QSCLDPSERVGRQLMQN-----IPgwTYKGRWWQRFGWRkrraiellhrvGIKdhkdamrsfpyeLTE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 682 GQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNR--TVLVIAHRLSTVRN-ADQVLVIDKGHIVERG 758
Cdd:PRK15093 162 GECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNntTILLISHDLQMLSQwADKINVLYCGQTVETA 241
|
....*..
gi 1005434824 759 THETLLA 765
Cdd:PRK15093 242 PSKELVT 248
|
|
| ABC_6TM_MRP4_D2_like |
cd18601 |
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) ... |
271-376 |
5.12e-05 |
|
Six-transmembrane helical domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4) and similar proteins; This group represents the six-transmembrane domain 2 (TMD2) of multidrug resistance-associated protein 4 (MRP4), which belongs to the subfamily C of the ATP-binding cassette (ABC) transporter superfamily. The MRP subfamily (ABCC subfamily) is composed of 13 members, of which MRP1 to MRP9 are the major transporters that cause multidrug resistance in tumor cells by pumping anticancer drugs out of the cell. These nine MRP members function as ATP-dependent exporters for endogenous substances and xenobiotics. MRP family can be divided into two groups, depending on their structural architecture. MRP4, MRP5, MRP8, and MRP9 (ABCC4, 5, 11 and 12, respectively) have a typical ABC transporter structure and each composed of two transmembrane domains (TMD1 and TMD2) and two nucleotide domains (NBD1 and NBD2). On the other hand, MRP1, 2, 3, 6 and 7 (ABCC1, 2, 3, 6 and 7, respectively) have an additional N-terminal five transmembrane segments in a single domain (TMD0) connected to the core (TMD-NBD) by a cytoplasmic linker (L0).
Pssm-ID: 350045 [Multi-domain] Cd Length: 314 Bit Score: 46.16 E-value: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 271 LIYLAGALAALV-----RSWLFTLAGQRLVARIRKQLFASVVEQEVAFFDSNRTGELINRLSSDTQVIQNALTVNVSMLL 345
Cdd:cd18601 62 LGIYAGLTAATFvfgflRSLLFFHVAVSASKNLHNKMFASVLRAPIRFFDTNPIGRILNRFSKDIGHLDDLLPLTFLDFL 141
|
90 100 110
....*....|....*....|....*....|.
gi 1005434824 346 RYIIQIIGSLAFMFSLsakLTGVLISVVPIV 376
Cdd:cd18601 142 QLLLQVVGVVLLAVVV---NPWVLIPVIPLV 169
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
559-710 |
5.42e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 559 LKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELDLF-WLRRKIALVSQEPVlfATTIAANI 637
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANeAINHGFALVTEERR--STGIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 638 aygceatqeEIEKAAEQANAHNFIASF----------------------EEGYQTQVGErgvkLSGGQKQRVAIARALLM 695
Cdd:PRK10982 342 ---------DIGFNSLISNIRNYKNKVglldnsrmksdtqwvidsmrvkTPGHRTQIGS----LSGGNQQKVIIGRWLLT 408
|
170
....*....|....*
gi 1005434824 696 NPDVLLLDEATSALD 710
Cdd:PRK10982 409 QPEILMLDEPTRGID 423
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
551-710 |
8.43e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 8.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 551 PSRPDSDVLKGMSFELKPGETVALVGPSGGGKS-TVISLLERFYDPK-SGVISI-GRtnlaELDLFWLRRKIA------- 620
Cdd:NF040905 268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRNiSGTVFKdGK----EVDVSTVSDAIDaglayvt 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 621 -------LVSQEPVLFATTIAA--NIA-YGCEATQEEIEKAAEQANAHNFIASfeegyqtQVGERGVKLSGGQKQRVAIA 690
Cdd:NF040905 344 edrkgygLNLIDDIKRNITLANlgKVSrRGVIDENEEIKVAEEYRKKMNIKTP-------SVFQKVGNLSGGNQQKVVLS 416
|
170 180
....*....|....*....|
gi 1005434824 691 RALLMNPDVLLLDEATSALD 710
Cdd:NF040905 417 KWLFTDPDVLILDEPTRGID 436
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
667-763 |
1.07e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 45.77 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 667 GYqTQVGERGVKLSGGQKQRVAIARALL---MNPDVLLLDEATSALdaeseHF--VKEAIDraMVNR------TVLVIAH 735
Cdd:TIGR00630 819 GY-IRLGQPATTLSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGL-----HFddIKKLLE--VLQRlvdkgnTVVVIEH 890
|
90 100 110
....*....|....*....|....*....|....*.
gi 1005434824 736 RLSTVRNADQvlVID--------KGHIVERGTHETL 763
Cdd:TIGR00630 891 NLDVIKTADY--IIDlgpeggdgGGTVVASGTPEEV 924
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
679-753 |
2.26e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 42.70 E-value: 2.26e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 679 LSGGQKQRVAIARALLMNPD--VLLLDEATSALDAESEHFVKEAIDRAM-VNRTVLVIAHRLSTVRNADQvlVIDKGH 753
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIdLGNTVILIEHNLDVLSSADW--IIDFGP 163
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
672-738 |
2.37e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.84 E-value: 2.37e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 672 VGERGVK-LSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIdRAMVN--RTVLVIAHRLS 738
Cdd:PLN03140 1012 VGLPGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTV-RNTVDtgRTVVCTIHQPS 1080
|
|
| ABC_6TM_T1SS_like |
cd18779 |
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ... |
269-500 |
3.63e-04 |
|
uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 secretion systems, and similar proteins; uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) and similar proteins. These transporter subunits include HylB, PrtD, CyaB, CvaB, RsaD, HasD, LipB, and LapB, among many others. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). Most targeted proteins are not cleaved at the N terminus, but rather carry signals located toward the extreme C terminus to direct type I secretion. However, the 10 kDa Escherichia coli colicin V (CvaB) targets the ABC transporter using a cleaved, N-terminal signal sequence. Almost all transport substrates of the type I system have critical functions in attacking host cells either directly or by being essential for host colonization. The ABC-dependent T1SS transports various molecules, from ions, drugs, to proteins of various sizes up to 900 kDa. The molecules secreted vary in size from the small Escherichia coli peptide colicin V, (10 kDa) to the Pseudomonas fluorescens cell adhesion protein LapA of 520 kDa. The best characterized are the RTX toxins such as the adenylate cyclase (CyaA) toxin from Bordetella pertussis, the causative agent of whooping cough, and the lipases such as LipA. Type I secretion is also involved in export of non-protein substrates such as cyclic beta-glucans and polysaccharides.
Pssm-ID: 350052 [Multi-domain] Cd Length: 294 Bit Score: 43.30 E-value: 3.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 269 LSLIYLAGALAALVRSWLFtlagQRLVARIRKQLFASVVEQEV----AFFDSNRTGELINRLSSDTqVIQNALTVNV-SM 343
Cdd:cd18779 48 LAALVLTQLLAGLLRSHLL----LRLRTRLDTQLTLGFLEHLLrlpyRFFQQRSTGDLLMRLSSNA-TIRELLTSQTlSA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 344 LLRYIIqIIGSLAFMFSLSAKLTGVLisvvpiVGIGAQRYGSFVqGLRKRFQD----ELAAASSTAEEAI---ANIRTVR 416
Cdd:cd18779 123 LLDGTL-VLGYLALLFAQSPLLGLVV------LGLAALQVALLL-ATRRRVRElmarELAAQAEAQSYLVealSGIETLK 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 417 SFSQERKSM----NSYDTDIDKSYKSGaklaLASGFFNGVIGIIGQGAVVLVLWYGGSLVNKHELDVGILTAfmlytLNv 492
Cdd:cd18779 195 ASGAEDRALdrwsNLFVDQLNASLRRG----RLDALVDALLATLRLAAPLVLLWVGAWQVLDGQLSLGTMLA-----LN- 264
|
....*...
gi 1005434824 493 AMAFAFLS 500
Cdd:cd18779 265 ALAGAFLA 272
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
682-710 |
3.87e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 43.73 E-value: 3.87e-04
10 20
....*....|....*....|....*....
gi 1005434824 682 GQKQRVAIARALLMNPDVLLLDEATSALD 710
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLD 187
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
678-768 |
4.42e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.96 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 678 KLSGGQKQRVAIARALLMNPDVLLLDEATSALDAESEHFVKEAIDRAMVNR---TVLVI------AHRLstvrnaDQVLV 748
Cdd:NF033858 136 KLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpgmSVLVAtaymeeAERF------DWLVA 209
|
90 100
....*....|....*....|
gi 1005434824 749 IDKGHIVERGTHETLLAKAG 768
Cdd:NF033858 210 MDAGRVLATGTPAELLARTG 229
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
558-750 |
5.45e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.78 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 558 VLKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVISIGRTNLAELdlfwlrrkialvsQEPvlFATTIAANI 637
Cdd:PRK13541 15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-------------AKP--YCTYIGHNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 638 AYGCEATQEE-------IEKAAE--QANAHNFiasfeeGYQTQVGERGVKLSGGQKQRVAIARALLMNPDVLLLDEATSA 708
Cdd:PRK13541 80 GLKLEMTVFEnlkfwseIYNSAEtlYAAIHYF------KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETN 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1005434824 709 LDAESEHFVKEAID-RAMVNRTVLVIAHRLSTVRNAdQVLVID 750
Cdd:PRK13541 154 LSKENRDLLNNLIVmKANSGGIVLLSSHLESSIKSA-QILQLD 195
|
|
| ABC_6TM_VMR1_D1_like |
cd18596 |
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; ... |
233-423 |
5.98e-04 |
|
Six-transmembrane helical domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1; ABCC subfamily; This group includes the six-transmembrane domain 1 (TMD1) of the yeast Vmr1p, Ybt1p and Nft1, all of which are ABC transporters of the MRP (multidrug resistance-associated protein) subfamily (ABCC). Yeast ABCC (also termed MRP/CFTR) subfamily includes six members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p, Vmr1p, and Yor1p), of which three members (Ycf1p, Bpt1P and Yor1p) are not included here. While Yor1p, an oligomycin resistance ABC transporter, has been shown to localize to the plasma membrane, the other 4 members (Ycf1p, Bpt1p, Ybt1p/Bat1p, Nft1p and Vmr1p) have been shown to localize to the vacuolar membrane. Ybt1p is originally identified as a bile acid transporter and regulates membrane fusion through Ca2+ transport modulation. Ybt1p also plays a part in ade2 pigment transport. Moreover, Ybt1p has been recently shown to translocate phosphatidylcholine from the outer leaflet of the vacuole to the inner leaflet for degradation and choline recycling. Vmr1p, a vacuolar membrane protein, participates in the export of numerous growth inhibitors from the cell, such as cycloheximide, 2,4-dinitrophenole, cadmium and other toxic metals. Nft1p is not well-characterized, but it is proposed to be regulate Ycf1p, which is involved in heavy metal detoxification.
Pssm-ID: 350040 [Multi-domain] Cd Length: 309 Bit Score: 42.87 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 233 LLASSGSQIAAPYFFGRVIQaSMEEGMS-HLNKTIVLLSLIYLAGALAALVRSWLFtLAGQRLVARIRKQL--------- 302
Cdd:cd18596 6 AVLSSVLSFAPPFFLNRLLR-YLEDPGEdATVRPWVWVLLLFLGPLLSSLLDQQYL-WIGRRLSVRLRAILtqlifekal 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 303 ----FASVVEQEVAFFD----------SNRTGELINRLSSDTQVIQNALTVnVSMLLRYIIQIIGSLAFMFSL---SAkL 365
Cdd:cd18596 84 rrrdKSGSSKSSESKKKdkeededeksSASVGKINNLMSVDANRISEFAAF-LHLLVSAPLQIVIAIVFLYRLlgwSA-L 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1005434824 366 TGVLISVV--PIVGIGAQRYGSFVQGLRKRfQD-------ELaaasstaeeaIANIRTVRSFSQERK 423
Cdd:cd18596 162 VGLAVMVLllPLNGYLAKRYSRAQKELMKA-RDarvqlvtEV----------LQGIRMIKFFAWERK 217
|
|
| ABC_6TM_McjD_like |
cd18556 |
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter ... |
226-510 |
5.99e-04 |
|
Six-transmembrane helical domain of the antibacterial peptide ATP-binding cassette transporter McjD and similar proteins; This group represents the 6-TM subunit of the ABC transporter McjD that exports the antibacterial peptide microcin J25, which is an antimicrobial peptide produced by Enterobacteriaceae against other microorganisms for survival under nutrient starvation. Thus, the ABC exporter McjD provides self-immunity of the producing bacteria through export of the toxic peptide out of the cell. Bacterial ABC exporters are typically expressed as half-transporters that contain one transmembrane domain (TMD) fused to a nucleotide-binding domain (NBD), which dimerize to form the full transporter.
Pssm-ID: 350000 Cd Length: 298 Bit Score: 42.63 E-value: 5.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 226 LFIASVALLASSGSQIAAPYFFGRVIQASMEEGmSHLNKTIVLLSLIYLAG-ALAALVRSWLFTLAGQ---RLVARIRKQ 301
Cdd:cd18556 4 FFSILFISLLSSILISISPVILAKITDLLTSSS-SDSYNYIVVLAALYVITiSATKLLGFLSLYLQSSlrvELIISISSS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 302 LFASVVEQEVAFFDSNRTGEL---INRLSSDTQVIQNALTVNvsmLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIV-G 377
Cdd:cd18556 83 YFRYLYEQPKTFFVKENSGDItqrLNQASNDLYTLVRNLSTN---ILPPLLQLIIAIVVILSSGDYFVAALFLLYAVLfV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 378 IGAQRYGSFVQGLRKRFQDELAAASSTAEEAIANIRTVRSFSQERKSMNSYDTDIDK---SYKSGAKLALASGFFNGVIG 454
Cdd:cd18556 160 INNTIFTKKIVSLRNDLMDAGRKSYSLLTDSVKNIVAAKQNNAFDFLFKRYEATLTNdrnSQKRYWKLTFKMLILNSLLN 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1005434824 455 IIGQGAVVLVLWYGgslVNKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAV 510
Cdd:cd18556 240 VILFGLSFFYSLYG---VVNGQVSIGHFVLITSYILLLSTPIESLGNMLSELRQSV 292
|
|
| ABC_6TM_AarD_CydD |
cd18584 |
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ... |
229-382 |
8.19e-04 |
|
Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH transporter, and a homolog AarD; The CydD protein, together with the CydC protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. Mutations in AarD, a homolog from Providencia stuartii, also show phenotypic characteristic consistent with a defect in the cytochrome d oxidase. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350028 [Multi-domain] Cd Length: 290 Bit Score: 42.01 E-value: 8.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 229 ASVALLASSGSQIAAPYFFGRVIQASMEEGM--SHLNKTIVLLSLIYLAGALAALVRSWLFTLAGQRLVARIRKQLFASV 306
Cdd:cd18584 1 AVLLGLLAALLIIAQAWLLARIIAGVFLEGAglAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 307 VEQEVAFFDSNRTGELINRLSSDTQVIQNALTvnvsmllRYIIQIIGS-------LAFMFSLSaKLTGVLISV----VPI 375
Cdd:cd18584 81 LALGPALLRRQSSGELATLLTEGVDALDGYFA-------RYLPQLVLAaivplliLVAVFPLD-WVSALILLVtaplIPL 152
|
170
....*....|.
gi 1005434824 376 ----VGIGAQR 382
Cdd:cd18584 153 fmilIGKAAQA 163
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
638-751 |
9.29e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.97 E-value: 9.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 638 AYGCEATQEEIEKAAEQ---ANAHNFIASFE---------EGYQTQVGERGV-----KLSGGQKQ------RVAIARALL 694
Cdd:PRK01156 744 AFDKSGVPAMIRKSASQamtSLTRKYLFEFNldfddidvdQDFNITVSRGGMvegidSLSGGEKTavafalRVAVAQFLN 823
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1005434824 695 MNPDVLLLDEATSALDAESEHFVKEAIDRAMVNRT----VLVIAHRLSTVRNADQVLVIDK 751
Cdd:PRK01156 824 NDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSdipqVIMISHHRELLSVADVAYEVKK 884
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
559-766 |
1.60e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 41.34 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 559 LKGMSFELKPGETVALVGPSGGGKSTVISLLERFYDPKSGVIS-IGRTNLAELDlfwlrrkIALVSQepvlfaTTIAANI 637
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDrNGEVSVIAIS-------AGLSGQ------LTGIENI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 638 AYGCEA---TQEEIEKAAEQanahnfIASFEEgyqtqVGE---RGVK-LSGGQKQRVAIARALLMNPDVLLLDEATSALD 710
Cdd:PRK13546 107 EFKMLCmgfKRKEIKAMTPK------IIEFSE-----LGEfiyQPVKkYSSGMRAKLGFSINITVNPDILVIDEALSVGD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1005434824 711 aesEHFVKEAIDRAM----VNRTVLVIAHRLSTVRN-ADQVLVIDKGHIVERGTHETLLAK 766
Cdd:PRK13546 176 ---QTFAQKCLDKIYefkeQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK 233
|
|
| PRK01889 |
PRK01889 |
GTPase RsgA; Reviewed |
566-589 |
2.90e-03 |
|
GTPase RsgA; Reviewed
Pssm-ID: 234988 [Multi-domain] Cd Length: 356 Bit Score: 40.69 E-value: 2.90e-03
|
| ABC_6TM_CydC |
cd18585 |
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH ... |
318-517 |
4.23e-03 |
|
Six-transmembrane helical domain (6-TMD) of the CydC, a component of the ABC cysteine/GSH transporter; The CydC protein, together with the CydD protein, constitutes a bacterial heterodimeric ATP-binding cassette (ABC) transporter complex required for formation of the functional cytochrome bd oxidase in both gram-positive and gram-negative aerobic bacteria. In Escherichia coli, the biogenesis of both cytochrome bd-type quinol oxidases and periplasmic cytochromes requires the ABC-type cysteine/GSH transporter CydDC, which exports cysteine and glutathione from the cytoplasm to the periplasm to maintain redox homeostasis. The CydDC forms a heterodimeric ABC transporter with two transmembrane domains (TMDs), each predicted to comprise six TM alpha-helices and two nucleotide binding domains (NBDs).
Pssm-ID: 350029 [Multi-domain] Cd Length: 290 Bit Score: 40.16 E-value: 4.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 318 RTGELINRLSSDTQVIQNA-LTVnVSMLLRYIIQIIGSLAFMFSLSAKLTGVLISVVPIVGIG----AQRYGSFVQGLRK 392
Cdd:cd18585 90 RSGDLLNRIVADIDTLDNLyLRV-LSPPVVALLVILATILFLAFFSPALALILLAGLLLAGVVipllFYRLGKKIGQQLV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 393 RFQDELAAASSTAeeaIANIRTVRSFSQERKSMNSYDTDIDKSYKSGAKLALASGFFNGVIGIIGQGAVVLVLWYGGSLV 472
Cdd:cd18585 169 QLRAELRTELVDG---LQGMAELLIFGALERQRQQLEQLSDALIKEQRRLARLSGLSQALMILLSGLTVWLVLWLGAPLV 245
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1005434824 473 NKHELDVGILTAFMLYTLNVAMAFAFLSSVYGDFMQAVGASVRMF 517
Cdd:cd18585 246 QNGALDGALLAMLVFAVLASFEAVAPLPLAFQYLGETRAAARRLF 290
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
679-752 |
4.41e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 39.55 E-value: 4.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1005434824 679 LSGGQKQRVAIARALLMNPDVLL--LDEATSALDAESEHFVKEAID--RAMVNrTVLVIAHRLSTVRNADQvlVIDKG 752
Cdd:cd03270 138 LSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKrlRDLGN-TVLVVEHDEDTIRAADH--VIDIG 212
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
679-770 |
7.21e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 40.01 E-value: 7.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1005434824 679 LSGGQKQRVAIARAlLMNPD----VLLLDEATSALdaeseHF--VK---EAIDRaMVNR--TVLVIAHRLSTVRNADQvl 747
Cdd:COG0178 827 LSGGEAQRVKLASE-LSKRStgktLYILDEPTTGL-----HFhdIRkllEVLHR-LVDKgnTVVVIEHNLDVIKTADW-- 897
|
90 100 110
....*....|....*....|....*....|.
gi 1005434824 748 VID--------KGHIVERGTHETLLAKAGVY 770
Cdd:COG0178 898 IIDlgpeggdgGGEIVAEGTPEEVAKVKASY 928
|
|
| |
