NCBI Conserved Domain Search

Conserved domains on [gi|1582666899|gb|TBE47250|]

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ABC transporter ATP-binding protein [Rhizobium ruizarguesonis]

Protein Classification

ABC transporter ATP-binding protein( domain architecture ID 11438555)

ABC transporter ATP-binding protein ABC transporter ATP-binding protein containing both ATPase and permease components of an ABC-type transport system

CATH: 3.40.50.300

EC: 7.-.-.-

Gene Ontology: GO:0055052|GO:0140359|GO:0042626|GO:0005524|GO:0016887

PubMed: 19234479|26517916|10529352|24638992|25750732

SCOP: 4003976

TCDB: 3.A.1

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

MdlB

COG1132

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

29-587

0e+00

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

Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 639.52 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  29 RDHLWGYVFAIACLIVVALSTAFTAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARY 108
Cdd:COG1132    17 RPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 109 QRRLYAHLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLY 188
Cdd:COG1132    97 RRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLL 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 189 ALRYVSKRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSPLTESFAG 268
Cdd:COG1132   177 VLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGN 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 269 FAVASVLAYAAYRSIYFNVPPGAFFSFVTALLLAYDPARRLARLQVQMERAVVNARMIYELLDMEPRQRDLPDARPLTVT 348
Cdd:COG1132   257 LGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPPGAVPLPPV 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 349 QARIEFRNVSFAYGNES-VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQL 427
Cdd:COG1132   337 RGEIEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQI 416

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 428 AYVSQQPYLFEGTIRDNIRYGRPEATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAP 507
Cdd:COG1132   417 GVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPP 496

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 508 ILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAKvSDGLYARLNNLQ 587
Cdd:COG1132   497 ILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLA-RGGLYARLYRLQ 575

Name

Accession

Description

Interval

E-value

MdlB

COG1132

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

29-587

0e+00

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

Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 639.52 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  29 RDHLWGYVFAIACLIVVALSTAFTAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARY 108
Cdd:COG1132    17 RPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 109 QRRLYAHLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLY 188
Cdd:COG1132    97 RRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLL 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 189 ALRYVSKRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSPLTESFAG 268
Cdd:COG1132   177 VLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGN 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 269 FAVASVLAYAAYRSIYFNVPPGAFFSFVTALLLAYDPARRLARLQVQMERAVVNARMIYELLDMEPRQRDLPDARPLTVT 348
Cdd:COG1132   257 LGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPPGAVPLPPV 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 349 QARIEFRNVSFAYGNES-VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQL 427
Cdd:COG1132   337 RGEIEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQI 416

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 428 AYVSQQPYLFEGTIRDNIRYGRPEATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAP 507
Cdd:COG1132   417 GVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPP 496

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 508 ILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAKvSDGLYARLNNLQ 587
Cdd:COG1132   497 ILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLA-RGGLYARLYRLQ 575

MsbA_lipidA

TIGR02203

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...

29-587

7.12e-168

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: 489.61 E-value: 7.12e-168

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  29 RDHLWGYVFAIACLIVVALSTAFTAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARY 108
Cdd:TIGR02203  10 RPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSWVSNKVVRDI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 109 QRRLYAHLMTLSVGFFSEARSAHI-------AAQVSQNVSGIrdvlnltITSTVRDLLTFVSLLAVMILQDPLLSLAVFI 181
Cdd:TIGR02203  90 RVRMFEKLLGLPVSFFDRQPTGTLlsritfdSEQVASAATDA-------FIVLVRETLTVIGLFIVLLYYSWQLTLIVVV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 182 MAPPLLYALRYVSKRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSP 261
Cdd:TIGR02203 163 MLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSP 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 262 LTESFAGFAVASVLAYAAYRSIYFNVPPGAFFSFVTALLLAYDPARRLARLQVQMERAVVNARMIYELLDMEPRQRDlpD 341
Cdd:TIGR02203 243 ITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDT--G 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 342 ARPLTVTQARIEFRNVSFAYGNES--VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHIT 419
Cdd:TIGR02203 321 TRAIERARGDVEFRNVTFRYPGRDrpALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 420 KKSLRQQLAYVSQQPYLFEGTIRDNIRYGRP-EATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSI 498
Cdd:TIGR02203 401 LASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAI 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 499 ARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAKvSDG 578
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLA-RNG 559


                  ....*....
gi 1582666899 579 LYARLNNLQ 587
Cdd:TIGR02203 560 LYAQLHNMQ 568

PRK11176

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

33-587

1.71e-137

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

Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 412.49 E-value: 1.71e-137

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  33 WGYVFAIACLIVVALSTAFTAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRL 112
Cdd:PRK11176   25 AGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKADRSVLKWMPLVVIGLMILRGITSFISSYCISWVSGKVVMTMRRRL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 113 YAHLMTLSVGFFSE-------ARSAHIAAQVSQNVSGirdvlnlTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPP 185
Cdd:PRK11176  105 FGHMMGMPVSFFDKqstgtllSRITYDSEQVASSSSG-------ALITVVREGASIIGLFIMMFYYSWQLSLILIVIAPI 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 186 LLYALRYVSKRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSPLTES 265
Cdd:PRK11176  178 VSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSISDPIIQL 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 266 FAGFAVASVLAYAAYRSIYFNVPPGAF---FSFVTALLlayDPARRLARLQVQMERAVVNARMIYELLDMEPRQrdlpDA 342
Cdd:PRK11176  258 IASLALAFVLYAASFPSVMDTLTAGTItvvFSSMIALM---RPLKSLTNVNAQFQRGMAACQTLFAILDLEQEK----DE 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 343 RPLTVTQAR--IEFRNVSFAY--GNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHI 418
Cdd:PRK11176  331 GKRVIERAKgdIEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDY 410

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 419 TKKSLRQQLAYVSQQPYLFEGTIRDNIRYGRPEA-TDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLS 497
Cdd:PRK11176  411 TLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIA 490

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 498 IARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAKvSD 577
Cdd:PRK11176  491 IARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLA-QN 569

                         570
                  ....*....|
gi 1582666899 578 GLYARLNNLQ 587
Cdd:PRK11176  570 GVYAQLHKMQ 579

ABC_MTABC3_MDL1_MDL2

cd03249

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...

352-587

7.63e-126

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: 369.56 E-value: 7.63e-126

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAY---GNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLA 428
Cdd:cd03249     1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 429 YVSQQPYLFEGTIRDNIRYGRPEATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAPI 508
Cdd:cd03249    81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582666899 509 LLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAKvSDGLYARLNNLQ 587
Cdd:cd03249   161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMA-QKGVYAKLVKAQ 238

ABC_tran

pfam00005

ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...

367-516

5.63e-44

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.

Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 153.57 E-value: 5.63e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 367 LSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYVSQQPYLF-EGTIRDNI 445
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582666899 446 RYGRP------EATDAEVEEAARLAYAHDFIsaqpqgyETPVGENGVTLSGGQRQRLSIARALVRNAPILLLDEATS 516
Cdd:pfam00005  81 RLGLLlkglskREKDARAEEALEKLGLGDLA-------DRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150

AztA

NF040873

zinc ABC transporter ATP-binding protein AztA;

360-558

2.05e-25

zinc ABC transporter ATP-binding protein AztA;

Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 103.47 E-value: 2.05e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 360 AYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGqdiahitkkslRQQLAYVSQQ---PYL 436
Cdd:NF040873    1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRsevPDS 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 437 FEGTIRDNIRYG---------RPEATD-AEVEEAARLAYAHDFISAQPQgyetpvgengvTLSGGQRQRLSIARALVRNA 506
Cdd:NF040873   70 LPLTVRDLVAMGrwarrglwrRLTRDDrAAVDDALERVGLADLAGRQLG-----------ELSGGQRQRALLAQGLAQEA 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 507 PILLLDEATSALDTESEAAVQKAL-DEAMSGRTVVVIAHRLSTVVRADKIVVM 558
Cdd:NF040873  139 DLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191

GguA

NF040905

sugar ABC transporter ATP-binding protein;

367-565

2.15e-14

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.98 E-value: 2.15e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 367 LSGVSFTAEGGATTALVGPSGAGKST---VISLI-PrfYDPREGEILIDGQDIAHitkKSLR-----------QQLAYVs 431
Cdd:NF040905   17 LDDVNLSVREGEIHALCGENGAGKSTlmkVLSGVyP--HGSYEGEILFDGEVCRF---KDIRdsealgiviihQELALI- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 qqPYLfegTIRDNIRYGRPEAT------DAEVEEAARLaYAHDFISAQPQgyeTPVGENGVtlsgGQRQRLSIARALVRN 505
Cdd:NF040905   91 --PYL---SIAENIFLGNERAKrgvidwNETNRRAREL-LAKVGLDESPD---TLVTDIGV----GKQQLVEIAKALSKD 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1582666899 506 APILLLDEATSAL-DTESEAAVQKALDEAMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVE 565
Cdd:NF040905  158 VKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219

AAA

smart00382

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...

377-562

3.13e-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: 58.92 E-value: 3.13e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  377 GATTALVGPSGAGKSTVISLIPRFYDPREGE-ILIDGQDIAHITKKSLRQqlayvsqqpylfegtirdnirygrpeatda 455
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLL------------------------------ 51

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  456 eveeaarlayahdfisaqpqgyeTPVGENGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAM- 534
Cdd:smart00382  52 -----------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLl 108

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1582666899  535 ------SGRTVVVIAHRLSTVV------RADKIVVMQQGR 562
Cdd:smart00382 109 lllkseKNLTVILTTNDEKDLGpallrrRFDRRIVLLLIL 148

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

352-519

2.95e-07

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.59 E-value: 2.95e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAhitKKSLRQQL---- 427
Cdd:NF033858    2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA---DARHRRAVcpri 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 428 AYVSQ------QPYLfegTIRDNIRY-GRPEATDAEVEEA--ARLAYA---HDFIsaqpqgyETPVGEngvtLSGGQRQR 495
Cdd:NF033858   79 AYMPQglgknlYPTL---SVFENLDFfGRLFGQDAAERRRriDELLRAtglAPFA-------DRPAGK----LSGGMKQK 144

                         170       180
                  ....*....|....*....|....
gi 1582666899 496 LSIARALVRNAPILLLDEATSALD 519
Cdd:NF033858  145 LGLCCALIHDPDLLILDEPTTGVD 168

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

370-519

4.52e-05

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.66 E-value: 4.52e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 370 VSFTAEGGATTALVGPSGAGKSTVIS----LIPrfydPREGEIL-----IDGQDIAhitkksLRQQLAYVSQQPYLF-EG 439
Cdd:NF033858  285 VSFRIRRGEIFGFLGSNGCGKSTTMKmltgLLP----ASEGEAWlfgqpVDAGDIA------TRRRVGYMSQAFSLYgEL 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 440 TIRDNIR-----YGRPEATDAE-VEEAAR---LAyahDFISAQPQGyetpvgengvtLSGGQRQRLSIARALVRNAPILL 510
Cdd:NF033858  355 TVRQNLElharlFHLPAAEIAArVAEMLErfdLA---DVADALPDS-----------LPLGIRQRLSLAVAVIHKPELLI 420


                  ....*....
gi 1582666899 511 LDEATSALD 519
Cdd:NF033858  421 LDEPTSGVD 429

40850658_otr

NF000106

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

482-572

1.84e-04

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

Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.96 E-value: 1.84e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 482 GENGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVqkaLDEAMS----GRTVVVIAHRLSTVVR-ADKIV 556
Cdd:NF000106  139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEV---WDEVRSmvrdGATVLLTTQYMEEAEQlAHELT 215

                          90
                  ....*....|....*.
gi 1582666899 557 VMQQGRVVEEGNHETL 572
Cdd:NF000106  216 VIDRGRVIADGKVDEL 231

GguA

NF040905

sugar ABC transporter ATP-binding protein;

366-566

2.43e-03

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 2.43e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 366 VLSGVSFTAEGGATTALVGPSGAGKS-TVISLIPRFYDPR-EGEILIDGQDIAHIT-KKSLRQQLAYVS----QQPYLFE 438
Cdd:NF040905  275 VVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRNiSGTVFKDGKEVDVSTvSDAIDAGLAYVTedrkGYGLNLI 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 439 GTIRDNI---------RYGRpeatdaeVEEAARLAYAHDFISAQpqGYETP-VGENGVTLSGGQRQRLSIARALVRNAPI 508
Cdd:NF040905  355 DDIKRNItlanlgkvsRRGV-------IDENEEIKVAEEYRKKM--NIKTPsVFQKVGNLSGGNQQKVVLSKWLFTDPDV 425

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 509 LLLDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLSTVV-RADKIVVMQQGRVVEE 566
Cdd:NF040905  426 LILDEPTRGIDVGAKYEIYTIINElAAEGKGVIVISSELPELLgMCDRIYVMNEGRITGE 485

Name

Accession

Description

Interval

E-value

MdlB

COG1132

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

29-587

0e+00

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

Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 639.52 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  29 RDHLWGYVFAIACLIVVALSTAFTAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARY 108
Cdd:COG1132    17 RPYRGLLILALLLLLLSALLELLLPLLLGRIIDALLAGGDLSALLLLLLLLLGLALLRALLSYLQRYLLARLAQRVVADL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 109 QRRLYAHLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLY 188
Cdd:COG1132    97 RRDLFEHLLRLPLSFFDRRRTGDLLSRLTNDVDAVEQFLAHGLPQLVRSVVTLIGALVVLFVIDWRLALIVLLVLPLLLL 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 189 ALRYVSKRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSPLTESFAG 268
Cdd:COG1132   177 VLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRANLRAARLSALFFPLMELLGN 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 269 FAVASVLAYAAYRSIYFNVPPGAFFSFVTALLLAYDPARRLARLQVQMERAVVNARMIYELLDMEPRQRDLPDARPLTVT 348
Cdd:COG1132   257 LGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIPDPPGAVPLPPV 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 349 QARIEFRNVSFAYGNES-VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQL 427
Cdd:COG1132   337 RGEIEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQI 416

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 428 AYVSQQPYLFEGTIRDNIRYGRPEATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAP 507
Cdd:COG1132   417 GVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGERGVNLSGGQRQRIAIARALLKDPP 496

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 508 ILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAKvSDGLYARLNNLQ 587
Cdd:COG1132   497 ILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIVEQGTHEELLA-RGGLYARLYRLQ 575

MsbA_lipidA

TIGR02203

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...

29-587

7.12e-168

Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 489.61 E-value: 7.12e-168

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  29 RDHLWGYVFAIACLIVVALSTAFTAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARY 108
Cdd:TIGR02203  10 RPYKAGLVLAGVAMILVAATESTLAALLKPLLDDGFGGRDRSVLWWVPLVVIGLAVLRGICSFVSTYLLSWVSNKVVRDI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 109 QRRLYAHLMTLSVGFFSEARSAHI-------AAQVSQNVSGIrdvlnltITSTVRDLLTFVSLLAVMILQDPLLSLAVFI 181
Cdd:TIGR02203  90 RVRMFEKLLGLPVSFFDRQPTGTLlsritfdSEQVASAATDA-------FIVLVRETLTVIGLFIVLLYYSWQLTLIVVV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 182 MAPPLLYALRYVSKRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSP 261
Cdd:TIGR02203 163 MLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAMKMTSAGSISSP 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 262 LTESFAGFAVASVLAYAAYRSIYFNVPPGAFFSFVTALLLAYDPARRLARLQVQMERAVVNARMIYELLDMEPRQRDlpD 341
Cdd:TIGR02203 243 ITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLLDSPPEKDT--G 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 342 ARPLTVTQARIEFRNVSFAYGNES--VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHIT 419
Cdd:TIGR02203 321 TRAIERARGDVEFRNVTFRYPGRDrpALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 420 KKSLRQQLAYVSQQPYLFEGTIRDNIRYGRP-EATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSI 498
Cdd:TIGR02203 401 LASLRRQVALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGENGVLLSGGQRQRLAI 480

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 499 ARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAKvSDG 578
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIVERGTHNELLA-RNG 559


                  ....*....
gi 1582666899 579 LYARLNNLQ 587
Cdd:TIGR02203 560 LYAQLHNMQ 568

SunT

COG2274

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...

31-587

4.93e-165

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: 487.42 E-value: 4.93e-165

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  31 HLWGYVFAIACLI-VVALSTAFtawIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQ 109
Cdd:COG2274   156 RLLLQVLLASLLInLLALATPL---FTQVVIDRVLPNQDLSTLWVLAIGLLLALLFEGLLRLLRSYLLLRLGQRIDLRLS 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 110 RRLYAHLMTLSVGFFSEARSAHIAAQVSQNVSgIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYA 189
Cdd:COG2274   233 SRFFRHLLRLPLSFFESRSVGDLASRFRDVES-IREFLTGSLLTALLDLLFVLIFLIVLFFYSPPLALVVLLLIPLYVLL 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 190 LRYVSKRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSPLTESFAGF 269
Cdd:COG2274   312 GLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYLNARFKLRRLSNLLSTLSGLLQQL 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 270 AVASVLAYAAYRSIYFNVPPGAFFSFVTALLLAYDPARRLARLQVQMERAVVNARMIYELLDMEPRQRDLPDARPLTVTQ 349
Cdd:COG2274   392 ATVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDDILDLPPEREEGRSKLSLPRLK 471

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 350 ARIEFRNVSFAYGNES--VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQL 427
Cdd:COG2274   472 GDIELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQI 551

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 428 AYVSQQPYLFEGTIRDNIRYGRPEATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAP 507
Cdd:COG2274   552 GVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGEGGSNLSGGQRQRLAIARALLRNPR 631

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 508 ILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAKvSDGLYARLNNLQ 587
Cdd:COG2274   632 ILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLA-RKGLYAELVQQQ 710

MsbA_rel

TIGR02204

ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...

29-587

3.60e-138

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: 413.71 E-value: 3.60e-138

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  29 RDHLWGYVFAIACLIVVALSTAFTAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARY 108
Cdd:TIGR02204  14 RPYRGRVLAALVALLITAAATLSLPYAVRLMIDHGFSKDSSGLLNRYFAFLLVVALVLALGTAARFYLVTWLGERVVADI 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 109 QRRLYAHLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLY 188
Cdd:TIGR02204  94 RRAVFAHLISLSPSFFDKNRSGEVVSRLTTDTTLLQSVIGSSLSMALRNALMCIGGLIMMFITSPKLTSLVLLAVPLVLL 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 189 ALRYVSKRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTmEEELERKvnkLIKGAESRANRIARLSERTSPLTESFAG 268
Cdd:TIGR02204 174 PILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFG-HEDAERS---RFGGAVEKAYEAARQRIRTRALLTAIVI 249

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 269 F----AVASVLAYAAYRSIYFNVPPGAFFSFVTALLLAYDPARRLARLQVQMERAVVNARMIYELLDMEPRQRDLPDARP 344
Cdd:TIGR02204 250 VlvfgAIVGVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERLIELLQAEPDIKAPAHPKT 329

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 345 LTV-TQARIEFRNVSFAYG---NESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITK 420
Cdd:TIGR02204 330 LPVpLRGEIEFEQVNFAYParpDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDP 409

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 421 KSLRQQLAYVSQQPYLFEGTIRDNIRYGRPEATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSIAR 500
Cdd:TIGR02204 410 AELRARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYLGERGVTLSGGQRQRIAIAR 489

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 501 ALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAKvSDGLY 580
Cdd:TIGR02204 490 AILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQGRIVAQGTHAELIA-KGGLY 568


                  ....*..
gi 1582666899 581 ARLNNLQ 587
Cdd:TIGR02204 569 ARLARLQ 575

PRK11176

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

33-587

1.71e-137

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

Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 412.49 E-value: 1.71e-137

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  33 WGYVFAIACLIVVALSTAFTAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRL 112
Cdd:PRK11176   25 AGLIVAGVALILNAASDTFMLSLLKPLLDDGFGKADRSVLKWMPLVVIGLMILRGITSFISSYCISWVSGKVVMTMRRRL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 113 YAHLMTLSVGFFSE-------ARSAHIAAQVSQNVSGirdvlnlTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPP 185
Cdd:PRK11176  105 FGHMMGMPVSFFDKqstgtllSRITYDSEQVASSSSG-------ALITVVREGASIIGLFIMMFYYSWQLSLILIVIAPI 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 186 LLYALRYVSKRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSPLTES 265
Cdd:PRK11176  178 VSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRFDKVSNRMRQQGMKMVSASSISDPIIQL 257

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 266 FAGFAVASVLAYAAYRSIYFNVPPGAF---FSFVTALLlayDPARRLARLQVQMERAVVNARMIYELLDMEPRQrdlpDA 342
Cdd:PRK11176  258 IASLALAFVLYAASFPSVMDTLTAGTItvvFSSMIALM---RPLKSLTNVNAQFQRGMAACQTLFAILDLEQEK----DE 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 343 RPLTVTQAR--IEFRNVSFAY--GNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHI 418
Cdd:PRK11176  331 GKRVIERAKgdIEFRNVTFTYpgKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDY 410

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 419 TKKSLRQQLAYVSQQPYLFEGTIRDNIRYGRPEA-TDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLS 497
Cdd:PRK11176  411 TLASLRNQVALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIA 490

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 498 IARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAKvSD 577
Cdd:PRK11176  491 IARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERGTHAELLA-QN 569

                         570
                  ....*....|
gi 1582666899 578 GLYARLNNLQ 587
Cdd:PRK11176  570 GVYAQLHKMQ 579

CydD

COG4988

ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...

36-572

2.94e-134

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: 403.37 E-value: 2.94e-134

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  36 VFAIACLIVVALSTAFTAWIMRAIIDEAFANR--RADVVWIICLsIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLY 113
Cdd:COG4988    20 ALAVLLGLLSGLLIIAQAWLLASLLAGLIIGGapLSALLPLLGL-LLAVLLLRALLAWLRERAAFRAAARVKRRLRRRLL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 114 AHLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAP--PLLYALr 191
Cdd:COG4988    99 EKLLALGPAWLRGKSTGELATLLTEGVEALDGYFARYLPQLFLAALVPLLILVAVFPLDWLSGLILLVTAPliPLFMIL- 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 192 yVSKRLRSATRE----AVHLNSHVLgamqETIQGIAIVKAFTMEEELERKVNKlikgaESRANRIA-----RLSERTSPL 262
Cdd:COG4988   178 -VGKGAAKASRRqwraLARLSGHFL----DRLRGLTTLKLFGRAKAEAERIAE-----ASEDFRKRtmkvlRVAFLSSAV 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 263 TESFAGFAVASVLAYAAYRSIYFNVPpgaFFSFVTALLLA---YDPARRL-----ARLQvqmerAVVNARMIYELLDmEP 334
Cdd:COG4988   248 LEFFASLSIALVAVYIGFRLLGGSLT---LFAALFVLLLApefFLPLRDLgsfyhARAN-----GIAAAEKIFALLD-AP 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 335 RQRDLPDARPLTVTQA-RIEFRNVSFAYGNES-VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDG 412
Cdd:COG4988   319 EPAAPAGTAPLPAAGPpSIELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILING 398

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 413 QDIAHITKKSLRQQLAYVSQQPYLFEGTIRDNIRYGRPEATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQ 492
Cdd:COG4988   399 VDLSDLDPASWRRQIAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAALPDGLDTPLGEGGRGLSGGQ 478

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 493 RQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETL 572
Cdd:COG4988   479 AQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQGTHEEL 558

ATM1

COG5265

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...

29-593

5.57e-131

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: 396.50 E-value: 5.57e-131

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  29 RDHLWGYVFAIACLIVVALS-TAFTAWIMRAIIDEAFANRRADVVWIICLSIFIAF-VLRGFAS-YGQA--VALSKVGND 103
Cdd:COG5265    29 PPYLRRRRRALAALLLLLLAaALALVVPPLLKDAIDALLSGAAALLVVPVGLLLAYgLLRLLSVlFGELrdALFARVTQR 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 104 IVARYQRRLYAHLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQ-DPLLSLAVFIM 182
Cdd:COG5265   109 AVRRLALEVFRHLHALSLRFHLERQTGGLSRDIERGTKGIEFLLRFLLFNILPTLLEIALVAGILLVKyDWWFALITLVT 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 183 AppLLYAL--RYVSKRLRSATREAVHLNSHVLGAM------QETiqgiaiVKAFTMEE-ELERKvnklikgAESRAN-RI 252
Cdd:COG5265   189 V--VLYIAftVVVTEWRTKFRREMNEADSEANTRAvdsllnYET------VKYFGNEArEARRY-------DEALARyER 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 253 ARLSERTSPLTESFA-----GFAVASVLAYAAYrsiyfNVPPGAF----FSFVTALLLA-YDPARRLARLQVQMERAVVN 322
Cdd:COG5265   254 AAVKSQTSLALLNFGqaliiALGLTAMMLMAAQ-----GVVAGTMtvgdFVLVNAYLIQlYIPLNFLGFVYREIRQALAD 328

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 323 ARMIYELLDMEPRQRDLPDARPLTVTQARIEFRNVSFAYGNES-VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFY 401
Cdd:COG5265   329 MERMFDLLDQPPEVADAPDAPPLVVGGGEVRFENVSFGYDPERpILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFY 408

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 402 DPREGEILIDGQDIAHITKKSLRQQLAYVSQQPYLFEGTIRDNIRYGRPEATDAEVEEAARLAYAHDFISAQPQGYETPV 481
Cdd:COG5265   409 DVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRV 488

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 482 GENGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQG 561
Cdd:COG5265   489 GERGLKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAG 568

                         570       580       590
                  ....*....|....*....|....*....|...
gi 1582666899 562 RVVEEGNHETL-AKvsDGLYARLNNLQRPSASD 593
Cdd:COG5265   569 RIVERGTHAELlAQ--GGLYAQMWARQQEEEEA 599

ABC_MTABC3_MDL1_MDL2

cd03249

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...

352-587

7.63e-126

Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 369.56 E-value: 7.63e-126

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAY---GNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLA 428
Cdd:cd03249     1 IEFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 429 YVSQQPYLFEGTIRDNIRYGRPEATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAPI 508
Cdd:cd03249    81 LVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPKI 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582666899 509 LLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAKvSDGLYARLNNLQ 587
Cdd:cd03249   161 LLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMA-QKGVYAKLVKAQ 238

ABCC_MsbA

cd03251

ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...

352-583

1.96e-122

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: 360.78 E-value: 1.96e-122

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNE--SVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAY 429
Cdd:cd03251     1 VEFKNVTFRYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 430 VSQQPYLFEGTIRDNIRYGRPEATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAPIL 509
Cdd:cd03251    81 VSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPPIL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1582666899 510 LLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAKvSDGLYARL 583
Cdd:cd03251   161 ILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLA-QGGVYAKL 233

ABCC_Glucan_exporter_like

cd03254

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...

350-572

2.47e-114

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: 339.97 E-value: 2.47e-114

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 350 ARIEFRNVSFAYGN-ESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLA 428
Cdd:cd03254     1 GEIEFENVNFSYDEkKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 429 YVSQQPYLFEGTIRDNIRYGRPEATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAPI 508
Cdd:cd03254    81 VVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKI 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1582666899 509 LLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETL 572
Cdd:cd03254   161 LILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDEL 224

ABCC_ATM1_transporter

cd03253

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...

352-587

6.95e-113

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: 336.51 E-value: 6.95e-113

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES-VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYV 430
Cdd:cd03253     1 IEFENVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 431 SQQPYLFEGTIRDNIRYGRPEATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAPILL 510
Cdd:cd03253    81 PQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582666899 511 LDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAKvSDGLYARLNNLQ 587
Cdd:cd03253   161 LDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLA-KGGLYAEMWKAQ 236

3a01208

TIGR00958

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

20-583

1.33e-109

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

Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 344.40 E-value: 1.33e-109

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  20 LKRIIAENGRDHLWgYVFAIACLIVVALSTAFTAWIMRAIIDEAFANRRADV----VWIICLSIFIAFVLRGF--ASYGQ 93
Cdd:TIGR00958 149 LFRLLGLSGRDWPW-LISAFVFLTLSSLGEMFIPFYTGRVIDTLGGDKGPPAlasaIFFMCLLSIASSVSAGLrgGSFNY 227

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  94 AVALskvgndIVARYQRRLYAHLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDP 173
Cdd:TIGR00958 228 TMAR------INLRIREDLFRSLLRQDLGFFDENKTGELTSRLSSDTQTMSRSLSLNVNVLLRNLVMLLGLLGFMLWLSP 301

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 174 LLSLAVFIMAPPLL-----YALRY--VSKRLRSATREAVHLNSHVLGAMQetiqgiaIVKAFTMEE-ELER---KVNKLI 242
Cdd:TIGR00958 302 RLTMVTLINLPLVFlaekvFGKRYqlLSEELQEAVAKANQVAEEALSGMR-------TVRSFAAEEgEASRfkeALEETL 374

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 243 KGAESRAnrIARLSERTSplTESFAGFAVASVLAYAAYRSIYFNVPPGAFFSFVTALLLAYDPARRLARLQVQMERAVVN 322
Cdd:TIGR00958 375 QLNKRKA--LAYAGYLWT--TSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGA 450

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 323 ARMIYELLDMEPRQrdlpdarPLTVTQA------RIEFRNVSFAYGNES---VLSGVSFTAEGGATTALVGPSGAGKSTV 393
Cdd:TIGR00958 451 SEKVFEYLDRKPNI-------PLTGTLAplnlegLIEFQDVSFSYPNRPdvpVLKGLTFTLHPGEVVALVGPSGSGKSTV 523

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 394 ISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYVSQQPYLFEGTIRDNIRYGRPEATDAEVEEAARLAYAHDFISAQ 473
Cdd:TIGR00958 524 AALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEF 603

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 474 PQGYETPVGENGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKalDEAMSGRTVVVIAHRLSTVVRAD 553
Cdd:TIGR00958 604 PNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERAD 681

                         570       580       590
                  ....*....|....*....|....*....|
gi 1582666899 554 KIVVMQQGRVVEEGNHETLAKvSDGLYARL 583
Cdd:TIGR00958 682 QILVLKKGSVVEMGTHKQLME-DQGCYKHL 710

CydC

COG4987

ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...

104-583

2.86e-105

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: 328.65 E-value: 2.86e-105

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 104 IVARYQRRLYAHLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMA 183
Cdd:COG4987    86 LLADLRVRLYRRLEPLAPAGLARLRSGDLLNRLVADVDALDNLYLRVLLPLLVALLVILAAVAFLAFFSPALALVLALGL 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 184 PPLLYALRYVSKRL-RSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSPL 262
Cdd:COG4987   166 LLAGLLLPLLAARLgRRAGRRLAAARAALRARLTDLLQGAAELAAYGALDRALARLDAAEARLAAAQRRLARLSALAQAL 245

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 263 TESFAGFAVASVLAYAAYRSIYFNVPPGAFFSFVTALLLAYDPARRLARLQVQMERAVVNARMIYELLDMEPRQRDLPDA 342
Cdd:COG4987   246 LQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARRLNELLDAPPAVTEPAEP 325

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 343 RPLTvTQARIEFRNVSFAYGNES--VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITK 420
Cdd:COG4987   326 APAP-GGPSLELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDE 404

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 421 KSLRQQLAYVSQQPYLFEGTIRDNIRYGRPEATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSIAR 500
Cdd:COG4987   405 DDLRRRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTWLGEGGRRLSGGERRRLALAR 484

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 501 ALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAKvSDGLY 580
Cdd:COG4987   485 ALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLEDGRIVEQGTHEELLA-QNGRY 563


                  ...
gi 1582666899 581 ARL 583
Cdd:COG4987   564 RQL 566

PRK13657

glucan ABC transporter ATP-binding protein/ permease;

291-583

5.89e-104

glucan ABC transporter ATP-binding protein/ permease;

Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 325.76 E-value: 5.89e-104

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 291 AFFSFVTALLLAYDPARRLARlQVQMERAVVnaRMIYELLDMEPRQRDLPDARPLTVTQARIEFRNVSFAYGNES-VLSG 369
Cdd:PRK13657  277 AFVGFATLLIGRLDQVVAFIN-QVFMAAPKL--EEFFEVEDAVPDVRDPPGAIDLGRVKGAVEFDDVSFSYDNSRqGVED 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 370 VSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYVSQQPYLFEGTIRDNIRYGR 449
Cdd:PRK13657  354 VSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDAGLFNRSIEDNIRVGR 433

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 450 PEATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKA 529
Cdd:PRK13657  434 PDATDEEMRAAAERAQAHDFIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAA 513

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1582666899 530 LDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAKvSDGLYARL 583
Cdd:PRK13657  514 LDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESGSFDELVA-RGGRFAAL 566

CydD

TIGR02857

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...

31-558

1.54e-99

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: 312.68 E-value: 1.54e-99

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  31 HLWGYVFAIACLIVVALSTAFTAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQR 110
Cdd:TIGR02857   2 RRALALLALLGVLGALLIIAQAWLLARVVDGLISAGEPLAELLPALGALALVLLLRALLGWLQERAAARAAAAVKSQLRE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 111 RLYAHLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAP--PLLY 188
Cdd:TIGR02857  82 RLLEAVAALGPRWLQGRPSGELATLALEGVEALDGYFARYLPQLVLAVIVPLAILAAVFPQDWISGLILLLTAPliPIFM 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 189 ALryVSKRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSPLTESFAG 268
Cdd:TIGR02857 162 IL--IGWAAQAAARKQWAALSRLSGHFLDRLRGLPTLKLFGRAKAQAAAIRRSSEEYRERTMRVLRIAFLSSAVLELFAT 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 269 FAVASVLAYAAYRSIYFNVPpgaFFSFVTALLLA---YDPARRLARLQVQMERAVVNARMIYELLDMEPR----QRDLPD 341
Cdd:TIGR02857 240 LSVALVAVYIGFRLLAGDLD---LATGLFVLLLApefYLPLRQLGAQYHARADGVAAAEALFAVLDAAPRplagKAPVTA 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 342 ARPLTvtqarIEFRNVSFAY-GNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITK 420
Cdd:TIGR02857 317 APASS-----LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA 391

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 421 KSLRQQLAYVSQQPYLFEGTIRDNIRYGRPEATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSIAR 500
Cdd:TIGR02857 392 DSWRDQIAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALAR 471

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1582666899 501 ALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVM 558
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALADRIVVL 529

type_I_sec_HlyB

TIGR01846

type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...

59-587

2.14e-99

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

Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 317.07 E-value: 2.14e-99

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  59 IIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYAHLMTLSVGFFSEARSAHIAAQVSQ 138
Cdd:TIGR01846 165 VIDKVLVHRGLSTLSVLALAMLAVAIFEPALGGLRTYLFAHLTSRIDVELGARLYRHLLGLPLGYFESRRVGDTVARVRE 244

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 139 nVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYVSKRLRSATREAVHLNSHVLGAMQET 218
Cdd:TIGR01846 245 -LEQIRNFLTGSALTVVLDLLFVVVFLAVMFFYSPTLTGVVIGSLVCYALLSVFVGPILRKRVEDKFERSAAATSFLVES 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 219 IQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSPLTESFAGFAVASVLAYAAYRSIYFNVPPGAFFSFVTA 298
Cdd:TIGR01846 324 VTGIETIKATATEPQFQNRWDRQLAAYVAASFRVTNLGNIAGQAIELIQKLTFAILLWFGAHLVIGGALSPGQLVAFNML 403

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 299 LLLAYDPARRLARLQVQMERAVVNARMIYELLDmEPRQRDLPDARPLTVTQARIEFRNVSFAYGNES--VLSGVSFTAEG 376
Cdd:TIGR01846 404 AGRVTQPVLRLAQLWQDFQQTGIALERLGDILN-SPTEPRSAGLAALPELRGAITFENIRFRYAPDSpeVLSNLNLDIKP 482

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 377 GATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYVSQQPYLFEGTIRDNIRYGRPEATDAE 456
Cdd:TIGR01846 483 GEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQENVLFSRSIRDNIALCNPGAPFEH 562

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 457 VEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSG 536
Cdd:TIGR01846 563 VIHAAKLAGAHDFISELPQGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICRG 642

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1582666899 537 RTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAKvSDGLYARLNNLQ 587
Cdd:TIGR01846 643 RTVIIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLA-LQGLYARLWQQQ 692

NHLM_micro_ABC1

TIGR03796

NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...

36-583

4.14e-94

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: 303.79 E-value: 4.14e-94

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  36 VFAIACLIVVALST-AFTawimRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYA 114
Cdd:TIGR03796 160 LLAGLLLVLPGLVIpAFS----QIFVDEILVQGRQDWLRPLLLGMGLTALLQGVLTWLQLYYLRRLEIKLAVGMSARFLW 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 115 HLMTLSVGFFSEARSAHIAAQVSQNVSgIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYVS 194
Cdd:TIGR03796 236 HILRLPVRFFAQRHAGDIASRVQLNDQ-VAEFLSGQLATTALDAVMLVFYALLMLLYDPVLTLIGIAFAAINVLALQLVS 314

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 195 KRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKvnklIKGAESRA----NRIARLSERTSPLTESFAGFA 270
Cdd:TIGR03796 315 RRRVDANRRLQQDAGKLTGVAISGLQSIETLKASGLESDFFSR----WAGYQAKLlnaqQELGVLTQILGVLPTLLTSLN 390

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 271 VASVLAYAAYRSIYFNVPPGAFFSFVTALLLAYDP-------ARRLARLQVQMERA--VVNARMIYELLDmepRQRDLPD 341
Cdd:TIGR03796 391 SALILVVGGLRVMEGQLTIGMLVAFQSLMSSFLEPvnnlvgfGGTLQELEGDLNRLddVLRNPVDPLLEE---PEGSAAT 467

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 342 ARPLTVTQARIEFRNVSFAYG--NESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHIT 419
Cdd:TIGR03796 468 SEPPRRLSGYVELRNITFGYSplEPPLIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIP 547

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 420 KKSLRQQLAYVSQQPYLFEGTIRDNIRYGRPEATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSIA 499
Cdd:TIGR03796 548 REVLANSVAMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHDVITSRPGGYDAELAEGGANLSGGQRQRLEIA 627

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 500 RALVRNAPILLLDEATSALDTESEaavqKALDEAMSGR--TVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAKVsD 577
Cdd:TIGR03796 628 RALVRNPSILILDEATSALDPETE----KIIDDNLRRRgcTCIIVAHRLSTIRDCDEIIVLERGKVVQRGTHEELWAV-G 702


                  ....*.
gi 1582666899 578 GLYARL 583
Cdd:TIGR03796 703 GAYARL 708

ABC_6TM_MsbA_like

cd18552

Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; ...

35-326

2.11e-93

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: 288.55 E-value: 2.11e-93

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  35 YVFAIACLIVVALSTAFTAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYA 114
Cdd:cd18552     1 LALAILGMILVAATTAALAWLLKPLLDDIFVEKDLEALLLVPLAIIGLFLLRGLASYLQTYLMAYVGQRVVRDLRNDLFD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 115 HLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYVS 194
Cdd:cd18552    81 KLLRLPLSFFDRNSSGDLISRITNDVNQVQNALTSALTVLVRDPLTVIGLLGVLFYLDWKLTLIALVVLPLAALPIRRIG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 195 KRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSPLTESFAGFAVASV 274
Cdd:cd18552   161 KRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANERLRRLSMKIARARALSSPLMELLGAIAIALV 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1582666899 275 LAYAAYRSIYFNVPPGAFFSFVTALLLAYDPARRLARLQVQMERAVVNARMI 326
Cdd:cd18552   241 LWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAERI 292

ABCC_Hemolysin

cd03252

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...

352-587

2.05e-88

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.

Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 273.59 E-value: 2.05e-88

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES--VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAY 429
Cdd:cd03252     1 ITFEHVRFRYKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 430 VSQQPYLFEGTIRDNIRYGRPEATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAPIL 509
Cdd:cd03252    81 VLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1582666899 510 LLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAKvSDGLYARLNNLQ 587
Cdd:cd03252   161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLA-ENGLYAYLYQLQ 237

ABCC_MRP_Like

cd03228

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...

352-562

3.70e-88

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 270.41 E-value: 3.70e-88

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES--VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAY 429
Cdd:cd03228     1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 430 VSQQPYLFEGTIRDNIrygrpeatdaeveeaarlayahdfisaqpqgyetpvgengvtLSGGQRQRLSIARALVRNAPIL 509
Cdd:cd03228    81 VPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPPIL 118

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 510 LLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGR 562
Cdd:cd03228   119 ILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171

ABCC_TAP

cd03248

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...

344-563

3.66e-86

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: 267.41 E-value: 3.66e-86

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 344 PLTVtQARIEFRNVSFAYGNES---VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITK 420
Cdd:cd03248     5 PDHL-KGIVKFQNVTFAYPTRPdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 421 KSLRQQLAYVSQQPYLFEGTIRDNIRYGRPEATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSIAR 500
Cdd:cd03248    84 KYLHSKVSLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIAR 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 501 ALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRV 563
Cdd:cd03248   164 ALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226

bacteriocin_ABC

TIGR01193

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...

38-583

2.97e-80

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: 266.99 E-value: 2.97e-80

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  38 AIACLIVVALSTAfTAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGN----DIVARYQRrly 113
Cdd:TIGR01193 162 VIAAIIVTLISIA-GSYYLQKIIDTYIPHKMMGTLGIISIGLIIAYIIQQILSYIQIFLLNVLGQrlsiDIILSYIK--- 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 114 aHLMTLSVGFFSEARSAHIAAQVSqNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPP---LLYAL 190
Cdd:TIGR01193 238 -HLFELPMSFFSTRRTGEIVSRFT-DASSIIDALASTILSLFLDMWILVIVGLFLVRQNMLLFLLSLLSIPVyavIIILF 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 191 RYVSKRLRSATREAvhlNSHVLGAMQETIQGIAIVKAFTMEEELERKV--------NKLIKGAESRANRIARLSERTSPL 262
Cdd:TIGR01193 316 KRTFNKLNHDAMQA---NAVLNSSIIEDLNGIETIKSLTSEAERYSKIdsefgdylNKSFKYQKADQGQQAIKAVTKLIL 392

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 263 TesfagfavASVLAYAAYRSIYFNVPPGAFFSFvtALLLAY--DPARRLARLQVQMERA-VVNARM--IYeLLDMEPRQR 337
Cdd:TIGR01193 393 N--------VVILWTGAYLVMRGKLTLGQLITF--NALLSYflTPLENIINLQPKLQAArVANNRLneVY-LVDSEFINK 461

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 338 DLPDArpLTVTQARIEFRNVSFAYG-NESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIA 416
Cdd:TIGR01193 462 KKRTE--LNNLNGDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLK 539

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 417 HITKKSLRQQLAYVSQQPYLFEGTIRDNIRYG-RPEATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQR 495
Cdd:TIGR01193 540 DIDRHTLRQFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQR 619

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 496 LSIARALVRNAPILLLDEATSALDTESEAAVQKALdEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAKv 575
Cdd:TIGR01193 620 IALARALLTDSKVLILDESTSNLDTITEKKIVNNL-LNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLD- 697


                  ....*...
gi 1582666899 576 SDGLYARL 583
Cdd:TIGR01193 698 RNGFYASL 705

chvA

TIGR01192

glucan exporter ATP-binding protein; This model describes glucan exporter ATP binding protein ...

158-583

5.15e-80

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: 263.29 E-value: 5.15e-80

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 158 LLTFVSL---LAVMILQDPLLSLAVFIMAPPLLYALRYVSKRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEEL 234
Cdd:TIGR01192 138 LATFVALfllIPTAFAMDWRLSIVLMVLGILYILIAKLVMQRTKNGQAAVEHHYHNVFKHVSDSISNVSVVHSYNRIEAE 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 235 ERKVNKLIKGAESRANRIARLSERTSPLTESFAGFAVASVLAYAAYRSIYFNVPPGAFFSFV--TALLLAydparRLARL 312
Cdd:TIGR01192 218 TSALKQFTNNLLSAQYPVLDWWALASGLNRMASTISMMCILVIGTVLVIKGELSVGEVIAFIgfANLLIG-----RLDQM 292

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 313 QVQMERAVVNARMIYELLDMEP--RQRDLP-DARPLTVTQARIEFRNVSFAYGNESV-LSGVSFTAEGGATTALVGPSGA 388
Cdd:TIGR01192 293 SGFITQIFEARAKLEDFFDLEDsvFQREEPaDAPELPNVKGAVEFRHITFEFANSSQgVFDVSFEAKAGQTVAIVGPTGA 372

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 389 GKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYVSQQPYLFEGTIRDNIRYGRPEATDAEVEEAARLAYAHD 468
Cdd:TIGR01192 373 GKTTLINLLQRVYDPTVGQILIDGIDINTVTRESLRKSIATVFQDAGLFNRSIRENIRLGREGATDEEVYEAAKAAAAHD 452

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 469 FISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLST 548
Cdd:TIGR01192 453 FILKRSNGYDTLVGERGNRLSGGERQRLAIARAILKNAPILVLDEATSALDVETEARVKNAIDALRKNRTTFIIAHRLST 532

                         410       420       430
                  ....*....|....*....|....*....|....*
gi 1582666899 549 VVRADKIVVMQQGRVVEEGNHETLAKvSDGLYARL 583
Cdd:TIGR01192 533 VRNADLVLFLDQGRLIEKGSFQELIQ-KDGRFYKL 566

ABCC_bacteriocin_exporters

cd03245

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...

351-567

1.57e-79

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.

Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 249.81 E-value: 1.57e-79

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 351 RIEFRNVSFAYGNE--SVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLA 428
Cdd:cd03245     2 RIEFRNVSFSYPNQeiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 429 YVSQQPYLFEGTIRDNIRYGRPEATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAPI 508
Cdd:cd03245    82 YVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLNDPPI 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1582666899 509 LLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEG 567
Cdd:cd03245   162 LLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220

ABCC_MRP_domain2

cd03244

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...

351-568

1.03e-77

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: 245.10 E-value: 1.03e-77

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 351 RIEFRNVSFAYGNES--VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLA 428
Cdd:cd03244     2 DIEFKNVSLRYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRIS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 429 YVSQQPYLFEGTIRDNIRygrP--EATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNA 506
Cdd:cd03244    82 IIPQDPVLFSGTIRSNLD---PfgEYSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1582666899 507 PILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGN 568
Cdd:cd03244   159 KILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220

NHLM_micro_ABC2

TIGR03797

NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...

19-583

1.55e-76

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: 256.42 E-value: 1.55e-76

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  19 ILKRIIAENGRDHLWgyvFAIACLIVVALSTAfTAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALS 98
Cdd:TIGR03797 126 LLRFALRGARRDLLA---ILAMGLLGTLLGML-VPIATGILIGTAIPDADRSLLVQIALALLAAAVGAAAFQLAQSLAVL 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  99 KVGNDIVARYQRRLYAHLMTLSVGFFSEARSAHIAAQVSqNVSGIRDVLNltiTSTVRDLLT-FVSL--LAVMILQDPLL 175
Cdd:TIGR03797 202 RLETRMDASLQAAVWDRLLRLPVSFFRQYSTGDLASRAM-GISQIRRILS---GSTLTTLLSgIFALlnLGLMFYYSWKL 277

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 176 SLAVFIMAPPLLYALRYVSKRLRSATREAVHLNSHVLGAMQETIQGIAivkaftmeeelerkvnKL-IKGAESRA----- 249
Cdd:TIGR03797 278 ALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGIS----------------KLrVAGAENRAfarwa 341

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 250 ------NRIARLSER----TSPLTESFAGFAVASVLAYAAYRSIYFNVPPGAFFSFVTALLLAYDPARRLARLQVqmerA 319
Cdd:TIGR03797 342 klfsrqRKLELSAQRienlLTVFNAVLPVLTSAALFAAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLI----S 417

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 320 VVNARMIYE----LLDMEPRQR-DLPDARPLTvtqARIEFRNVSFAYGNES--VLSGVSFTAEGGATTALVGPSGAGKST 392
Cdd:TIGR03797 418 ILAVIPLWErakpILEALPEVDeAKTDPGKLS---GAIEVDRVTFRYRPDGplILDDVSLQIEPGEFVAIVGPSGSGKST 494

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 393 VISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYVSQQPYLFEGTIRDNIRYGRPEATDaEVEEAARLAYAHDFISA 472
Cdd:TIGR03797 495 LLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQLGVVLQNGRLMSGSIFENIAGGAPLTLD-EAWEAARMAGLAEDIRA 573

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 473 QPQGYETPVGENGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALdEAMSGrTVVVIAHRLSTVVRA 552
Cdd:TIGR03797 574 MPMGMHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESL-ERLKV-TRIVIAHRLSTIRNA 651

                         570       580       590
                  ....*....|....*....|....*....|.
gi 1582666899 553 DKIVVMQQGRVVEEGNHETLAKVsDGLYARL 583
Cdd:TIGR03797 652 DRIYVLDAGRVVQQGTYDELMAR-EGLFAQL 681

PRK10789

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

39-580

1.71e-76

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

Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 253.48 E-value: 1.71e-76

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  39 IACLIVVALSTAFTAWIMRAIID----EAFANRRAdVVWI--ICLSIFIAFVLRGF-------ASYGQAVALskvgndiv 105
Cdd:PRK10789    1 VALLIIIAMLQLIPPKVVGIIVDgvteQHMTTGQI-LMWIgtMVLIAVVVYLLRYVwrvllfgASYQLAVEL-------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 106 aryQRRLYAHLMTLSVGFFSEARSAHIAAQVSQNVSGI-----RDVLNLtitstVRDLLTFVSLLAVMILQdplLS--LA 178
Cdd:PRK10789   72 ---REDFYRQLSRQHPEFYLRHRTGDLMARATNDVDRVvfaagEGVLTL-----VDSLVMGCAVLIVMSTQ---ISwqLT 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 179 VFIMAPPLLYAL---RY---VSKRLRSATREAVHLNSHVlgamQETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRI 252
Cdd:PRK10789  141 LLALLPMPVMAImikRYgdqLHERFKLAQAAFSSLNDRT----QESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRV 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 253 ARLSERTSPLTesFAGFAVASVLAYA--AYRSIYFNVPPGAFFSFVTALLLAYDPARRLARLQVQMERAVVNARMIYELL 330
Cdd:PRK10789  217 ARIDARFDPTI--YIAIGMANLLAIGggSWMVVNGSLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAML 294

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 331 DMEPRQRDLPDARPLTVTQARIEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILI 410
Cdd:PRK10789  295 AEAPVVKDGSEPVPEGRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRF 374

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 411 DGQDIAHITKKSLRQQLAYVSQQPYLFEGTIRDNIRYGRPEATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSG 490
Cdd:PRK10789  375 HDIPLTKLQLDSWRSRLAVVSQTPFLFSDTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSG 454

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 491 GQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHE 570
Cdd:PRK10789  455 GQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHD 534

                         570
                  ....*....|
gi 1582666899 571 TLAKVSdGLY 580
Cdd:PRK10789  535 QLAQQS-GWY 543

ArpD

COG4618

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...

79-567

9.77e-74

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: 245.81 E-value: 9.77e-74

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  79 IFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYAHLMTLSVgffseARSAHIAAQvsqnvsGIRDVlnltitSTVRDL 158
Cdd:COG4618    66 ALGLYAVMGLLDAVRSRILVRVGARLDRRLGPRVFDAAFRAAL-----RGGGGAAAQ------ALRDL------DTLRQF 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 159 LTFVSLLAVMilqD----PLLSLAVFIMAPPL----------LYALRYVSKRL-RSATREAVHLNSHVLGAMQETIQGIA 223
Cdd:COG4618   129 LTGPGLFALF---DlpwaPIFLAVLFLFHPLLgllalvgalvLVALALLNERLtRKPLKEANEAAIRANAFAEAALRNAE 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 224 IVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSPLTESFAGFAVASVLAYAAYRSIYFNVPPGAFF--SFVTALLL 301
Cdd:COG4618   206 VIEAMGMLPALRRRWQRANARALALQARASDRAGGFSALSKFLRLLLQSAVLGLGAYLVIQGEITPGAMIaaSILMGRAL 285

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 302 AydPARRLarlqVQMERAVVNARMIY----ELLDMEPRQrdlPDARPLTVTQARIEFRNVSFAY--GNESVLSGVSFTAE 375
Cdd:COG4618   286 A--PIEQA----IGGWKQFVSARQAYrrlnELLAAVPAE---PERMPLPRPKGRLSVENLTVVPpgSKRPILRGVSFSLE 356

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 376 GGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYVSQQPYLFEGTIRDNI-RYGrpEATD 454
Cdd:COG4618   357 PGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDGTIAENIaRFG--DADP 434

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 455 AEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEA- 533
Cdd:COG4618   435 EKVVAAAKLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALk 514

                         490       500       510
                  ....*....|....*....|....*....|....
gi 1582666899 534 MSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEG 567
Cdd:COG4618   515 ARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFG 548

PRK11174

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

251-583

3.06e-71

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

Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 240.13 E-value: 3.06e-71

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 251 RIARLSertSPLTESFAGFAVAsVLAyaayrsIYFNvppgafFSF------------VT------ALLLA---YDPARRL 309
Cdd:PRK11174  244 RMAFLS---SAVLEFFASISIA-LVA------VYFG------FSYlgelnfghygtgVTlfagffVLILApefYQPLRDL 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 310 -----ARLQvqmerAVVNARMIYELLDMEPRQ-----RDLPDARPLTvtqarIEFRNVSFAYGNESVLSG-VSFTAEGGA 378
Cdd:PRK11174  308 gtfyhAKAQ-----AVGAAESLVTFLETPLAHpqqgeKELASNDPVT-----IEAEDLEILSPDGKTLAGpLNFTLPAGQ 377

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 379 TTALVGPSGAGKSTVISLIPRFYdPREGEILIDGQDIAHITKKSLRQQLAYVSQQPYLFEGTIRDNIRYGRPEATDAEVE 458
Cdd:PRK11174  378 RIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLRDNVLLGNPDASDEQLQ 456

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 459 EAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRT 538
Cdd:PRK11174  457 QALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQT 536

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1582666899 539 VVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAKvSDGLYARL 583
Cdd:PRK11174  537 TLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQ-AGGLFATL 580

PRK11160

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

104-583

1.12e-67

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

Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 230.10 E-value: 1.12e-67

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 104 IVARYQRRLYAH------LMTLSVGFFSEarsahIAAQVSQNVSGIR--DVLNL--------------TITSTVRDLLTF 161
Cdd:PRK11160   74 TAGRYGERLVSHdatfrvLTHLRVFTFSK-----LLPLSPAGLARYRqgDLLNRlvadvdtldhlylrLISPLVAALVVI 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 162 VSLLAVMILQDPLLSLAVFIMAPPLLYALRYVSKRL-RSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKVNK 240
Cdd:PRK11160  149 LVLTIGLSFFDLTLALTLGGILLLLLLLLPLLFYRLgKKPGQDLTHLRAQYRVQLTEWLQGQAELTLFGAEDRYRQQLEQ 228

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 241 LIKGAESRANRIARLSERTSPLTESFAGFAVASVLAYAAyRSIYFNVPPGAFFS-FVTALLLAYDPARRLARLQVQMERA 319
Cdd:PRK11160  229 TEQQWLAAQRRQANLTGLSQALMILANGLTVVLMLWLAA-GGVGGNAQPGALIAlFVFAALAAFEALMPVAGAFQHLGQV 307

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 320 VVNARMIYELLDMEPrQRDLPDARPLTVTQARIEFRNVSFAY--GNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLI 397
Cdd:PRK11160  308 IASARRINEITEQKP-EVTFPTTSTAAADQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLL 386

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 398 PRFYDPREGEILIDGQDIAHITKKSLRQQLAYVSQQPYLFEGTIRDNIRYGRPEATDAEVEEAAR---LAYAHDfisaQP 474
Cdd:PRK11160  387 TRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLFSATLRDNLLLAAPNASDEALIEVLQqvgLEKLLE----DD 462

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 475 QGYETPVGENGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADK 554
Cdd:PRK11160  463 KGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQFDR 542

                         490       500
                  ....*....|....*....|....*....
gi 1582666899 555 IVVMQQGRVVEEGNHETLAKvSDGLYARL 583
Cdd:PRK11160  543 ICVMDNGQIIEQGTHQELLA-QQGRYYQL 570

PRK10790

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

290-588

1.35e-65

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

Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 224.98 E-value: 1.35e-65

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 290 GAFFSFVTALLLAYDPARRLARLQVQMERAVVNARMIYELLDmEPRQRDLPDARPLTvtQARIEFRNVSFAYGNE-SVLS 368
Cdd:PRK10790  282 GVLYAFISYLGRLNEPLIELTTQQSMLQQAVVAGERVFELMD-GPRQQYGNDDRPLQ--SGRIDIDNVSFAYRDDnLVLQ 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 369 GVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYVSQQPYLFEGTIRDNIRYG 448
Cdd:PRK10790  359 NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDPVVLADTFLANVTLG 438

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 449 RPEATDA--EVEEAARLAyahDFISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAV 526
Cdd:PRK10790  439 RDISEEQvwQALETVQLA---ELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAI 515

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1582666899 527 QKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAkVSDGLYARLNNLQR 588
Cdd:PRK10790  516 QQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLL-AAQGRYWQMYQLQL 576

CydC

TIGR02868

thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...

84-546

2.55e-65

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: 222.62 E-value: 2.55e-65

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  84 VLRGFASYGQAVALSKVGNDIVARYQRRLYAHLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVS 163
Cdd:TIGR02868  64 IGRAVFRYLERLVGHDAALRSLGALRVRVYERLARQALAGRRRLRRGDLLGRLGADVDALQDLYVRVIVPAGVALVVGAA 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 164 LLAVMILQDP------LLSLAVFIMAPPLLYALRyvskrLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERK 237
Cdd:TIGR02868 144 AVAAIAVLSVpaalilAAGLLLAGFVAPLVSLRA-----ARAAEQALARLRGELAAQLTDALDGAAELVASGALPAALAQ 218

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 238 V---NKLIKGAESRANRIARLSERTSPLtesFAGFAVASVLAYAAYRSIYFNVPPGAFFSFVTALLLAYDPARRLARLQV 314
Cdd:TIGR02868 219 VeeaDRELTRAERRAAAATALGAALTLL---AAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQ 295

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 315 QMERAVVNARMIYELLDMEPRQRD--LPDARPLTVTQARIEFRNVSFAY-GNESVLSGVSFTAEGGATTALVGPSGAGKS 391
Cdd:TIGR02868 296 QLTRVRAAAERIVEVLDAAGPVAEgsAPAAGAVGLGKPTLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKS 375

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 392 TVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYVSQQPYLFEGTIRDNIRYGRPEATDAEVEEAARLAYAHDFIS 471
Cdd:TIGR02868 376 TLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLR 455

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582666899 472 AQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRL 546
Cdd:TIGR02868 456 ALPDGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530

ABC_6TM_exporters

cd07346

Six-transmembrane helical domain of the ATP-binding cassette transporters; This family ...

36-323

2.46e-56

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: 191.61 E-value: 2.46e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  36 VFAIACLIVVALSTAFTAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYAH 115
Cdd:cd07346     2 LLALLLLLLATALGLALPLLTKLLIDDVIPAGDLSLLLWIALLLLLLALLRALLSYLRRYLAARLGQRVVFDLRRDLFRH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 116 LMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYVSK 195
Cdd:cd07346    82 LQRLSLSFFDRNRTGDLMSRLTSDVDAVQNLVSSGLLQLLSDVLTLIGALVILFYLNWKLTLVALLLLPLYVLILRYFRR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 196 RLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSPLTESFAGFAVASVL 275
Cdd:cd07346   162 RIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANLRAARLSALFSPLIGLLTALGTALVL 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1582666899 276 AYAAYRSIYFNVPPGAFFSFVTALLLAYDPARRLARLQVQMERAVVNA 323
Cdd:cd07346   242 LYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASL 289

ABCC_NFT1

cd03369

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...

351-567

6.27e-56

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: 187.62 E-value: 6.27e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 351 RIEFRNVSFAYGNE--SVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLA 428
Cdd:cd03369     6 EIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 429 YVSQQPYLFEGTIRDNI-RYGrpEATDAEVEEAARlayahdfisaqpqgyetpVGENGVTLSGGQRQRLSIARALVRNAP 507
Cdd:cd03369    86 IIPQDPTLFSGTIRSNLdPFD--EYSDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALLKRPR 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 508 ILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEG 567
Cdd:cd03369   146 VLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205

MRP_assoc_pro

TIGR00957

multi drug resistance-associated protein (MRP); This model describes multi drug ...

36-567

8.74e-55

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: 201.33 E-value: 8.74e-55

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899   36 VFAIACLIVVALSTAF--TAWIMRAIIDEAFANRRadvvwiICLSIFIAF-VLRGFASYGQAVALSKVGNDIVARYQRRL 112
Cdd:TIGR00957  971 IFLFVCNHVSALASNYwlSLWTDDPMVNGTQNNTS------LRLSVYGALgILQGFAVFGYSMAVSIGGIQASRVLHQDL 1044

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  113 YAHLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLslAVFIMAPPLLYALR- 191
Cdd:TIGR00957 1045 LHNKLRSPMSFFERTPSGNLVNRFSKELDTVDSMIPPVIKMFMGSLFNVIGALIVILLATPIA--AVIIPPLGLLYFFVq 1122

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  192 --YVS-----KRLRSATREAVHlnSHvlgaMQETIQGIAIVKAFTMEEELERkVNKLIKGAESRANRIARLSERTSPLTE 264
Cdd:TIGR00957 1123 rfYVAssrqlKRLESVSRSPVY--SH----FNETLLGVSVIRAFEEQERFIH-QSDLKVDENQKAYYPSIVANRWLAVRL 1195

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  265 SFAGFAVasVLAYAAYRSI-YFNVPPGAFFSFVTALLLAYDPARRLARLQVQMERAVVNARMIYELLDME---PRQrdLP 340
Cdd:TIGR00957 1196 ECVGNCI--VLFAALFAVIsRHSLSAGLVGLSVSYSLQVTFYLNWLVRMSSEMETNIVAVERLKEYSETEkeaPWQ--IQ 1271

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  341 DARPLTV--TQARIEFRNVSFAY--GNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIA 416
Cdd:TIGR00957 1272 ETAPPSGwpPRGRVEFRNYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIA 1351

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  417 HITKKSLRQQLAYVSQQPYLFEGTIRDNIR-YGrpEATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQR 495
Cdd:TIGR00957 1352 KIGLHDLRFKITIIPQDPVLFSGSLRMNLDpFS--QYSDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQL 1429

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1582666899  496 LSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEG 567
Cdd:TIGR00957 1430 VCLARALLRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFG 1501

type_I_sec_PrtD

TIGR01842

type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...

42-563

1.50e-54

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

Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 194.10 E-value: 1.50e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  42 LIVVALSTAF-------TAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYA 114
Cdd:TIGR01842   8 FIIVGLFSFVinilmlaPPLYMLQVYDRVLTSGSVPTLLMLTVLALGLYLFLGLLDALRSFVLVRIGEKLDGALNQPIFA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 115 HLMTLSVgffseARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPpLLYALRYVS 194
Cdd:TIGR01842  88 ASFSATL-----RRGSGDGLQALRDLDQLRQFLTGPGLFAFFDAPWMPIYLLVCFLLHPWIGILALGGAV-VLVGLALLN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 195 KRL-RSATREAVHLNS---HVLGAMQETIQgiaIVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSPLTESFAGFA 270
Cdd:TIGR01842 162 NRAtKKPLKEATEASIranNLADSALRNAE---VIEAMGMMGNLTKRWGRFHSKYLSAQSAASDRAGMLSNLSKYFRIVL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 271 VASVLAYAAYRSIYFNVPPGAFF--SFVTALLLAydPARRLARLQVQMERAVVNARMIYELLDMEPRQrdlPDARPLTVT 348
Cdd:TIGR01842 239 QSLVLGLGAYLAIDGEITPGMMIagSILVGRALA--PIDGAIGGWKQFSGARQAYKRLNELLANYPSR---DPAMPLPEP 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 349 QARIEFRNVSFAY--GNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQ 426
Cdd:TIGR01842 314 EGHLSVENVTIVPpgGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKH 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 427 LAYVSQQPYLFEGTIRDNI-RYGRpEATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRN 505
Cdd:TIGR01842 394 IGYLPQDVELFPGTVAENIaRFGE-NADPEKIIEAAKLAGVHELILRLPDGYDTVIGPGGATLSGGQRQRIALARALYGD 472

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1582666899 506 APILLLDEATSALDTESEAAVQKALDEA-MSGRTVVVIAHRLSTVVRADKIVVMQQGRV 563
Cdd:TIGR01842 473 PKLVVLDEPNSNLDEEGEQALANAIKALkARGITVVVITHRPSLLGCVDKILVLQDGRI 531

ABC_PstB_phosphate_transporter

cd03260

ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...

352-572

2.85e-54

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: 183.92 E-value: 2.85e-54

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYD-----PREGEILIDGQDIAHITKK--SLR 424
Cdd:cd03260     1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLDVDvlELR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 425 QQLAYVSQQPYLFEGTIRDNIRYG-------RPEATDAEVEEAARLAYAHDFISAQPQGYEtpvgengvtLSGGQRQRLS 497
Cdd:cd03260    81 RRVGMVFQKPNPFPGSIYDNVAYGlrlhgikLKEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQQRLC 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582666899 498 IARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHETL 572
Cdd:cd03260   152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARvADRTAFLLNGRLVEFGPTEQI 227

PTZ00265

multidrug resistance protein (mdr1); Provisional

62-588

6.47e-54

multidrug resistance protein (mdr1); Provisional

Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 198.71 E-value: 6.47e-54

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899   62 EAFANRRADVVWIICLSIFIAFVLRGFASygqavalSKVGNDIVARYQRRLYAHLMTLSVGFFSEarSAHIAAQVSQNVS 141
Cdd:PTZ00265   862 EANSNKYSLYILVIAIAMFISETLKNYYN-------NVIGEKVEKTMKRRLFENILYQEISFFDQ--DKHAPGLLSAHIN 932

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  142 giRDVlNLTITSTVRDLLTFVSLLaVMILQDPLLSLAVFIMAPPLLYALRYVSKRLrSATREAVHLNSHVlgaMQETIQG 221
Cdd:PTZ00265   933 --RDV-HLLKTGLVNNIVIFTHFI-VLFLVSMVMSFYFCPIVAAVLTGTYFIFMRV-FAIRARLTANKDV---EKKEINQ 1004

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  222 IAIVKAFTMEEELERKVNKLIKGAESRANRIA--------------------RLSERTSPLTESFAGFAVASVLAYAAYR 281
Cdd:PTZ00265  1005 PGTVFAYNSDDEIFKDPSFLIQEAFYNMNTVIiygledyfcnliekaidysnKGQKRKTLVNSMLWGFSQSAQLFINSFA 1084

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  282 SIY--FNVPPGA-----FFSFVTALLLAYDPARRLARLQVQMERAVVNARMIYELLdMEPRQRDLPDARPLTVT-----Q 349
Cdd:PTZ00265  1085 YWFgsFLIRRGTilvddFMKSLFTFLFTGSYAGKLMSLKGDSENAKLSFEKYYPLI-IRKSNIDVRDNGGIRIKnkndiK 1163

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  350 ARIEFRNVSFAY---GNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPR---------------------- 404
Cdd:PTZ00265  1164 GKIEIMDVNFRYisrPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKndhhivfknehtndmtneqdyq 1243

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  405 --------------------------------EGEILIDGQDIAHITKKSLRQQLAYVSQQPYLFEGTIRDNIRYGRPEA 452
Cdd:PTZ00265  1244 gdeeqnvgmknvnefsltkeggsgedstvfknSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDA 1323

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  453 TDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKAL-- 530
Cdd:PTZ00265  1324 TREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIvd 1403

                          570       580       590       600       610       620
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582666899  531 --DEAmsGRTVVVIAHRLSTVVRADKIVVM----QQGRVVE-EGNHETLAKVSDGLYARLNNLQR 588
Cdd:PTZ00265  1404 ikDKA--DKTIITIAHRIASIKRSDKIVVFnnpdRTGSFVQaHGTHEELLSVQDGVYKKYVKLAK 1466

FetA

COG4619

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

352-563

3.34e-52

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

Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 177.70 E-value: 3.34e-52

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYVS 431
Cdd:COG4619     1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYLFEGTIRDNIRY-----GRPEATDAEVEEAARLAYAHDFIsaqpqgyETPVGEngvtLSGGQRQRLSIARALVRNA 506
Cdd:COG4619    81 QEPALWGGTVRDNLPFpfqlrERKFDRERALELLERLGLPPDIL-------DKPVER----LSGGERQRLALIRALLLQP 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582666899 507 PILLLDEATSALDTESEAAVQKALDE--AMSGRTVVVIAH------RLstvvrADKIVVMQQGRV 563
Cdd:COG4619   150 DVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHdpeqieRV-----ADRVLTLEAGRL 209

FepC

COG1120

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...

351-575

6.03e-52

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: 178.70 E-value: 6.03e-52

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 351 RIEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYV 430
Cdd:COG1120     1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 431 SQQPYL-FEGTIRDNIRYGR---------PEATDAE-VEEAARLAYAHDFIsaqpqgyETPVGEngvtLSGGQRQRLSIA 499
Cdd:COG1120    81 PQEPPApFGLTVRELVALGRyphlglfgrPSAEDREaVEEALERTGLEHLA-------DRPVDE----LSGGERQRVLIA 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 500 RALVRNAPILLLDEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG------NHE 570
Cdd:COG1120   150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNLAARyADRLVLLKDGRIVAQGppeevlTPE 229


                  ....*
gi 1582666899 571 TLAKV 575
Cdd:COG1120   230 LLEEV 234

ABCC_Protease_Secretion

cd03246

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...

352-563

1.82e-51

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.

Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 174.71 E-value: 1.82e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES--VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAY 429
Cdd:cd03246     1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 430 VSQQPYLFEGTIRDNIrygrpeatdaeveeaarlayahdfisaqpqgyetpvgengvtLSGGQRQRLSIARALVRNAPIL 509
Cdd:cd03246    81 LPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGNPRIL 118

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1582666899 510 LLDEATSALDTESEAAVQKALDEA-MSGRTVVVIAHRLSTVVRADKIVVMQQGRV 563
Cdd:cd03246   119 VLDEPNSHLDVEGERALNQAIAALkAAGATRIVIAHRPETLASADRILVLEDGRV 173

ABCC_cytochrome_bd

cd03247

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...

352-567

6.05e-51

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

Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 173.27 E-value: 6.05e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES--VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIaHITKKSLRQQLAY 429
Cdd:cd03247     1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV-SDLEKALSSLISV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 430 VSQQPYLFEGTIRDNIrygrpeatdaeveeaarlayahdfisaqpqgyetpvgenGVTLSGGQRQRLSIARALVRNAPIL 509
Cdd:cd03247    80 LNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAPIV 120

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1582666899 510 LLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEG 567
Cdd:cd03247   121 LLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178

PTZ00265

multidrug resistance protein (mdr1); Provisional

70-595

4.72e-49

multidrug resistance protein (mdr1); Provisional

Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 184.08 E-value: 4.72e-49

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899   70 DVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLY-----------AHLMTLSVGFFSEARSAHIaaqvsq 138
Cdd:PTZ00265    98 DIIFSLVLIGIFQFILSFISSFCMDVVTTKILKTLKLEFLKSVFyqdgqfhdnnpGSKLTSDLDFYLEQVNAGI------ 171

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  139 nvsGIRDVLNLTITSTvrdlltFVSLLAVMILQDPLLSLAVFIMAPpLLYALRYV-SKRLRSATREAVHLNSHVLGAMQE 217
Cdd:PTZ00265   172 ---GTKFITIFTYASA------FLGLYIWSLFKNARLTLCITCVFP-LIYICGVIcNKKVKINKKTSLLYNNNTMSIIEE 241

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  218 TIQGIAIVKAFTMEEELERKVN---KLIKGAESRANRIARL--SERTSPLTESFA-GFAVASVLAYAAYRSIYFN--VPP 289
Cdd:PTZ00265   242 ALVGIRTVVSYCGEKTILKKFNlseKLYSKYILKANFMESLhiGMINGFILASYAfGFWYGTRIIISDLSNQQPNndFHG 321

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  290 GAFFSFVTALLLAYDPARRLARLQVQMERAVVNARMIYELLDMEPRQRDLPDARPLTVTQaRIEFRNVSFAYGNE---SV 366
Cdd:PTZ00265   322 GSVISILLGVLISMFMLTIILPNITEYMKSLEATNSLYEIINRKPLVENNDDGKKLKDIK-KIQFKNVRFHYDTRkdvEI 400

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  367 LSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILI-DGQDIAHITKKSLRQQLAYVSQQPYLFEGTIRDNI 445
Cdd:PTZ00265   401 YKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNNI 480

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  446 RYG-------------------------------RPEAT--------------------------DAEVEEAARLAYAHD 468
Cdd:PTZ00265   481 KYSlyslkdlealsnyynedgndsqenknkrnscRAKCAgdlndmsnttdsneliemrknyqtikDSEVVDVSKKVLIHD 560

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  469 FISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALD--EAMSGRTVVVIAHRL 546
Cdd:PTZ00265   561 FVSALPDKYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRL 640

                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  547 STVVRADKIVVM------------------------------QQGR-----------------VVEEGNHETLAKVSDGL 579
Cdd:PTZ00265   641 STIRYANTIFVLsnrergstvdvdiigedptkdnkennnknnKDDNnnnnnnnnnkinnagsyIIEQGTHDALMKNKNGI 720

                          650
                   ....*....|....*.
gi 1582666899  580 YARLNNLQRPSASDSN 595
Cdd:PTZ00265   721 YYTMINNQKVSSKKSS 736

EcfA2

COG1122

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...

352-568

9.55e-49

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];

Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 169.44 E-value: 9.55e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES-VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYV 430
Cdd:COG1122     1 IELENLSFSYPGGTpALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 431 SQQP--YLFEGTIRDNIRYG------RPEATDAEVEEAARLAYAHDFISAQPQgyetpvgengvTLSGGQRQRLSIARAL 502
Cdd:COG1122    81 FQNPddQLFAPTVEEDVAFGpenlglPREEIRERVEEALELVGLEHLADRPPH-----------ELSGGQKQRVAIAGVL 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1582666899 503 VRNAPILLLDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGN 568
Cdd:COG1122   150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGT 217

CcmA

COG1131

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

352-572

2.84e-48

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

Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 168.32 E-value: 2.84e-48

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKsLRQQLAYVS 431
Cdd:COG1131     1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAE-VRRRIGYVP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYLFEG-TIRDNIR-----YGRPEATDAE-VEEAARL----AYAHDFISaqpqgyetpvgengvTLSGGQRQRLSIAR 500
Cdd:COG1131    80 QEPALYPDlTVRENLRffarlYGLPRKEARErIDELLELfgltDAADRKVG---------------TLSGGMKQRLGLAL 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1582666899 501 ALVRNAPILLLDEATSALDTESEAAVQKAL-DEAMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHETL 572
Cdd:COG1131   145 ALLHDPELLILDEPTSGLDPEARRELWELLrELAAEGKTVLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDEL 218

NatA

COG4555

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...

352-568

2.92e-48

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];

Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 168.50 E-value: 2.92e-48

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKsLRQQLAYVS 431
Cdd:COG4555     2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-ARRQIGVLP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYLFEG-TIRDNIRY------GRPEATDAEVEEAARLAYAHDFIsaqpqgyETPVGEngvtLSGGQRQRLSIARALVR 504
Cdd:COG4555    81 DERGLYDRlTVRENIRYfaelygLFDEELKKRIEELIELLGLEEFL-------DRRVGE----LSTGMKKKVALARALVH 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582666899 505 NAPILLLDEATSALDTESEAAVQKALDEAM-SGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGN 568
Cdd:COG4555   150 DPKVLLLDEPTNGLDVMARRLLREILRALKkEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGS 215

PLN03130

ABC transporter C family member; Provisional

338-583

1.83e-47

ABC transporter C family member; Provisional

Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 179.55 E-value: 1.83e-47

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  338 DLPDARPLTVTQAR----------IEFRNVSFAYGNE--SVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPRE 405
Cdd:PLN03130  1214 DLPSEAPLVIENNRpppgwpssgsIKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELER 1293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  406 GEILIDGQDIAHITKKSLRQQLAYVSQQPYLFEGTIRDNIRygrP--EATDAEVEEAARLAYAHDFISAQPQGYETPVGE 483
Cdd:PLN03130  1294 GRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGTVRFNLD---PfnEHNDADLWESLERAHLKDVIRRNSLGLDAEVSE 1370

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  484 NGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRV 563
Cdd:PLN03130  1371 AGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRV 1450

                          250       260
                   ....*....|....*....|
gi 1582666899  564 VEEGNHETLAKVSDGLYARL 583
Cdd:PLN03130  1451 VEFDTPENLLSNEGSAFSKM 1470

ABCC_MRP_domain1

cd03250

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...

352-562

3.73e-47

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: 164.18 E-value: 3.73e-47

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES-----VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQdiahitkkslrqq 426
Cdd:cd03250     1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 427 LAYVSQQPYLFEGTIRDNIRYGRPEatDAE----VEEAARLAYahDfISAQPQGYETPVGENGVTLSGGQRQRLSIARAL 502
Cdd:cd03250    68 IAYVSQEPWIQNGTIRENILFGKPF--DEEryekVIKACALEP--D-LEILPDGDLTEIGEKGINLSGGQKQRISLARAV 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582666899 503 VRNAPILLLDEATSALDTESEA-----AVQKALdeaMSGRTVVVIAHRLSTVVRADKIVVMQQGR 562
Cdd:cd03250   143 YSDADIYLLDDPLSAVDAHVGRhifenCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204

ABC_Class3

cd03229

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...

352-562

1.27e-46

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: 161.97 E-value: 1.27e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKS--LRQQLAY 429
Cdd:cd03229     1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELppLRRRIGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 430 VSQQPYLFEG-TIRDNIRYGrpeatdaeveeaarlayahdfisaqpqgyetpvgengvtLSGGQRQRLSIARALVRNAPI 508
Cdd:cd03229    81 VFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMDPDV 121

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1582666899 509 LLLDEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGR 562
Cdd:cd03229   122 LLLDEPTSALDPITRREVRALLKSlqAQLGITVVLVTHDLDEAARlADRVVVLRDGK 178

GsiA

COG1123

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...

328-567

2.03e-46

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: 170.85 E-value: 2.03e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 328 ELLDMEPRQRDLPDARPLTVTQAR--IEFRNVSFAYGNES-----VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRF 400
Cdd:COG1123   235 QALAAVPRLGAARGRAAPAAAAAEplLEVRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGL 314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 401 YDPREGEILIDGQDIAHITKKS---LRQQLAYVSQQPY--LFEG-TIRDNIRYG-------RPEATDAEVEEAARL---- 463
Cdd:COG1123   315 LRPTSGSILFDGKDLTKLSRRSlreLRRRVQMVFQDPYssLNPRmTVGDIIAEPlrlhgllSRAERRERVAELLERvglp 394

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 464 -AYAHDFISAqpqgyetpvgengvtLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDE--AMSGRTVV 540
Cdd:COG1123   395 pDLADRYPHE---------------LSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDlqRELGLTYL 459

                         250       260
                  ....*....|....*....|....*....
gi 1582666899 541 VIAHRLStVVR--ADKIVVMQQGRVVEEG 567
Cdd:COG1123   460 FISHDLA-VVRyiADRVAVMYDGRIVEDG 487

ABC_Iron-Siderophores_B12_Hemin

cd03214

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...

353-567

5.29e-45

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: 157.60 E-value: 5.29e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 353 EFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYVSQ 432
Cdd:cd03214     1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 433 qpYLfegtirdnirygrpEATDAEveeaarlAYAHDFISaqpqgyetpvgengvTLSGGQRQRLSIARALVRNAPILLLD 512
Cdd:cd03214    81 --AL--------------ELLGLA-------HLADRPFN---------------ELSGGERQRVLLARALAQEPPILLLD 122

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1582666899 513 EATSALDTESEAAVQKALDE--AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:cd03214   123 EPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNLAARyADRVILLKDGRIVAQG 180

PLN03232

ABC transporter C family member; Provisional

123-572

6.36e-45

ABC transporter C family member; Provisional

Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 171.70 E-value: 6.36e-45

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  123 FFSEARSAHIAAQVSQNVSGI-RDVLNLT---ITSTVRDLLTF--------VSLLAVMilqdPLLslaVFIMAPPLLY-- 188
Cdd:PLN03232  1000 FFHTNPTGRVINRFSKDIGDIdRNVANLMnmfMNQLWQLLSTFaligtvstISLWAIM----PLL---ILFYAAYLYYqs 1072

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  189 ALRYVsKRLRSATReavhlnSHVLGAMQETIQGIAIVKAFTMEEELErKVNKLIKGAESRANRIARLSERTSPL-TESFA 267
Cdd:PLN03232  1073 TSREV-RRLDSVTR------SPIYAQFGEALNGLSSIRAYKAYDRMA-KINGKSMDNNIRFTLANTSSNRWLTIrLETLG 1144

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  268 GFAVASVLAYAAYRsiYFNVPPGAFFSFVTALLLAY-----DPARRLARLQVQMERAVVNARMIYELLDMEPRQRDL-PD 341
Cdd:PLN03232  1145 GVMIWLTATFAVLR--NGNAENQAGFASTMGLLLSYtlnitTLLSGVLRQASKAENSLNSVERVGNYIDLPSEATAIiEN 1222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  342 ARPLTVTQAR--IEFRNVSFAY--GNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAH 417
Cdd:PLN03232  1223 NRPVSGWPSRgsIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAK 1302

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  418 ITKKSLRQQLAYVSQQPYLFEGTIRDNIRygrP--EATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQR 495
Cdd:PLN03232  1303 FGLTDLRRVLSIIPQSPVLFSGTVRFNID---PfsEHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQL 1379

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582666899  496 LSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETL 572
Cdd:PLN03232  1380 LSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQEL 1456

ABC_Carb_Solutes_like

cd03259

ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...

352-567

9.19e-45

ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 158.07 E-value: 9.19e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKslRQQLAYVS 431
Cdd:cd03259     1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYLFEG-TIRDNIRYG-----RPEAT-DAEVEEAARLAYAHDFISAQPQgyetpvgengvTLSGGQRQRLSIARALVR 504
Cdd:cd03259    79 QDYALFPHlTVAENIAFGlklrgVPKAEiRARVRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALARALAR 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582666899 505 NAPILLLDEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:cd03259   148 EPSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213

ABC_6TM_exporter_like

cd18564

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...

36-323

1.41e-44

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: 160.37 E-value: 1.41e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  36 VFAIACLIVVALSTAFTAWIMRAIIDEAFANRRAD---------------VVWIICLSIFIAFVLRGFASYGQAVALSKV 100
Cdd:cd18564     2 ALALLALLLETALRLLEPWPLKVVIDDVLGDKPLPgllglapllgpdplaLLLLAAAALVGIALLRGLASYAGTYLTALV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 101 GNDIVARYQRRLYAHLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVF 180
Cdd:cd18564    82 GQRVVLDLRRDLFAHLQRLSLSFHDRRRTGDLLSRLTGDVGAIQDLLVSGVLPLLTNLLTLVGMLGVMFWLDWQLALIAL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 181 IMAPPLLYALRYVSKRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKVnklikGAESRAN-----RIARL 255
Cdd:cd18564   162 AVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRF-----ARENRKSlraglRAARL 236

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1582666899 256 SERTSPLTESFAGFAVASVLAYAAYRSIYFNVPPGAFFSFVTALLLAYDPARRLARLQVQMERAVVNA 323
Cdd:cd18564   237 QALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASA 304

ABC_cobalt_CbiO_domain1

cd03225

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...

353-562

1.71e-44

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: 157.24 E-value: 1.71e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 353 EFRNVSFAYGN--ESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYV 430
Cdd:cd03225     1 ELKNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 431 SQQP--YLFEGTIRDNI-----RYGRPEAT-DAEVEEAARL----AYAHDFISaqpqgyetpvgengvTLSGGQRQRLSI 498
Cdd:cd03225    81 FQNPddQFFGPTVEEEVafgleNLGLPEEEiEERVEEALELvgleGLRDRSPF---------------TLSGGQKQRVAI 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582666899 499 ARALVRNAPILLLDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGR 562
Cdd:cd03225   146 AGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211

ABC_ATPase

cd00267

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...

353-562

4.61e-44

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 154.32 E-value: 4.61e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 353 EFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYVSQ 432
Cdd:cd00267     1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 433 qpylfegtirdnirygrpeatdaeveeaarlayahdfisaqpqgyetpvgengvtLSGGQRQRLSIARALVRNAPILLLD 512
Cdd:cd00267    81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1582666899 513 EATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLSTVVRA-DKIVVMQQGR 562
Cdd:cd00267   106 EPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAaDRVIVLKDGK 157

ABC_tran

pfam00005

ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...

367-516

5.63e-44

Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 153.57 E-value: 5.63e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 367 LSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYVSQQPYLF-EGTIRDNI 445
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582666899 446 RYGRP------EATDAEVEEAARLAYAHDFIsaqpqgyETPVGENGVTLSGGQRQRLSIARALVRNAPILLLDEATS 516
Cdd:pfam00005  81 RLGLLlkglskREKDARAEEALEKLGLGDLA-------DRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150

ABC_DR_subfamily_A

cd03230

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...

352-563

3.05e-43

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: 152.55 E-value: 3.05e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIaHITKKSLRQQLAYVS 431
Cdd:cd03230     1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI-KKEPEEVKRRIGYLP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYLFEG-TIRDNIRYgrpeatdaeveeaarlayahdfisaqpqgyetpvgengvtlSGGQRQRLSIARALVRNAPILL 510
Cdd:cd03230    80 EEPSLYENlTVRENLKL-----------------------------------------SGGMKQRLALAQALLHDPELLI 118

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1582666899 511 LDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRV 563
Cdd:cd03230   119 LDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERlCDRVAILNNGRI 173

ZnuC

COG1121

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

352-563

3.23e-43

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

Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 154.86 E-value: 3.23e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHitkksLRQQLAYVS 431
Cdd:COG1121     7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARRRIGYVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYLFEG---TIRDNI---RYG------RPEATD-AEVEEA-ARL---AYAHdfisaqpqgyeTPVGEngvtLSGGQRQ 494
Cdd:COG1121    82 QRAEVDWDfpiTVRDVVlmgRYGrrglfrRPSRADrEAVDEAlERVgleDLAD-----------RPIGE----LSGGQQQ 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582666899 495 RLSIARALVRNAPILLLDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRV 563
Cdd:COG1121   147 RVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLV 217

DppF

COG1124

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...

352-582

1.41e-42

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: 153.42 E-value: 1.41e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES----VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQL 427
Cdd:COG1124     2 LEVRNLSVSYGQGGrrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 428 AYVSQQPYL-----FegTIRDNIR-----YGRPEaTDAEVEEAARLA---------YAHDfisaqpqgyetpvgengvtL 488
Cdd:COG1124    82 QMVFQDPYAslhprH--TVDRILAeplriHGLPD-REERIAELLEQVglppsfldrYPHQ-------------------L 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 489 SGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVE 565
Cdd:COG1124   140 SGGQRQRVAIARALILEPELLLLDEPTSALDVSVQAEILNLLKDlrEERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVE 219

                         250
                  ....*....|....*..
gi 1582666899 566 EGNHETLAKVSDGLYAR 582
Cdd:COG1124   220 ELTVADLLAGPKHPYTR 236

LolD

COG1136

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

352-566

1.45e-42

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

Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 152.50 E-value: 1.45e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES----VLSGVSFTAEGGATTALVGPSGAGKST---VISLIPRfydPREGEILIDGQDIAHITKKSL- 423
Cdd:COG1136     5 LELRNLTKSYGTGEgevtALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLSERELa 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 424 ---RQQLAYVSQQPYLFEG-TIRDNIRY-----GRPEATDAE-VEEAARL----AYAHDFISAqpqgyetpvgengvtLS 489
Cdd:COG1136    82 rlrRRHIGFVFQFFNLLPElTALENVALplllaGVSRKERRErARELLERvglgDRLDHRPSQ---------------LS 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582666899 490 GGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEE 566
Cdd:COG1136   147 GGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225

ABC_NikE_OppD_transporters

cd03257

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...

352-567

1.97e-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: 152.27 E-value: 1.97e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES----VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSL---R 424
Cdd:cd03257     2 LEVKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkirR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 425 QQLAYVSQQPYL-------FEGTIRDNIRYGRPEATDAEVEEAARLAYAH-----DFISAQPqgYEtpvgengvtLSGGQ 492
Cdd:cd03257    82 KEIQMVFQDPMSslnprmtIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGvglpeEVLNRYP--HE---------LSGGQ 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582666899 493 RQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRLStVVR--ADKIVVMQQGRVVEEG 567
Cdd:cd03257   151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKlqEELGLTLLFITHDLG-VVAkiADRVAVMYAGKIVEEG 228

ABC_MetN_methionine_transporter

cd03258

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...

352-567

4.87e-42

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: 151.19 E-value: 4.87e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES----VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSL---R 424
Cdd:cd03258     2 IELKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkaR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 425 QQLAYVSQQPYLFEG-TIRDNIRY-----GRPeatDAEVEEAAR-------LAYAHDFISAQpqgyetpvgengvtLSGG 491
Cdd:cd03258    82 RRIGMIFQHFNLLSSrTVFENVALpleiaGVP---KAEIEERVLellelvgLEDKADAYPAQ--------------LSGG 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582666899 492 QRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMS--GRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:cd03258   145 QKQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEG 223

ABC_OpuCA_Osmoprotection

cd03295

ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...

352-572

1.12e-41

ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 150.53 E-value: 1.12e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES-VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYV 430
Cdd:cd03295     1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 431 SQQPYLF-EGTIRDNI-------RYGRPEAtDAEVEEAARLayahdfISAQPQGYetpVGENGVTLSGGQRQRLSIARAL 502
Cdd:cd03295    81 IQQIGLFpHMTVEENIalvpkllKWPKEKI-RERADELLAL------VGLDPAEF---ADRYPHELSGGQQQRVGVARAL 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1582666899 503 VRNAPILLLDEATSALDTESEAAVQ---KALDEAMsGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHETL 572
Cdd:cd03295   151 AADPPLLLMDEPFGALDPITRDQLQeefKRLQQEL-GKTIVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEI 223

MlaF

COG1127

ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...

352-577

2.00e-41

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: 149.74 E-value: 2.00e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKK---SLRQQLA 428
Cdd:COG1127     6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRRRIG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 429 YVSQQPYLFEG-TIRDNIRYG---RPEATDAEVEEAAR-------LAYAHDFISAQpqgyetpvgengvtLSGGQRQRLS 497
Cdd:COG1127    86 MLFQGGALFDSlTVFENVAFPlreHTDLSEAEIRELVLeklelvgLPGAADKMPSE--------------LSGGMRKRVA 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 498 IARALVRNAPILLLDEATSALDTESEAAV-------QKALdeamsGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNH 569
Cdd:COG1127   152 LARALALDPEILLYDEPTAGLDPITSAVIdelirelRDEL-----GLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTP 226


                  ....*...
gi 1582666899 570 ETLAKVSD 577
Cdd:COG1127   227 EELLASDD 234

ABC_NrtD_SsuB_transporters

cd03293

ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...

352-566

9.10e-41

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: 147.23 E-value: 9.10e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES----VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAhitkkSLRQQL 427
Cdd:cd03293     1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----GPGPDR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 428 AYVSQQPYLFE-GTIRDNIRYGrPEAtdAEVEEAARLAYAHDFISAqpqgyetpVGENGV------TLSGGQRQRLSIAR 500
Cdd:cd03293    76 GYVFQQDALLPwLTVLDNVALG-LEL--QGVPKAEARERAEELLEL--------VGLSGFenayphQLSGGMRQRVALAR 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 501 ALVRNAPILLLDEATSALDTESEAAVQ----KALDEamSGRTVVVIAHRLSTVVR-ADKIVVMQQ--GRVVEE 566
Cdd:cd03293   145 ALAVDPDVLLLDEPFSALDALTREQLQeellDIWRE--TGKTVLLVTHDIDEAVFlADRVVVLSArpGRIVAE 215

ABC_MJ0796_LolCDE_FtsE

cd03255

ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...

352-563

1.03e-40

ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.

Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 147.25 E-value: 1.03e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES----VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSL---- 423
Cdd:cd03255     1 IELKNLSKTYGGGGekvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELaafr 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 424 RQQLAYVSQQPYLFEG-TIRDNIRY-----GRPEATDAEVEEAArLAYAH--DFISAQPQgyetpvgengvTLSGGQRQR 495
Cdd:cd03255    81 RRHIGFVFQSFNLLPDlTALENVELplllaGVPKKERRERAEEL-LERVGlgDRLNHYPS-----------ELSGGQQQR 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 496 LSIARALVRNAPILLLDEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRLSTVVRADKIVVMQQGRV 563
Cdd:cd03255   149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218

ABCC_SUR2

cd03288

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...

351-583

1.46e-40

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.

Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 148.13 E-value: 1.46e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 351 RIEFRNVSFAYGN--ESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLA 428
Cdd:cd03288    19 EIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLS 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 429 YVSQQPYLFEGTIRDNIRygrPE--ATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNA 506
Cdd:cd03288    99 IILQDPILFSGSIRFNLD---PEckCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKS 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582666899 507 PILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAKVSDGLYARL 583
Cdd:cd03288   176 SILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASL 252

ABC_Metallic_Cations

cd03235

ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...

353-558

1.78e-40

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: 146.52 E-value: 1.78e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 353 EFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHItkkslRQQLAYVSQ 432
Cdd:cd03235     1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE-----RKRIGYVPQ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 433 QPYL---FEGTIRDNIRYGR----------PEATDAEVEEA----ARLAYAHDFISaqpqgyetpvgengvTLSGGQRQR 495
Cdd:cd03235    76 RRSIdrdFPISVRDVVLMGLyghkglfrrlSKADKAKVDEAlervGLSELADRQIG---------------ELSGGQQQR 140

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582666899 496 LSIARALVRNAPILLLDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLSTVVR-ADKIVVM 558
Cdd:cd03235   141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEyFDRVLLL 205

PstB

COG1117

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

342-572

1.80e-40

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

Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 147.88 E-value: 1.80e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 342 ARPLTVTQARIEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYD--PR---EGEILIDGQDI- 415
Cdd:COG1117     2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGarvEGEILLDGEDIy 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 416 -AHITKKSLRQQLAYVSQQPYLFEGTIRDNIRYG-------RPEATDAEVEEAARLAYAHDfisaqpqgyEtpV----GE 483
Cdd:COG1117    82 dPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGlrlhgikSKSELDEIVEESLRKAALWD---------E--VkdrlKK 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 484 NGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVR-ADKIVVMQQGR 562
Cdd:COG1117   151 SALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQQAARvSDYTAFFYLGE 230

                         250
                  ....*....|
gi 1582666899 563 VVEEGNHETL 572
Cdd:COG1117   231 LVEFGPTEQI 240

ABC_Org_Solvent_Resistant

cd03261

ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...

352-567

3.09e-40

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: 146.49 E-value: 3.09e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKK---SLRQQLA 428
Cdd:cd03261     1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRRMG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 429 YVSQQPYLFEG-TIRDNIRYGRPEAT---DAEVEEAAR-------LAYAHDFISAQpqgyetpvgengvtLSGGQRQRLS 497
Cdd:cd03261    81 MLFQSGALFDSlTVFENVAFPLREHTrlsEEEIREIVLekleavgLRGAEDLYPAE--------------LSGGMKKRVA 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1582666899 498 IARALVRNAPILLLDEATSALDTESEAAVQ---KALDEAMsGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:cd03261   147 LARALALDPELLLYDEPTAGLDPIASGVIDdliRSLKKEL-GLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEG 219

AbcC

COG1135

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

352-568

5.09e-40

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

Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 149.07 E-value: 5.09e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVS--FAYGNESV--LSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSL---R 424
Cdd:COG1135     2 IELENLSktFPTKGGPVtaLDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELraaR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 425 QQLAYVSQQPYLFEG-TIRDNIRY-----GRP-EATDAEVEEAARL----AYAHDFISAqpqgyetpvgengvtLSGGQR 493
Cdd:COG1135    82 RKIGMIFQHFNLLSSrTVAENVALpleiaGVPkAEIRKRVAELLELvglsDKADAYPSQ---------------LSGGQK 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582666899 494 QRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMS--GRTVVVIAHRLStVVR--ADKIVVMQQGRVVEEGN 568
Cdd:COG1135   147 QRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMD-VVRriCDRVAVLENGRIVEQGP 224

GlnQ

COG1126

ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...

352-567

5.94e-40

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

Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 145.91 E-value: 5.94e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIaHITKKSL---RQQLA 428
Cdd:COG1126     2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDInklRRKVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 429 YVSQQPYLFEG-TIRDNIRY------GRPEatdAEVEEAAR-------LAyahDFISAQPQgyetpvgengvTLSGGQRQ 494
Cdd:COG1126    81 MVFQQFNLFPHlTVLENVTLapikvkKMSK---AEAEERAMellervgLA---DKADAYPA-----------QLSGGQQQ 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582666899 495 RLSIARALVRNAPILLLDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLS---TVvrADKIVVMQQGRVVEEG 567
Cdd:COG1126   144 RVAIARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDlAKEGMTMVVVTHEMGfarEV--ADRVVFMDGGRIVEEG 218

fecE

PRK11231

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

352-567

9.00e-40

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

Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 145.93 E-value: 9.00e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYVS 431
Cdd:PRK11231    3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYLFEG-TIRDNIRYGRP----------EATDAEVEEAARLAYAHDFIsaqpqgyETPVGEngvtLSGGQRQRLSIAR 500
Cdd:PRK11231   83 QHHLTPEGiTVRELVAYGRSpwlslwgrlsAEDNARVNQAMEQTRINHLA-------DRRLTD----LSGGQRQRAFLAM 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582666899 501 ALVRNAPILLLDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:PRK11231  152 VLAQDTPVVLLDEPTTYLDINHQVELMRLMRElNTQGKTVVTVLHDLNQASRyCDHLVVLANGHVMAQG 220

TauB

COG1116

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...

346-566

3.90e-39

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: 3.90e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 346 TVTQARIEFRNVSFAYGNES----VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAhitkk 421
Cdd:COG1116     2 SAAAPALELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT----- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 422 SLRQQLAYVSQQPYLFE-GTIRDNIRYGrPEATDAEVEEAARLAYAH-------DFISAQPQgyetpvgengvTLSGGQR 493
Cdd:COG1116    77 GPGPDRGVVFQEPALLPwLTVLDNVALG-LELRGVPKAERRERARELlelvglaGFEDAYPH-----------QLSGGMR 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 494 QRLSIARALVRNAPILLLDEATSALDTESEAAVQkalDEAMS-----GRTVVVIAHRLSTVVR-ADKIVVMQQ--GRVVE 565
Cdd:COG1116   145 QRVAIARALANDPEVLLMDEPFGALDALTRERLQ---DELLRlwqetGKTVLFVTHDVDEAVFlADRVVVLSArpGRIVE 221


                  .
gi 1582666899 566 E 566
Cdd:COG1116   222 E 222

ABC_6TM_TmrA_like

cd18544

Six-transmembrane helical domain (TmrA) of the heterodimeric Thermus thermophilus multidrug ...

36-323

1.59e-38

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: 143.68 E-value: 1.59e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  36 VFAIACLIVVALSTAFTAWIMRAIIDEAFANRRADV--VWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLY 113
Cdd:cd18544     2 ILALLLLLLATALELLGPLLIKRAIDDYIVPGQGDLqgLLLLALLYLGLLLLSFLLQYLQTYLLQKLGQRIIYDLRRDLF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 114 AHLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYV 193
Cdd:cd18544    82 SHIQRLPLSFFDRTPVGRLVTRVTNDTEALNELFTSGLVTLIGDLLLLIGILIAMFLLNWRLALISLLVLPLLLLATYLF 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 194 SKRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERK---VNKLIKGAESRANRIARLSertSPLTESFAGFA 270
Cdd:cd18544   162 RKKSRKAYREVREKLSRLNAFLQESISGMSVIQLFNREKREFEEfdeINQEYRKANLKSIKLFALF---RPLVELLSSLA 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 271 VASVLAYAAYRSIYFNVPPGAFFSFVTALLLAYDPARRLARLQVQMERAVVNA 323
Cdd:cd18544   239 LALVLWYGGGQVLSGAVTLGVLYAFIQYIQRFFRPIRDLAEKFNILQSAMASA 291

CeuD

COG4604

ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...

352-567

1.76e-38

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

Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 142.14 E-value: 1.76e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYVS 431
Cdd:COG4604     2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYL-FEGTIRDNI---RY----GRPEATDAE-VEEAarLAY------AHDFISaqpqgyetpvgengvTLSGGQRQRL 496
Cdd:COG4604    82 QENHInSRLTVRELVafgRFpyskGRLTAEDREiIDEA--IAYldledlADRYLD---------------ELSGGQRQRA 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1582666899 497 SIARALVRNAPILLLDEATSALDTesEAAVQ------KALDEamSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:COG4604   145 FIAMVLAQDTDYVLLDEPLNNLDM--KHSVQmmkllrRLADE--LGKTVVIVLHDINFASCyADHIVAMKDGRVVAQG 218

MalK

COG3839

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

350-564

2.00e-38

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

Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 144.83 E-value: 2.00e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 350 ARIEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKslRQQLAY 429
Cdd:COG3839     2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNIAM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 430 VSQQPYLFEG-TIRDNIRYG-----RPEAT-DAEVEEAARL----AYAHDFISAqpqgyetpvgengvtLSGGQRQRLSI 498
Cdd:COG3839    80 VFQSYALYPHmTVYENIAFPlklrkVPKAEiDRRVREAAELlgleDLLDRKPKQ---------------LSGGQRQRVAL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 499 ARALVRNAPILLLDEATSALD------TESE-AAVQKALD-----------EAMSgrtvvviahrLstvvrADKIVVMQQ 560
Cdd:COG3839   145 GRALVREPKVFLLDEPLSNLDaklrveMRAEiKRLHRRLGtttiyvthdqvEAMT----------L-----ADRIAVMND 209


                  ....
gi 1582666899 561 GRVV 564
Cdd:COG3839   210 GRIQ 213

ABC_6TM_exporter_like

cd18550

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...

36-321

3.35e-38

Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 142.62 E-value: 3.35e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  36 VFAIACLIVVALSTAFTAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYAH 115
Cdd:cd18550     2 ALVLLLILLSALLGLLPPLLLREIIDDALPQGDLGLLVLLALGMVAVAVASALLGVVQTYLSARIGQGVMYDLRVQLYAH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 116 LMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYVSK 195
Cdd:cd18550    82 LQRMSLAFFTRTRTGEIQSRLNNDVGGAQSVVTGTLTSVVSNVVTLVATLVAMLALDWRLALLSLVLLPLFVLPTRRVGR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 196 RLRSATREAVHLNSHVLGAMQET--IQGIAIVKAFTMEEELERKVNKlikgaesRANRIARLSERTSPLTESF------- 266
Cdd:cd18550   162 RRRKLTREQQEKLAELNSIMQETlsVSGALLVKLFGREDDEAARFAR-------RSRELRDLGVRQALAGRWFfaalglf 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1582666899 267 AGFAVASVLAYAAYRSIYFNVPPGAFFSFVTALLLAYDPARRLARLQVQMERAVV 321
Cdd:cd18550   235 TAIGPALVYWVGGLLVIGGGLTIGTLVAFTALLGRLYGPLTQLLNIQVDLMTSLA 289

PotA

COG3842

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...

348-567

7.32e-38

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

Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 143.31 E-value: 7.32e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 348 TQARIEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHItkKSLRQQL 427
Cdd:COG3842     2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL--PPEKRNV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 428 AYVSQQ----PYLfegTIRDNIRYG------RPEATDAEVEEAARL----AYAHDFISaqpqgyetpvgengvTLSGGQR 493
Cdd:COG3842    80 GMVFQDyalfPHL---TVAENVAFGlrmrgvPKAEIRARVAELLELvgleGLADRYPH---------------QLSGGQQ 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 494 QRLSIARALVRNAPILLLDEATSALD------TESE-AAVQKALdeamsGRTVVVIAHRLS---TVvrADKIVVMQQGRV 563
Cdd:COG3842   142 QRVALARALAPEPRVLLLDEPLSALDaklreeMREElRRLQREL-----GITFIYVTHDQEealAL--ADRIAVMNDGRI 214


                  ....
gi 1582666899 564 VEEG 567
Cdd:COG3842   215 EQVG 218

ABC_HisP_GlnQ

cd03262

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...

352-563

9.59e-38

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: 9.59e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKK--SLRQQLAY 429
Cdd:cd03262     1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNinELRQKVGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 430 VSQQPYLFEG-TIRDNIRYGRPEATDAEVEEAARLAYAH-------DFISAQPQgyetpvgengvTLSGGQRQRLSIARA 501
Cdd:cd03262    81 VFQQFNLFPHlTVLENITLAPIKVKGMSKAEAEERALELlekvglaDKADAYPA-----------QLSGGQQQRVAIARA 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582666899 502 LVRNAPILLLDEATSALDTESEAAVQKAL-DEAMSGRTVVVIAHRLStVVR--ADKIVVMQQGRV 563
Cdd:cd03262   150 LAMNPKVMLFDEPTSALDPELVGEVLDVMkDLAEEGMTMVVVTHEMG-FARevADRVIFMDDGRI 213

GsiA

COG1123

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...

352-582

1.22e-37

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: 146.20 E-value: 1.22e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAY--GNESVLSGVSFTAEGGATTALVGPSGAGKST----VISLIPRFYDPrEGEILIDGQDIAHITKKSLRQ 425
Cdd:COG1123     5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTlalaLMGLLPHGGRI-SGEVLLDGRDLLELSEALRGR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 426 QLAYVSQQPY--LFEGTIRDNIRYG------RPEATDAEVEEAARLAYAHDFISAQPQgyetpvgengvTLSGGQRQRLS 497
Cdd:COG1123    84 RIGMVFQDPMtqLNPVTVGDQIAEAlenlglSRAEARARVLELLEAVGLERRLDRYPH-----------QLSGGQRQRVA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 498 IARALVRNAPILLLDEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHETLAK 574
Cdd:COG1123   153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRElqRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232


                  ....*...
gi 1582666899 575 VSDGLYAR 582
Cdd:COG1123   233 APQALAAV 240

PhnC

COG3638

ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...

352-564

1.84e-37

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

Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 139.04 E-value: 1.84e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES-VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQ---QL 427
Cdd:COG3638     3 LELRNLSKRYPGGTpALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrrRI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 428 AYVSQQPYLFEG-TIRDNI-----------RYGRPEATDAEVEEAAR-------LAYAHDfisaqpqgyetPVGengvTL 488
Cdd:COG3638    83 GMIFQQFNLVPRlSVLTNVlagrlgrtstwRSLLGLFPPEDRERALEalervglADKAYQ-----------RAD----QL 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582666899 489 SGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKAL-DEAMS-GRTVVVIAHRLSTVVR-ADKIVVMQQGRVV 564
Cdd:COG3638   148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLrRIAREdGITVVVNLHQVDLARRyADRIIGLRDGRVV 226

ABC_6TM_YknU_like

cd18542

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and ...

35-326

4.73e-37

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: 139.49 E-value: 4.73e-37

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  35 YVFAIACLIVVALSTAFTAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYA 114
Cdd:cd18542     1 YLLAILALLLATALNLLIPLLIRRIIDSVIGGGLRELLWLLALLILGVALLRGVFRYLQGYLAEKASQKVAYDLRNDLYD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 115 HLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYVS 194
Cdd:cd18542    81 HLQRLSFSFHDKARTGDLMSRCTSDVDTIRRFLAFGLVELVRAVLLFIGALIIMFSINWKLTLISLAIIPFIALFSYVFF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 195 KRLRSA-----TREAVhLNShvlgAMQETIQGIAIVKAFTMEE-ELER--KVNKLIKGaesRANRIARLSERTSPLTESF 266
Cdd:cd18542   161 KKVRPAfeeirEQEGE-LNT----VLQENLTGVRVVKAFAREDyEIEKfdKENEEYRD---LNIKLAKLLAKYWPLMDFL 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 267 AGFAVASVLAYAAYRSIYFNVPPG---AFFSFVTALLLaydPARRLARLQVQMERAVVNARMI 326
Cdd:cd18542   233 SGLQIVLVLWVGGYLVINGEITLGelvAFISYLWMLIW---PVRQLGRLINDMSRASASAERI 292

PLN03232

ABC transporter C family member; Provisional

68-583

4.74e-37

ABC transporter C family member; Provisional

Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 147.82 E-value: 4.74e-37

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899   68 RADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNdIVARYQRRLYAHLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVL 147
Cdd:PLN03232   333 EGDPAWVGYVYAFLIFFGVTFGVLCESQYFQNVGR-VGFRLRSTLVAAIFHKSLRLTHEARKNFASGKVTNMITTDANAL 411

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  148 NLTI-------TSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRyvskRLRSATREAVHLNSHVLGAMQETIQ 220
Cdd:PLN03232   412 QQIAeqlhglwSAPFRIIVSMVLLYQQLGVASLFGSLILFLLIPLQTLIVR----KMRKLTKEGLQWTDKRVGIINEILA 487

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  221 GIAIVKAFTMEEELERKVNKLikgaesranRIARLSE-RTSPLTESFAGF------AVASVLAYAAYRSIYFNVPPGAFF 293
Cdd:PLN03232   488 SMDTVKCYAWEKSFESRIQGI---------RNEELSWfRKAQLLSAFNSFilnsipVVVTLVSFGVFVLLGGDLTPARAF 558

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  294 SFVTALLLAYDPARRLARLQVQMERAVVNARMIYELLDMEprQRDLPDARPLTVTQARIEFRNVSFAYGNES---VLSGV 370
Cdd:PLN03232   559 TSLSLFAVLRSPLNMLPNLLSQVVNANVSLQRIEELLLSE--ERILAQNPPLQPGAPAISIKNGYFSWDSKTskpTLSDI 636

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  371 SFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIdgqdiahitkksLRQQLAYVSQQPYLFEGTIRDNIRYGrp 450
Cdd:PLN03232   637 NLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV------------IRGSVAYVPQVSWIFNATVRENILFG-- 702

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  451 eaTDAEVEEAAR----LAYAHDfISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAV 526
Cdd:PLN03232   703 --SDFESERYWRaidvTALQHD-LDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQV 779

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1582666899  527 -QKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAKvSDGLYARL 583
Cdd:PLN03232   780 fDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELSK-SGSLFKKL 836

ABC_6TM_YknV_like

cd18545

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknV and ...

36-323

3.33e-36

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: 137.21 E-value: 3.33e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  36 VFAIACLIVVALSTAFTAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYAH 115
Cdd:cd18545     3 LLALLLMLLSTAASLAGPYLIKIAIDEYIPNGDLSGLLIIALLFLALNLVNWVASRLRIYLMAKVGQRILYDLRQDLFSH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 116 LMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYVSK 195
Cdd:cd18545    83 LQKLSFSFFDSRPVGKILSRVINDVNSLSDLLSNGLINLIPDLLTLVGIVIIMFSLNVRLALVTLAVLPLLVLVVFLLRR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 196 RLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKVNKLIKgAESRAN-RIARLSERTSPLTESFAGFAVASV 274
Cdd:cd18545   163 RARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFDELNR-ENRKANmRAVRLNALFWPLVELISALGTALV 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1582666899 275 LAYAAYRSIYFNVPPGAFFSFVTALLLAYDPARRLARLQVQMERAVVNA 323
Cdd:cd18545   242 YWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASA 290

CcmA

COG4133

ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...

350-559

5.96e-36

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: 133.76 E-value: 5.96e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 350 ARIEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIaHITKKSLRQQLAY 429
Cdd:COG4133     1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI-RDAREDYRRRLAY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 430 VSQQPYLFEG-TIRDNIR-----YGRPeATDAEVEEAARL----AYAHdfisaqpqgyeTPVGengvTLSGGQRQRLSIA 499
Cdd:COG4133    80 LGHADGLKPElTVRENLRfwaalYGLR-ADREAIDEALEAvglaGLAD-----------LPVR----QLSAGQKRRVALA 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582666899 500 RALVRNAPILLLDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLSTVVRADKIVVMQ 559
Cdd:COG4133   144 RLLLSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELAAARVLDLGD 204

PTZ00243

ABC transporter; Provisional

340-580

7.69e-36

ABC transporter; Provisional

Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 144.15 E-value: 7.69e-36

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  340 PDARPLTVTQARIEFRNVSFAY--GNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAH 417
Cdd:PTZ00243  1297 TSAAPHPVQAGSLVFEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGA 1376

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  418 ITKKSLRQQLAYVSQQPYLFEGTIRDNIrygRP--EATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQR 495
Cdd:PTZ00243  1377 YGLRELRRQFSMIPQDPVLFDGTVRQNV---DPflEASSAEVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQL 1453

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  496 LSIARALV-RNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAK 574
Cdd:PTZ00243  1454 MCMARALLkKGSGFILMDEATANIDPALDRQIQATVMSAFSAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVM 1533


                   ....*.
gi 1582666899  575 VSDGLY 580
Cdd:PTZ00243  1534 NRQSIF 1539

ABC_ModC_like

cd03299

ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...

352-570

6.96e-35

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: 131.69 E-value: 6.96e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGnESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHItkKSLRQQLAYVS 431
Cdd:cd03299     1 LKVENLSKDWK-EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNL--PPEKRDISYVP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYLFEG-TIRDNIRYG-------RPEaTDAEVEEAARLAYAHDFISAQPQgyetpvgengvTLSGGQRQRLSIARALV 503
Cdd:cd03299    78 QNYALFPHmTVYKNIAYGlkkrkvdKKE-IERKVLEIAEMLGIDHLLNRKPE-----------TLSGGEQQRVAIARALV 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 504 RNAPILLLDEATSALDTESEAAVQKALDEAM--SGRTVVVIAHRLSTV-VRADKIVVMQQGRVVEEGNHE 570
Cdd:cd03299   146 VNPKILLLDEPFSALDVRTKEKLREELKKIRkeFGVTVLHVTHDFEEAwALADKVAIMLNGKLIQVGKPE 215

ABC_Mj1267_LivG_branched

cd03219

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...

352-567

8.11e-35

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: 131.41 E-value: 8.11e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHIT-KKSLRQQLAYV 430
Cdd:cd03219     1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPpHEIARLGIGRT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 431 SQQPYLFEG-TIRDNIRYG------------RPEATDAEVEEAAR--------LAYAHdfisaqpqgyeTPVGEngvtLS 489
Cdd:cd03219    81 FQIPRLFPElTVLENVMVAaqartgsglllaRARREEREARERAEellervglADLAD-----------RPAGE----LS 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 490 GGQRQRLSIARALVRNAPILLLDEATSAL-DTESEAAVQKALDEAMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:cd03219   146 YGQQRRLEIARALATDPKLLLLDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEG 225

FtsE

COG2884

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

352-567

1.08e-34

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

Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 130.56 E-value: 1.08e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES-VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKS---LRQQL 427
Cdd:COG2884     2 IRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 428 AYVSQQPYLFEG-TIRDNIRY-----GRPEATDAE-VEEAARL----AYAHDFISaqpqgyetpvgengvTLSGGQRQRL 496
Cdd:COG2884    82 GVVFQDFRLLPDrTVYENVALplrvtGKSRKEIRRrVREVLDLvglsDKAKALPH---------------ELSGGEQQRV 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 497 SIARALVRNAPILLLDEATSALDTESEAAVQKALDEA-MSGRTVVVIAHRLSTVVRADK-IVVMQQGRVVEEG 567
Cdd:COG2884   147 AIARALVNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKrVLELEDGRLVRDE 219

AppF

COG4608

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

367-582

3.71e-34

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

Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 132.16 E-value: 3.71e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 367 LSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITK---KSLRQQLAYVSQQPYlfeG---- 439
Cdd:COG4608    34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGrelRPLRRRMQMVFQDPY---Aslnp 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 440 --TIRDNI-------RYGRPEATDAEVEEAARLA---------YAHDFisaqpqgyetpvgengvtlSGGQRQRLSIARA 501
Cdd:COG4608   111 rmTVGDIIaeplrihGLASKAERRERVAELLELVglrpehadrYPHEF-------------------SGGQRQRIGIARA 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 502 LVRNAPILLLDEATSALDTESEAAV-------QKALdeamsGRTVVVIAHRLStVVR--ADKIVVMQQGRVVEEGNhetl 572
Cdd:COG4608   172 LALNPKLIVCDEPVSALDVSIQAQVlnlledlQDEL-----GLTYLFISHDLS-VVRhiSDRVAVMYLGKIVEIAP---- 241

                         250
                  ....*....|
gi 1582666899 573 akvSDGLYAR 582
Cdd:COG4608   242 ---RDELYAR 248

ABCG_EPDR

cd03213

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...

350-567

3.99e-34

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: 128.05 E-value: 3.99e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 350 ARIEFRNVSFA------YGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIP--RFYDPREGEILIDGQDIahiTKK 421
Cdd:cd03213     2 VTLSFRNLTVTvksspsKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL---DKR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 422 SLRQQLAYVSQQPYLFEG-TIRDNIRYgrpeatdaeveeaarlayahdfiSAQPQGyetpvgengvtLSGGQRQRLSIAR 500
Cdd:cd03213    79 SFRKIIGYVPQDDILHPTlTVRETLMF-----------------------AAKLRG-----------LSGGERKRVSIAL 124

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 501 ALVRNAPILLLDEATSALDTESEAAVQKAL-DEAMSGRTVVVIAHRLSTVV--RADKIVVMQQGRVVEEG 567
Cdd:cd03213   125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLrRLADTGRTIICSIHQPSSEIfeLFDKLLLLSQGRVIYFG 194

CysA

COG1118

ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...

352-567

5.23e-34

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

Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 132.58 E-value: 5.23e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDiAHITKKSLRQQLAYVS 431
Cdd:COG1118     3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRD-LFTNLPPRERRVGFVF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYLFEG-TIRDNIRYG---RP---EATDAEVEEAARLAYAHDFISAQP-QgyetpvgengvtLSGGQRQRLSIARALV 503
Cdd:COG1118    82 QHYALFPHmTVAENIAFGlrvRPpskAEIRARVEELLELVQLEGLADRYPsQ------------LSGGQRQRVALARALA 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 504 RNAPILLLDEATSALDteseAAVQKAL--------DEamSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:COG1118   150 VEPEVLLLDEPFGALD----AKVRKELrrwlrrlhDE--LGGTTVFVTHDQEEALElADRVVVMNQGRIEQVG 216

cbiO

PRK13632

cobalt transporter ATP-binding subunit; Provisional

349-567

5.40e-34

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 130.50 E-value: 5.40e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 349 QARIEFRNVSFAYGNES--VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQ 426
Cdd:PRK13632    5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKK 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 427 LAYVSQQP-YLFEG-TIRDNIRYG------RPEATDAEVEEAARLAYAHDFISAQPQgyetpvgengvTLSGGQRQRLSI 498
Cdd:PRK13632   85 IGIIFQNPdNQFIGaTVEDDIAFGlenkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQ-----------NLSGGQKQRVAI 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582666899 499 ARALVRNAPILLLDEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEG 567
Cdd:PRK13632  154 ASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDlrKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQG 224

ABC_PotA_N

cd03300

ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...

352-568

9.06e-34

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: 128.51 E-value: 9.06e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKslRQQLAYVS 431
Cdd:cd03300     1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH--KRPVNTVF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYLFEG-TIRDNIRYG------RPEATDAEVEEAARL----AYAHDFISAqpqgyetpvgengvtLSGGQRQRLSIAR 500
Cdd:cd03300    79 QNYALFPHlTVFENIAFGlrlkklPKAEIKERVAEALDLvqleGYANRKPSQ---------------LSGGQQQRVAIAR 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582666899 501 ALVRNAPILLLDEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRLS-TVVRADKIVVMQQGRVVEEGN 568
Cdd:cd03300   144 ALVNEPKVLLLDEPLGALDLKLRKDMQLELKRlqKELGITFVFVTHDQEeALTMSDRIAVMNKGKIQQIGT 214

ABC_cobalt_CbiO_domain2

cd03226

Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...

356-564

9.61e-34

Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.

Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 127.37 E-value: 9.61e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 356 NVSFAYG-NESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAhitKKSLRQQLAYVSQQP 434
Cdd:cd03226     4 NISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK---AKERRKSIGYVMQDV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 435 --YLFEGTIRDNIRYGRPEATD--AEVEEAARLAYAHDFISAQPQgyetpvgengvTLSGGQRQRLSIARALVRNAPILL 510
Cdd:cd03226    81 dyQLFTDSVREELLLGLKELDAgnEQAETVLKDLDLYALKERHPL-----------SLSGGQKQRLAIAAALLSGKDLLI 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1582666899 511 LDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVV 564
Cdd:cd03226   150 FDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKvCDRVLLLANGAIV 205

ABC_Pro_Gly_Betaine

cd03294

ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...

370-572

1.72e-33

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: 128.92 E-value: 1.72e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 370 VSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQ----QLAYVSQQPYLF-EGTIRDN 444
Cdd:cd03294    43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMVFQSFALLpHRTVLEN 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 445 IRY-----GRPEATDAEV-EEAARLAYAHDFISAQPQgyetpvgengvTLSGGQRQRLSIARALVRNAPILLLDEATSAL 518
Cdd:cd03294   123 VAFglevqGVPRAEREERaAEALELVGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1582666899 519 DTESEAAVQKALDE--AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHETL 572
Cdd:cd03294   192 DPLIRREMQDELLRlqAELQKTIVFITHDLDEALRlGDRIAIMKDGRLVQVGTPEEI 248

glnQ

PRK09493

glutamine ABC transporter ATP-binding protein GlnQ;

352-572

1.82e-33

glutamine ABC transporter ATP-binding protein GlnQ;

Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 127.90 E-value: 1.82e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDI--AHITKKSLRQQLAY 429
Cdd:PRK09493    2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndPKVDERLIRQEAGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 430 VSQQPYLF-EGTIRDNIRYGRPE---ATDAEVEEAARLAYAHDFISAQPQGYETpvgengvTLSGGQRQRLSIARALVRN 505
Cdd:PRK09493   82 VFQQFYLFpHLTALENVMFGPLRvrgASKEEAEKQARELLAKVGLAERAHHYPS-------ELSGGQQQRVAIARALAVK 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582666899 506 APILLLDEATSALDTESEAAVQKAL-DEAMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHETL 572
Cdd:PRK09493  155 PKLMLFDEPTSALDPELRHEVLKVMqDLAEEGMTMVIVTHEIGFAEKvASRLIFIDKGRIAEDGDPQVL 223

PLN03130

ABC transporter C family member; Provisional

176-574

1.94e-33

ABC transporter C family member; Provisional

Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 136.79 E-value: 1.94e-33

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  176 SLAVFIMAPpllyALRYVSKRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKVNKLikgaesranRIARL 255
Cdd:PLN03130   447 SLMLVLMFP----IQTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENSFQSKVQTV---------RDDEL 513

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  256 SE-RTSPLTESFAGF------AVASVLAYAAYRSIYFNVPPGAFFSFVTALLLAYDPARRLARLQVQMERAVVNARMIYE 328
Cdd:PLN03130   514 SWfRKAQLLSAFNSFilnsipVLVTVVSFGVFTLLGGDLTPARAFTSLSLFAVLRFPLFMLPNLITQAVNANVSLKRLEE 593

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  329 LLDMEprQRDLPDARPLTVTQARIEFRNVSFAY---GNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPRE 405
Cdd:PLN03130   594 LLLAE--ERVLLPNPPLEPGLPAISIKNGYFSWdskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRS 671

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  406 GEILIdgqdiahitkksLRQQLAYVSQQPYLFEGTIRDNIRYGRPeaTDAE-VEEAARL-AYAHDfISAQPQGYETPVGE 483
Cdd:PLN03130   672 DASVV------------IRGTVAYVPQVSWIFNATVRDNILFGSP--FDPErYERAIDVtALQHD-LDLLPGGDLTEIGE 736

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  484 NGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAV-QKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGR 562
Cdd:PLN03130   737 RGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVfDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGM 816

                          410
                   ....*....|..
gi 1582666899  563 VVEEGNHETLAK 574
Cdd:PLN03130   817 IKEEGTYEELSN 828

ThiQ

COG3840

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

352-572

2.13e-33

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

Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 127.56 E-value: 2.13e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVlsGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHiTKKSLRqQLAYVS 431
Cdd:COG3840     2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTA-LPPAER-PVSMLF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYLFEG-TIRDNIRYG-----RPEATD-AEVEEAARLAYAHDFISAQPQgyetpvgengvTLSGGQRQRLSIARALVR 504
Cdd:COG3840    78 QENNLFPHlTVAQNIGLGlrpglKLTAEQrAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALARCLVR 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 505 NAPILLLDEATSALD----TESEAAVQKALDEAmsGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHETL 572
Cdd:COG3840   147 KRPILLLDEPFSALDpalrQEMLDLVDELCRER--GLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAAL 217

ABC_drug_resistance_like

cd03264

ABC-type multidrug transport system, ATPase component; The biological function of this family ...

352-567

2.67e-33

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: 126.54 E-value: 2.67e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGaTTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAhITKKSLRQQLAYVS 431
Cdd:cd03264     1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL-KQPQKLRRRIGYLP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYLFEG-TIRDNIRY-----GRPEAT-DAEVEEAARLAYAHDFisaqpqgYETPVGengvTLSGGQRQRLSIARALVR 504
Cdd:cd03264    79 QEFGVYPNfTVREFLDYiawlkGIPSKEvKARVDEVLELVNLGDR-------AKKKIG----SLSGGMRRRVGIAQALVG 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1582666899 505 NAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTV-VRADKIVVMQQGRVVEEG 567
Cdd:cd03264   148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVeSLCNQVAVLNKGKLVFEG 211

hmuV

PRK13548

hemin importer ATP-binding subunit; Provisional

352-575

5.82e-33

hemin importer ATP-binding subunit; Provisional

Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 126.81 E-value: 5.82e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYVS 431
Cdd:PRK13548    3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYL-FEGTIRDNIRYGR------PEATDAEVEEAARLA----YAHDFISaqpqgyetpvgengvTLSGGQRQRLSIAR 500
Cdd:PRK13548   83 QHSSLsFPFTVEEVVAMGRaphglsRAEDDALVAAALAQVdlahLAGRDYP---------------QLSGGEQQRVQLAR 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 501 ALVR------NAPILLLDEATSALD-----TESEAAVQKALDEamsGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG- 567
Cdd:PRK13548  148 VLAQlwepdgPPRWLLLDEPTSALDlahqhHVLRLARQLAHER---GLAVIVVLHDLNLAARyADRIVLLHQGRLVADGt 224

                         250
                  ....*....|...
gi 1582666899 568 -----NHETLAKV 575
Cdd:PRK13548  225 paevlTPETLRRV 237

DppD

COG0444

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...

352-572

6.52e-33

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: 128.63 E-value: 6.52e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRN--VSFAYGNESV--LSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPR---EGEILIDGQDIAHITKKSLR 424
Cdd:COG0444     2 LEVRNlkVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 425 Q----QLAYVSQQPY-----LFegTIRDNI-------RYGRPEATDAEVEEAAR---LAYAHDFISAQPqgYEtpvgeng 485
Cdd:COG0444    82 KirgrEIQMIFQDPMtslnpVM--TVGDQIaeplrihGGLSKAEARERAIELLErvgLPDPERRLDRYP--HE------- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 486 vtLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRLStVVR--ADKIVVMQQG 561
Cdd:COG0444   151 --LSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDlqRELGLAILFITHDLG-VVAeiADRVAVMYAG 227

                         250
                  ....*....|.
gi 1582666899 562 RVVEEGNHETL 572
Cdd:COG0444   228 RIVEEGPVEEL 238

ABC_TM1139_LivF_branched

cd03224

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...

352-573

6.98e-33

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.

Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 125.62 E-value: 6.98e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHI-TKKSLRQQLAYV 430
Cdd:cd03224     1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLpPHERARAGIGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 431 SQQPYLFEG-TIRDNIRYGrpEATDAEVEEAARLAYAHDFISAQPQGYETPVGengvTLSGGQRQRLSIARALVRNAPIL 509
Cdd:cd03224    81 PEGRRIFPElTVEENLLLG--AYARRRAKRKARLERVYELFPRLKERRKQLAG----TLSGGEQQMLAIARALMSRPKLL 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582666899 510 LLDEATSALdteSEAAVQ---KALDE-AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHETLA 573
Cdd:cd03224   155 LLDEPSEGL---APKIVEeifEAIRElRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220

MRP_assoc_pro

TIGR00957

multi drug resistance-associated protein (MRP); This model describes multi drug ...

128-593

7.28e-33

Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 135.07 E-value: 7.28e-33

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  128 RSAHIAAQVSQNVSGIRDVLNLTITSTVR--DLLTFVSLLAVMILQ--------------DPLLSLAVFIMAPPLLYALR 191
Cdd:TIGR00957  399 RKALVITNSARKSSTVGEIVNLMSVDAQRfmDLATYINMIWSAPLQvilalyflwlnlgpSVLAGVAVMVLMVPLNAVMA 478

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  192 yvskrLRSATREAVHLNS--HVLGAMQETIQGIAIVKAFTMEEELERKVNKlIKGAESRANRIARLSERTSPLTESFAGF 269
Cdd:TIGR00957  479 -----MKTKTYQVAHMKSkdNRIKLMNEILNGIKVLKLYAWELAFLDKVEG-IRQEELKVLKKSAYLHAVGTFTWVCTPF 552

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  270 AVAsVLAYAAYRSIYFNVPPGAFFSFVTALL--LAYDPARRLARLQVQMERAVVNARMIYELLDMEPRQRDLPDARPLTV 347
Cdd:TIGR00957  553 LVA-LITFAVYVTVDENNILDAEKAFVSLALfnILRFPLNILPMVISSIVQASVSLKRLRIFLSHEELEPDSIERRTIKP 631

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  348 TQAR-IEFRNVSF--AYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQdiahitkkslr 424
Cdd:TIGR00957  632 GEGNsITVHNATFtwARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS----------- 700

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  425 qqLAYVSQQPYLFEGTIRDNIRYGRP--EATDAEVEEAARLAYAHDFIsaqPQGYETPVGENGVTLSGGQRQRLSIARAL 502
Cdd:TIGR00957  701 --VAYVPQQAWIQNDSLRENILFGKAlnEKYYQQVLEACALLPDLEIL---PSGDRTEIGEKGVNLSGGQKQRVSLARAV 775

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  503 VRNAPILLLDEATSALDteseAAVQKALDE-------AMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAKv 575
Cdd:TIGR00957  776 YSNADIYLFDDPLSAVD----AHVGKHIFEhvigpegVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQ- 850

                          490
                   ....*....|....*...
gi 1582666899  576 SDGLYArlnNLQRPSASD 593
Cdd:TIGR00957  851 RDGAFA---EFLRTYAPD 865

COG4559

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

352-567

7.36e-33

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

Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 126.77 E-value: 7.36e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYVS 431
Cdd:COG4559     2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYL-FEGTIRDNIRYGR------PEATDAEVEEAARLAYAHDFISAQPQgyetpvgengvTLSGGQRQRLSIARALV- 503
Cdd:COG4559    82 QHSSLaFPFTVEEVVALGRaphgssAAQDRQIVREALALVGLAHLAGRSYQ-----------TLSGGEQQRVQLARVLAq 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1582666899 504 ----RNAP--ILLLDEATSALDTESEAAV-QKALDEAMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:COG4559   151 lwepVDGGprWLFLDEPTSALDLAHQHAVlRLARQLARRGGGVVAVLHDLNLAAQyADRILLLHQGRLVAQG 222

potA

PRK09452

spermidine/putrescine ABC transporter ATP-binding protein PotA;

352-567

1.20e-32

spermidine/putrescine ABC transporter ATP-binding protein PotA;

Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 129.30 E-value: 1.20e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKslRQQLAYVS 431
Cdd:PRK09452   15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--NRHVNTVF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYLF-EGTIRDNIRYG-----RPEA-TDAEVEEAARLAYAHDFISAQPQgyetpvgengvTLSGGQRQRLSIARALVR 504
Cdd:PRK09452   93 QSYALFpHMTVFENVAFGlrmqkTPAAeITPRVMEALRMVQLEEFAQRKPH-----------QLSGGQQQRVAIARAVVN 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582666899 505 NAPILLLDEATSALDTESEAAVQ---KALDEAMsGRTVVVIAH-RLSTVVRADKIVVMQQGRVVEEG 567
Cdd:PRK09452  162 KPKVLLLDESLSALDYKLRKQMQnelKALQRKL-GITFVFVTHdQEEALTMSDRIVVMRDGRIEQDG 227

ArtP

COG4161

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

352-570

2.29e-32

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

Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 124.74 E-value: 2.29e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDG------QDIAHITKKSLRQ 425
Cdd:COG4161     3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLLRQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 426 QLAYVSQQ----PYLfegTIRDNI--------RYGRPEATDAEVEEAARLAYAhDFISAQPQgyetpvgengvTLSGGQR 493
Cdd:COG4161    83 KVGMVFQQynlwPHL---TVMENLieapckvlGLSKEQAREKAMKLLARLRLT-DKADRFPL-----------HLSGGQQ 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 494 QRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLStVVR--ADKIVVMQQGRVVEEGNHE 570
Cdd:COG4161   148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRElSQTGITQVIVTHEVE-FARkvASQVVYMEKGRIIEQGDAS 226

ABC_PhnC_transporter

cd03256

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...

352-567

2.82e-32

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: 124.60 E-value: 2.82e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGN-ESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQ---QL 427
Cdd:cd03256     1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrQI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 428 AYVSQQPYLFEG-TIRDNIRYGRPEA-----------TDAEVEEAAR-------LAYAHdfisaqpqgyeTPVGEngvtL 488
Cdd:cd03256    81 GMIFQQFNLIERlSVLENVLSGRLGRrstwrslfglfPKEEKQRALAalervglLDKAY-----------QRADQ----L 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 489 SGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMS--GRTVVVIAHRLSTVVR-ADKIVVMQQGRVVE 565
Cdd:cd03256   146 SGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAREyADRIVGLKDGRIVF 225


                  ..
gi 1582666899 566 EG 567
Cdd:cd03256   226 DG 227

ABC_6TM_TmrB_like

cd18541

Six-transmembrane helical domain (TmrB) of the heterodimeric Thermus thermophilus multidrug ...

35-301

3.27e-32

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: 125.99 E-value: 3.27e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  35 YVFAIACLIVVALSTAFTAWIMRAIIDE-AFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLY 113
Cdd:cd18541     1 YLLGILFLILVDLLQLLIPRIIGRAIDAlTAGTLTASQLLRYALLILLLALLIGIFRFLWRYLIFGASRRIEYDLRNDLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 114 AHLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYV 193
Cdd:cd18541    81 AHLLTLSPSFYQKNRTGDLMARATNDLNAVRMALGPGILYLVDALFLGVLVLVMMFTISPKLTLIALLPLPLLALLVYRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 194 SKRLRSATREA----VHLNSHVlgamQETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSPLTESFAGF 269
Cdd:cd18541   161 GKKIHKRFRKVqeafSDLSDRV----QESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNLRLARVDALFFPLIGLLIGL 236

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1582666899 270 AVASVLAYAAYRSIYFNVPPGAFFSFVTALLL 301
Cdd:cd18541   237 SFLIVLWYGGRLVIRGTITLGDLVAFNSYLGM 268

artP

PRK11124

arginine transporter ATP-binding subunit; Provisional

352-570

8.01e-32

arginine transporter ATP-binding subunit; Provisional

Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 123.20 E-value: 8.01e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQ--DIAHITK----KSLRQ 425
Cdd:PRK11124    3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSdkaiRELRR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 426 QLAYVSQQ----PYLfegTIRDNI--------RYGRPEATDAEVEEAARLAYAhDFISAQPQgyetpvgengvTLSGGQR 493
Cdd:PRK11124   83 NVGMVFQQynlwPHL---TVQQNLieapcrvlGLSKDQALARAEKLLERLRLK-PYADRFPL-----------HLSGGQQ 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 494 QRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLStVVR--ADKIVVMQQGRVVEEGNHE 570
Cdd:PRK11124  148 QRVAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRElAETGITQVIVTHEVE-VARktASRVVYMENGHIVEQGDAS 226

ABC_MalK_N

cd03301

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...

352-567

1.25e-31

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: 121.98 E-value: 1.25e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKslRQQLAYVS 431
Cdd:cd03301     1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK--DRDIAMVF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYLF-EGTIRDNIRYG------RPEATDAEVEEAARLAYAHDFISAQPQgyetpvgengvTLSGGQRQRLSIARALVR 504
Cdd:cd03301    79 QNYALYpHMTVYDNIAFGlklrkvPKDEIDERVREVAELLQIEHLLDRKPK-----------QLSGGQRQRVALGRAIVR 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582666899 505 NAPILLLDEATSALD------TESE-AAVQKALdeamsGRTVVVIAH-RLSTVVRADKIVVMQQGRVVEEG 567
Cdd:cd03301   148 EPKVFLMDEPLSNLDaklrvqMRAElKRLQQRL-----GTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213

LivG

COG0411

ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...

348-567

2.79e-31

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: 122.07 E-value: 2.79e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 348 TQARIEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAH-----ITkks 422
Cdd:COG0411     1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGlpphrIA--- 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 423 lRQQLAYVSQQPYLFEG-TIRDNI-----------------RYGRPEATDAEVEEAAR--------LAYAHdfisaqpqg 476
Cdd:COG0411    78 -RLGIARTFQNPRLFPElTVLENVlvaaharlgrgllaallRLPRARREEREARERAEellervglADRAD--------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 477 yeTPVGEngvtLSGGQRQRLSIARALVRNAPILLLDEATSAL-DTESEAAVQ--KALDEAMsGRTVVVIAHRLSTVVR-A 552
Cdd:COG0411   148 --EPAGN----LSYGQQRRLEIARALATEPKLLLLDEPAAGLnPEETEELAEliRRLRDER-GITILLIEHDMDLVMGlA 220

                         250
                  ....*....|....*
gi 1582666899 553 DKIVVMQQGRVVEEG 567
Cdd:COG0411   221 DRIVVLDFGRVIAEG 235

ABC_6TM_bac_exporter_ABCB8_10_like

cd18576

Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...

41-296

4.82e-31

Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ABCB10; This group includes putative bacterial ABC transporters similar to ABCB8 and ABCB10, which are found in the inner membrane of mitochondria, with the nucleotide-binding domains (NBDs) inside the mitochondrial matrix. Mammalian ABCB10 is essential for erythropoiesis and for protection of mitochondria against oxidative stress, while ABCB8 is essential for normal cardiac function, maintenance of mitochondrial iron homeostasis and maturation of cytosolic Fe/S proteins. Bacterial exporters are typically formed by dimers of TMD-NBD half-transporters. Thus, most bacterial ABC transporters are formed of two identical TMDs and two identical NBDs.

Pssm-ID: 350020 [Multi-domain] Cd Length: 289 Bit Score: 122.59 E-value: 4.82e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  41 CLIVVALSTAFT---AWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYAHLM 117
Cdd:cd18576     1 GLILLLLSSAIGlvfPLLAGQLIDAALGGGDTASLNQIALLLLGLFLLQAVFSFFRIYLFARVGERVVADLRKDLYRHLQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 118 TLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYVSKRL 197
Cdd:cd18576    81 RLPLSFFHERRVGELTSRLSNDVTQIQDTLTTTLAEFLRQILTLIGGVVLLFFISWKLTLLMLATVPVVVLVAVLFGRRI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 198 RSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSPLTESFAGFAVASVLAY 277
Cdd:cd18576   161 RKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLALKRARIRALFSSFIIFLLFGAIVAVLWY 240

                         250
                  ....*....|....*....
gi 1582666899 278 AAYRSIYFNVPPGAFFSFV 296
Cdd:cd18576   241 GGRLVLAGELTAGDLVAFL 259

metN

PRK11153

DL-methionine transporter ATP-binding subunit; Provisional

352-567

8.21e-31

DL-methionine transporter ATP-binding subunit; Provisional

Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 123.37 E-value: 8.21e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES----VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSL---R 424
Cdd:PRK11153    2 IELKNISKVFPQGGrtihALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELrkaR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 425 QQLAYVSQQPYLFEG-TIRDNIRY-----GRPEA-TDAEVEE---AARLAYAHDFISAQpqgyetpvgengvtLSGGQRQ 494
Cdd:PRK11153   82 RQIGMIFQHFNLLSSrTVFDNVALplelaGTPKAeIKARVTElleLVGLSDKADRYPAQ--------------LSGGQKQ 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582666899 495 RLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMS--GRTVVVIAHRLStVVR--ADKIVVMQQGRVVEEG 567
Cdd:PRK11153  148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMD-VVKriCDRVAVIDAGRLVEQG 223

ABC_membrane

pfam00664

ABC transporter transmembrane region; This family represents a unit of six transmembrane ...

36-297

1.16e-30

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: 120.83 E-value: 1.16e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  36 VFAIACLIVVALSTAFTAWIMRAIIDEAFANRRADVVWII--CLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLY 113
Cdd:pfam00664   2 ILAILLAILSGAISPAFPLVLGRILDVLLPDGDPETQALNvySLALLLLGLAQFILSFLQSYLLNHTGERLSRRLRRKLF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 114 AHLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYV 193
Cdd:pfam00664  82 KKILRQPMSFFDTNSVGELLSRLTNDTSKIRDGLGEKLGLLFQSLATIVGGIIVMFYYGWKLTLVLLAVLPLYILVSAVF 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 194 SKRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSPLTESFAGFAVAS 273
Cdd:pfam00664 162 AKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEALKAGIKKAVANGLSFGITQFIGYLSYAL 241

                         250       260
                  ....*....|....*....|....
gi 1582666899 274 VLAYAAYRSIYFNVPPGAFFSFVT 297
Cdd:pfam00664 242 ALWFGAYLVISGELSVGDLVAFLS 265

btuD

PRK09536

corrinoid ABC transporter ATPase; Reviewed

352-567

1.17e-30

corrinoid ABC transporter ATPase; Reviewed

Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 124.18 E-value: 1.17e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYVS 431
Cdd:PRK09536    4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYL-FEGTIRDNIRYGRP----------EATDAEVEEAARLAYAHDFIsaqpqgyETPVgengVTLSGGQRQRLSIAR 500
Cdd:PRK09536   84 QDTSLsFEFDVRQVVEMGRTphrsrfdtwtETDRAAVERAMERTGVAQFA-------DRPV----TSLSGGERQRVLLAR 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1582666899 501 ALVRNAPILLLDEATSALDTESE----AAVQKALDEamsGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:PRK09536  153 ALAQATPVLLLDEPTASLDINHQvrtlELVRRLVDD---GKTAVAAIHDLDLAARyCDELVLLADGRVRAAG 221

MglA

COG1129

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

348-568

1.27e-30

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

Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 125.52 E-value: 1.27e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 348 TQARIEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHIT-KKSLRQQ 426
Cdd:COG1129     1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDAQAAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 427 LAYVSQQPYLFEG-TIRDNIRYGRPEAT------DAEVEEAARLAYAHDF-ISAqpqgyETPVGEngvtLSGGQRQRLSI 498
Cdd:COG1129    81 IAIIHQELNLVPNlSVAENIFLGREPRRgglidwRAMRRRARELLARLGLdIDP-----DTPVGD----LSVAQQQLVEI 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582666899 499 ARALVRNAPILLLDEATSALdTESEAAVqkaLDEAM-----SGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGN 568
Cdd:COG1129   152 ARALSRDARVLILDEPTASL-TEREVER---LFRIIrrlkaQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGP 223

ABC_Carb_Monos_I

cd03216

First domain of the ATP-binding cassette component of monosaccharide transport system; This ...

352-564

1.63e-30

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: 117.14 E-value: 1.63e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHIT-KKSLRQQLAYV 430
Cdd:cd03216     1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAMV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 431 SQqpylfegtirdnirygrpeatdaeveeaarlayahdfisaqpqgyetpvgengvtLSGGQRQRLSIARALVRNAPILL 510
Cdd:cd03216    81 YQ-------------------------------------------------------LSVGERQMVEIARALARNARLLI 105

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1582666899 511 LDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVV 564
Cdd:cd03216   106 LDEPTAALTPAEVERLFKVIRRlRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVV 161

PRK10247

putative ABC transporter ATP-binding protein YbbL; Provisional

352-570

1.86e-30

putative ABC transporter ATP-binding protein YbbL; Provisional

Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 119.05 E-value: 1.86e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYVS 431
Cdd:PRK10247    8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCA 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYLFEGTIRDN------IRYGRPEAtDAEVEEAARLAYAhdfisaqpqgyETPVGENGVTLSGGQRQRLSIARALVRN 505
Cdd:PRK10247   88 QTPTLFGDTVYDNlifpwqIRNQQPDP-AIFLDDLERFALP-----------DTILTKNIAELSGGEKQRISLIRNLQFM 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1582666899 506 APILLLDEATSALDTESEAAVQKALDEAMSGRTVVVI--AHRLSTVVRADKIVVMQ-QGRVVEEGNHE 570
Cdd:PRK10247  156 PKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLwvTHDKDEINHADKVITLQpHAGEMQEARYE 223

Uup

COG0488

ATPase components of ABC transporters with duplicated ATPase domains [General function ...

307-568

2.04e-30

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

Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 125.18 E-value: 2.04e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 307 RRLARLQVQMERAVVNAR----------MIYELLDMEPRQRD------LPDARPL--TVtqarIEFRNVSFAYGNESVLS 368
Cdd:COG0488   257 KKIAKEEEFIRRFRAKARkakqaqsrikALEKLEREEPPRRDktveirFPPPERLgkKV----LELEGLSKSYGDKTLLD 332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 369 GVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIdGQDIahitkkslrqQLAYVSQ-QPYLFEG-TIRDNIR 446
Cdd:COG0488   333 DLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGYFDQhQEELDPDkTVLDELR 401

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 447 YGRPEATDAEVeeaarLAYAHDFISAQPQGYeTPVGengvTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAV 526
Cdd:COG0488   402 DGAPGGTEQEV-----RGYLGRFLFSGDDAF-KPVG----VLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEAL 471

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1582666899 527 QKALDEaMSGrTVVVIAH-R--LSTVvrADKIVVMQQGRVVE-EGN 568
Cdd:COG0488   472 EEALDD-FPG-TVLLVSHdRyfLDRV--ATRILEFEDGGVREyPGG 513

ABC_subfamily_A

cd03263

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...

352-567

2.34e-30

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.

Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 118.38 E-value: 2.34e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES--VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIaHITKKSLRQQLAY 429
Cdd:cd03263     1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSI-RTDRKAARQSLGY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 430 VSQQPYLFEG-TIRDNIRY-----GRPEAT-DAEVEEAARL----AYAHDFISaqpqgyetpvgengvTLSGGQRQRLSI 498
Cdd:cd03263    80 CPQFDALFDElTVREHLRFyarlkGLPKSEiKEEVELLLRVlgltDKANKRAR---------------TLSGGMKRKLSL 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 499 ARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTV-VRADKIVVMQQGRVVEEG 567
Cdd:cd03263   145 AIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAeALCDRIAIMSDGKLRCIG 214

ABC_6TM_exporter_like

cd18563

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...

36-323

3.26e-30

Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 120.31 E-value: 3.26e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  36 VFAIACLIVVALSTAFTAWIMRAIIDEAF----ANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRR 111
Cdd:cd18563     2 ILGFLLMLLGTALGLVPPYLTKILIDDVLiqlgPGGNTSLLLLLVLGLAGAYVLSALLGILRGRLLARLGERITADLRRD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 112 LYAHLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALR 191
Cdd:cd18563    82 LYEHLQRLSLSFFDKRQTGSLMSRVTSDTDRLQDFLSDGLPDFLTNILMIIGIGVVLFSLNWKLALLVLIPVPLVVWGSY 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 192 YVSKRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEE-ELER--KVNKLIKGAESRANRIarlSERTSPLTESFAG 268
Cdd:cd18563   162 FFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKrEIKRfdEANQELLDANIRAEKL---WATFFPLLTFLTS 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1582666899 269 FAVASVLAYAAYRSIYFNVPPGAFFSFVTALLLAYDPARRLARLQVQMERAVVNA 323
Cdd:cd18563   239 LGTLIVWYFGGRQVLSGTMTLGTLVAFLSYLGMFYGPLQWLSRLNNWITRALTSA 293

ABC_6TM_exporter_like

cd18778

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...

36-324

4.14e-30

Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 119.95 E-value: 4.14e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  36 VFAIACLIVVALSTAFTAWIMRAIIDEAF-ANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYA 114
Cdd:cd18778     2 ILTLLCALLSTLLGLVPPWLIRELVDLVTiGSKSLGLLLGLALLLLGAYLLRALLNFLRIYLNHVAEQKVVADLRSDLYD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 115 HLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYVS 194
Cdd:cd18778    82 KLQRLSLRYFDDRQTGDLMSRVINDVANVERLIADGIPQGITNVLTLVGVAIILFSINPKLALLTLIPIPFLALGAWLYS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 195 KRLRSATREavhlNSHVLGAM----QETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSPLTESFAGFA 270
Cdd:cd18778   162 KKVRPRYRK----VREALGELnallQDNLSGIREIQAFGREEEEAKRFEALSRRYRKAQLRAMKLWAIFHPLMEFLTSLG 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1582666899 271 VASVLAYAAYRSIYFNVPPGAFFSFVTALLLAYDPARRLARLQVQMERAVVNAR 324
Cdd:cd18778   238 TVLVLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALAGAE 291

dppF

PRK11308

dipeptide transporter ATP-binding subunit; Provisional

367-572

4.24e-30

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 120.84 E-value: 4.24e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 367 LSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIA---HITKKSLRQQLAYVSQQPY-------- 435
Cdd:PRK11308   31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNPYgslnprkk 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 436 ---LFEGTIRDNIRYGRPEATD------AEV----EEAARlaYAHDFisaqpqgyetpvgengvtlSGGQRQRLSIARAL 502
Cdd:PRK11308  111 vgqILEEPLLINTSLSAAERREkalammAKVglrpEHYDR--YPHMF-------------------SGGQRQRIAIARAL 169

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582666899 503 VRNAPILLLDEATSALDTESEAAV-------QKALdeamsGRTVVVIAHRLStVVR--ADKIVVMQQGRVVEEGNHETL 572
Cdd:PRK11308  170 MLDPDVVVADEPVSALDVSVQAQVlnlmmdlQQEL-----GLSYVFISHDLS-VVEhiADEVMVMYLGRCVEKGTKEQI 242

YejF

COG4172

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...

328-572

4.31e-30

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];

Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 124.41 E-value: 4.31e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 328 ELLDMEPRQRDLP---DARP-LTVTQARIEF--RNVSFAYGNESV--LSGVSFTAEGGATTALVGPSGAGKST----VIS 395
Cdd:COG4172   255 KLLAAEPRGDPRPvppDAPPlLEARDLKVWFpiKRGLFRRTVGHVkaVDGVSLTLRRGETLGLVGESGSGKSTlglaLLR 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 396 LIPRfydprEGEILIDGQDIAHITKK---SLRQQLAYVSQQPYlfeG------TIRDNIRYG----RPEATDAEVEEAAR 462
Cdd:COG4172   335 LIPS-----EGEIRFDGQDLDGLSRRalrPLRRRMQVVFQDPF---GslsprmTVGQIIAEGlrvhGPGLSAAERRARVA 406

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 463 LA-------------YAHDFisaqpqgyetpvgengvtlSGGQRQRLSIARALVRNAPILLLDEATSALDteseAAVQK- 528
Cdd:COG4172   407 EAleevgldpaarhrYPHEF-------------------SGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQAq 463

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1582666899 529 ------ALDEAMsGRTVVVIAHRLStVVRA--DKIVVMQQGRVVEEGNHETL 572
Cdd:COG4172   464 ildllrDLQREH-GLAYLFISHDLA-VVRAlaHRVMVMKDGKVVEQGPTEQV 513

ABC_BcrA_bacitracin_resist

cd03268

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...

352-567

4.90e-30

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: 117.32 E-value: 4.90e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHiTKKSLRQQLAYVS 431
Cdd:cd03268     1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQK-NIEALRRIGALIE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQ---PYLfegTIRDNIR-----YGRPEATDAEVEEAARL-AYAHDfisaqpqgyetPVGengvTLSGGQRQRLSIARAL 502
Cdd:cd03268    80 APgfyPNL---TARENLRllarlLGIRKKRIDEVLDVVGLkDSAKK-----------KVK----GFSLGMKQRLGIALAL 141

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582666899 503 VRNAPILLLDEATSALDTESEAAVQKAL-DEAMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:cd03268   142 LGNPDLLILDEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIQKvADRIGIINKGKLIEEG 208

cbiO

PRK13648

cobalt transporter ATP-binding subunit; Provisional

352-579

6.14e-30

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 118.70 E-value: 6.14e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAY-GNES-VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAY 429
Cdd:PRK13648    8 IVFKNVSFQYqSDASfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 430 VSQQP-YLFEGTI---------------RDNIRYGRPEAtdaeVEEAARLAYAHDfisaQPQgyetpvgengvTLSGGQR 493
Cdd:PRK13648   88 VFQNPdNQFVGSIvkydvafglenhavpYDEMHRRVSEA----LKQVDMLERADY----EPN-----------ALSGGQK 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 494 QRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGR--TVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHET 571
Cdd:PRK13648  149 QRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTE 228


                  ....*...
gi 1582666899 572 LAKVSDGL 579
Cdd:PRK13648  229 IFDHAEEL 236

ABC_NatA_sodium_exporter

cd03266

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...

352-567

3.92e-29

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: 115.16 E-value: 3.92e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES----VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHiTKKSLRQQL 427
Cdd:cd03266     2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 428 AYVSQQPYLFEG-TIRDNIRY-GR-----PEATDAEVEEAARLAYAHDFIsaqpqgyETPVGEngvtLSGGQRQRLSIAR 500
Cdd:cd03266    81 GFVSDSTGLYDRlTARENLEYfAGlyglkGDELTARLEELADRLGMEELL-------DRRVGG----FSTGMRQKVAIAR 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582666899 501 ALVRNAPILLLDEATSALDTESEAAVQKALDEAMS-GRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:cd03266   150 ALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRAlGKCILFSTHIMQEVERlCDRVVVLHRGRVVYEG 218

ABC_FtsE

cd03292

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...

352-568

5.45e-29

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: 114.43 E-value: 5.45e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESV-LSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKS---LRQQL 427
Cdd:cd03292     1 IEFINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 428 AYVSQQ-PYLFEGTIRDNIRYGRpEATDAEVEEAA-RLAYAHDFISAQPQGYETPVGengvtLSGGQRQRLSIARALVRN 505
Cdd:cd03292    81 GVVFQDfRLLPDRNVYENVAFAL-EVTGVPPREIRkRVPAALELVGLSHKHRALPAE-----LSGGEQQRVAIARAIVNS 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1582666899 506 APILLLDEATSALDTESEAAVQKALDEA-MSGRTVVVIAHrlstvvrADKIVVMQQGRVVEEGN 568
Cdd:cd03292   155 PTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATH-------AKELVDTTRHRVIALER 211

cbiO

PRK13635

energy-coupling factor ABC transporter ATP-binding protein;

352-579

6.77e-29

energy-coupling factor ABC transporter ATP-binding protein;

Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 116.27 E-value: 6.77e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES--VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAY 429
Cdd:PRK13635    6 IRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQVGM 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 430 VSQQP-YLFEG-TIRDNIRYG-------RPEATDaEVEEAARLAYAHDFISAQPQgyetpvgengvTLSGGQRQRLSIAR 500
Cdd:PRK13635   86 VFQNPdNQFVGaTVQDDVAFGlenigvpREEMVE-RVDQALRQVGMEDFLNREPH-----------RLSGGQKQRVAIAG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 501 ALVRNAPILLLDEATSALD----TESEAAVQKALDEamSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAKVS 576
Cdd:PRK13635  154 VLALQPDIIILDEATSMLDprgrREVLETVRQLKEQ--KGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEIFKSG 231


                  ...
gi 1582666899 577 DGL 579
Cdd:PRK13635  232 HML 234

PRK14247

phosphate ABC transporter ATP-binding protein; Provisional

349-567

7.78e-29

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 115.01 E-value: 7.78e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 349 QARIEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVIS----LIPRFYDPR-EGEILIDGQDIAHITKKSL 423
Cdd:PRK14247    1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfnrLIELYPEARvSGEVYLDGQDIFKMDVIEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 424 RQQLAYVSQQPYLFEG-TIRDNIRYG----RPEATDAEVEEAARLAYAHDFISAQPQG-YETPVGEngvtLSGGQRQRLS 497
Cdd:PRK14247   81 RRRVQMVFQIPNPIPNlSIFENVALGlklnRLVKSKKELQERVRWALEKAQLWDEVKDrLDAPAGK----LSGGQQQRLC 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582666899 498 IARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:PRK14247  157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARiSDYVAFLYKGQIVEWG 227

ABC_CysA_sulfate_importer

cd03296

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...

352-567

3.97e-28

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: 112.82 E-value: 3.97e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKslRQQLAYVS 431
Cdd:cd03296     3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYLFEG-TIRDNIRYG--------RPEAT--DAEVEEAARLAYAHDFISAQPQgyetpvgengvTLSGGQRQRLSIAR 500
Cdd:cd03296    81 QHYALFRHmTVFDNVAFGlrvkprseRPPEAeiRAKVHELLKLVQLDWLADRYPA-----------QLSGGQRQRVALAR 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582666899 501 ALVRNAPILLLDEATSALDteseAAVQKAL--------DEAmsGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:cd03296   150 ALAVEPKVLLLDEPFGALD----AKVRKELrrwlrrlhDEL--HVTTVFVTHDQEEALEvADRVVVMNKGRIEQVG 219

YddA

COG4178

ABC-type uncharacterized transport system, permease and ATPase components [General function ...

290-561

4.13e-28

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

Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 118.76 E-value: 4.13e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 290 GAFFSFVTALLLAYDPARRLARLqvqmeRAVVNaRmIYELLD-ME-PRQRDLPDARPLTVTQARIEFRNVSFAYGNESVL 367
Cdd:COG4178   306 SAFGQVQGALSWFVDNYQSLAEW-----RATVD-R-LAGFEEaLEaADALPEAASRIETSEDGALALEDLTLRTPDGRPL 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 368 -SGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILI-DGQDIAhitkkslrqqlaYVSQQPYLFEGTIRDNI 445
Cdd:COG4178   379 lEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVL------------FLPQRPYLPLGTLREAL 446

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 446 RYGRPEA--TDAEVEEA---ARLAYAHDFISAQpqgyetpvgEN-GVTLSGGQRQRLSIARALVRNAPILLLDEATSALD 519
Cdd:COG4178   447 LYPATAEafSDAELREAleaVGLGHLAERLDEE---------ADwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1582666899 520 TESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQG 561
Cdd:COG4178   518 EENEAALYQLLREELPGTTVISVGHRSTLAAFHDRVLELTGD 559

ABC_6TM_Rv0194_D2_like

cd18546

Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ...

36-312

4.16e-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: 4.16e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  36 VFAIACLIVVALSTAFTAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYAH 115
Cdd:cd18546     2 ALALLLVVVDTAASLAGPLLVRYGIDSGVRAGDLGVLLLAAAAYLAVVLAGWVAQRAQTRLTGRTGERLLYDLRLRVFAH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 116 LMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRY--- 192
Cdd:cd18546    82 LQRLSLDFHERETSGRIMTRMTSDIDALSELLQTGLVQLVVSLLTLVGIAVVLLVLDPRLALVALAALPPLALATRWfrr 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 193 VSKRLRSATREAVhlnSHVLGAMQETIQGIAIVKAFTMEEELERKVnklikGAESRANRIARL-SERTS----PLTESFA 267
Cdd:cd18546   162 RSSRAYRRARERI---AAVNADLQETLAGIRVVQAFRRERRNAERF-----AELSDDYRDARLrAQRLVaiyfPGVELLG 233

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1582666899 268 GFAVASVLAYAAYRSIYFNVPPGAFFSFVTALLLAYDPARRLARL 312
Cdd:cd18546   234 NLATAAVLLVGAWRVAAGTLTVGVLVAFLLYLRRFFAPIQQLSQV 278

ABCC_SUR1_N

cd03290

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...

359-561

6.31e-28

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.

Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 111.65 E-value: 6.31e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 359 FAYG-NESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEIL----IDGQDIAHITKKSLRQQLAYVSQQ 433
Cdd:cd03290     8 FSWGsGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnkNESEPSFEATRSRNRYSVAYAAQK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 434 PYLFEGTIRDNIRYGRP--EATDAEVEEAARLAYAHDFIsaqPQGYETPVGENGVTLSGGQRQRLSIARALVRNAPILLL 511
Cdd:cd03290    88 PWLLNATVEENITFGSPfnKQRYKAVTDACSLQPDIDLL---PFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 512 DEATSALDTE-SEAAVQKALDEAMSG--RTVVVIAHRLSTVVRADKIVVMQQG 561
Cdd:cd03290   165 DDPFSALDIHlSDHLMQEGILKFLQDdkRTLVLVTHKLQYLPHADWIIAMKDG 217

thiQ

TIGR01277

thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...

371-563

6.73e-28

thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]

Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 111.49 E-value: 6.73e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 371 SFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDiaHITKKSLRQQLAYVSQQPYLFEG-TIRDNIRYG- 448
Cdd:TIGR01277  18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQS--HTGLAPYQRPVSMLFQENNLFAHlTVRQNIGLGl 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 449 ----RPEATDAE-VEEAARLAYAHDFISAQPQgyetpvgengvTLSGGQRQRLSIARALVRNAPILLLDEATSALD---- 519
Cdd:TIGR01277  96 hpglKLNAEQQEkVVDAAQQVGIADYLDRLPE-----------QLSGGQRQRVALARCLVRPNPILLLDEPFSALDpllr 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1582666899 520 TESEAAVQKALDEamSGRTVVVIAHRLSTVVR-ADKIVVMQQGRV 563
Cdd:TIGR01277 165 EEMLALVKQLCSE--RQRTLLMVTHHLSDARAiASQIAVVSQGKI 207

LivF

COG0410

ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...

353-573

1.05e-27

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: 111.61 E-value: 1.05e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 353 EFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHI-TKKSLRQQLAYVS 431
Cdd:COG0410     5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLpPHRIARLGIGYVP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYLFEG-TIRDNIRYGRPEATDAEvEEAARLAYAHDF------ISAQPQGyetpvgengvTLSGGQRQRLSIARALVR 504
Cdd:COG0410    85 EGRRIFPSlTVEENLLLGAYARRDRA-EVRADLERVYELfprlkeRRRQRAG----------TLSGGEQQMLAIGRALMS 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1582666899 505 NAPILLLDEATSALD----TESEAAVQKALDEamsGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHETLA 573
Cdd:COG0410   154 RPKLLLLDEPSLGLAplivEEIFEIIRRLNRE---GVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAELL 224

cbiO

PRK13647

cobalt transporter ATP-binding subunit; Provisional

352-573

1.71e-27

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 112.14 E-value: 1.71e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAY--GNESvLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAY 429
Cdd:PRK13647    5 IEVEDLHFRYkdGTKA-LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 430 VSQQP--YLFEGTIRDNIRYG------RPEATDAEVEEAARLAYAHDFISAQPQgyetpvgengvTLSGGQRQRLSIARA 501
Cdd:PRK13647   84 VFQDPddQVFSSTVWDDVAFGpvnmglDKDEVERRVEEALKAVRMWDFRDKPPY-----------HLSYGQKKRVAIAGV 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1582666899 502 LVRNAPILLLDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHETLA 573
Cdd:PRK13647  153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRlHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDKSLLT 226

ABC_ThiQ_thiamine_transporter

cd03298

ATP-binding cassette domain of the thiamine transport system; Part of the ...

352-567

1.90e-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: 109.89 E-value: 1.90e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFtaEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKslRQQLAYVS 431
Cdd:cd03298     1 VRLDKIRFSYGEQPMHFDLTF--AQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLF 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYLFEG-TIRDNIRYGRPEAT--DAEVEEAARLAYAHDFIsaqpQGYETPVGEngvTLSGGQRQRLSIARALVRNAPI 508
Cdd:cd03298    77 QENNLFAHlTVEQNVGLGLSPGLklTAEDRQAIEVALARVGL----AGLEKRLPG---ELSGGERQRVALARVLVRDKPV 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1582666899 509 LLLDEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:cd03298   150 LLLDEPFAALDPALRAEMLDLVLDlhAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211

PTZ00243

ABC transporter; Provisional

366-583

2.71e-27

ABC transporter; Provisional

Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 117.96 E-value: 2.71e-27

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  366 VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDgqdiahitkkslrQQLAYVSQQPYLFEGTIRDNI 445
Cdd:PTZ00243   675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNI 741

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  446 RYGRPEATdAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTE-SEA 524
Cdd:PTZ00243   742 LFFDEEDA-ARLADAVRVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAHvGER 820

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1582666899  525 AVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAKVSdgLYARL 583
Cdd:PTZ00243   821 VVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMRTS--LYATL 877

cbiO

PRK13650

energy-coupling factor transporter ATPase;

352-563

3.00e-27

energy-coupling factor transporter ATPase;

Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 111.36 E-value: 3.00e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES---VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLA 428
Cdd:PRK13650    5 IEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 429 YVSQQP-YLFEG-TIRDNIRYGRP------EATDAEVEEAARLAYAHDFISAQPqgyetpvgengVTLSGGQRQRLSIAR 500
Cdd:PRK13650   85 MVFQNPdNQFVGaTVEDDVAFGLEnkgiphEEMKERVNEALELVGMQDFKEREP-----------ARLSGGQKQRVAIAG 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582666899 501 ALVRNAPILLLDEATSALDTESE----AAVQKALDEamSGRTVVVIAHRLSTVVRADKIVVMQQGRV 563
Cdd:PRK13650  154 AVAMRPKIIILDEATSMLDPEGRleliKTIKGIRDD--YQMTVISITHDLDEVALSDRVLVMKNGQV 218

PRK14243

phosphate transporter ATP-binding protein; Provisional

342-568

4.51e-27

phosphate transporter ATP-binding protein; Provisional

Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 110.64 E-value: 4.51e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 342 ARPLTVTQARIEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVI-------SLIPRFYdpREGEILIDGQD 414
Cdd:PRK14243    1 TSTLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlnDLIPGFR--VEGKVTFHGKN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 415 I--AHITKKSLRQQLAYVSQQPYLFEGTIRDNIRYGrPEAT------DAEVEEAARLAYAHDFISAQpqgyetpVGENGV 486
Cdd:PRK14243   79 LyaPDVDPVEVRRRIGMVFQKPNPFPKSIYDNIAYG-ARINgykgdmDELVERSLRQAALWDEVKDK-------LKQSGL 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 487 TLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEE 566
Cdd:PRK14243  151 SLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAFFNVELTEG 230


                  ..
gi 1582666899 567 GN 568
Cdd:PRK14243  231 GG 232

cbiO

PRK13639

cobalt transporter ATP-binding subunit; Provisional

352-567

5.47e-27

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 110.55 E-value: 5.47e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES-VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHiTKKSL---RQQL 427
Cdd:PRK13639    2 LETRDLKYSYPDGTeALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKY-DKKSLlevRKTV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 428 AYVSQQP--YLFEGTIRDNIRYG------RPEATDAEVEEAARLAYAHDFISAQPQgyetpvgengvTLSGGQRQRLSIA 499
Cdd:PRK13639   81 GIVFQNPddQLFAPTVEEDVAFGplnlglSKEEVEKRVKEALKAVGMEGFENKPPH-----------HLSGGQKKRVAIA 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 500 RALVRNAPILLLDEATSALDTESEAAVQKALDEA-MSGRTVVVIAHRLSTV-VRADKIVVMQQGRVVEEG 567
Cdd:PRK13639  150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEG 219

PRK10575

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

348-572

7.16e-27

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

Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 109.88 E-value: 7.16e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 348 TQARIEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQL 427
Cdd:PRK10575    8 SDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 428 AYVSQQPYLFEG-TIRDNI---RY------GRPEATDAE-VEEAARLA----YAHDFISaqpqgyetpvgengvTLSGGQ 492
Cdd:PRK10575   88 AYLPQQLPAAEGmTVRELVaigRYpwhgalGRFGAADREkVEEAISLVglkpLAHRLVD---------------SLSGGE 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 493 RQRLSIARALVRNAPILLLDEATSALDTESEAAVQkALDEAMS---GRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGN 568
Cdd:PRK10575  153 RQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVL-ALVHRLSqerGLTVIAVLHDINMAARyCDYLVALRGGEMIAQGT 231


                  ....
gi 1582666899 569 HETL 572
Cdd:PRK10575  232 PAEL 235

PRK14239

phosphate transporter ATP-binding protein; Provisional

348-568

7.88e-27

phosphate transporter ATP-binding protein; Provisional

Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 109.48 E-value: 7.88e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 348 TQARIEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYD--PR---EGEILIDGQDIAHITKKS 422
Cdd:PRK14239    2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIYSPRTDT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 423 --LRQQLAYVSQQPYLFEGTIRDNIRYG-------RPEATDAEVEEAARLAYAHDFISAQpqgyetpVGENGVTLSGGQR 493
Cdd:PRK14239   82 vdLRKEIGMVFQQPNPFPMSIYENVVYGlrlkgikDKQVLDEAVEKSLKGASIWDEVKDR-------LHDSALGLSGGQQ 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582666899 494 QRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGN 568
Cdd:PRK14239  155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRiSDRTGFFLDGDLIEYND 230

thiQ

PRK10771

thiamine ABC transporter ATP-binding protein ThiQ;

371-572

1.63e-26

thiamine ABC transporter ATP-binding protein ThiQ;

Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 108.13 E-value: 1.63e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 371 SFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDiaHITKKSLRQQLAYVSQQPYLFEG-TIRDNIRYG- 448
Cdd:PRK10771   19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD--HTTTPPSRRPVSMLFQENNLFSHlTVAQNIGLGl 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 449 RP-----EATDAEVEEAARLAYAHDFISAQPqgyetpvGEngvtLSGGQRQRLSIARALVRNAPILLLDEATSALDTESE 523
Cdd:PRK10771   97 NPglklnAAQREKLHAIARQMGIEDLLARLP-------GQ----LSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1582666899 524 AAVQKALDEAMSGR--TVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHETL 572
Cdd:PRK10771  166 QEMLTLVSQVCQERqlTLLMVSHSLEDAARiAPRSLVVADGRIAWDGPTDEL 217

ModF

COG1119

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...

352-567

1.84e-26

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: 108.25 E-value: 1.84e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREG-EILIDGQDIAHITKKSLRQQLAYV 430
Cdd:COG1119     4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRIGLV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 431 S---QQPYLFEGTIRDNIRYGR-------PEATDAEVEEAARL-------AYAhdfisaqpqgyETPVGengvTLSGGQR 493
Cdd:COG1119    84 SpalQLRFPRDETVLDVVLSGFfdsiglyREPTDEQRERARELlellglaHLA-----------DRPFG----TLSQGEQ 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582666899 494 QRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRLSTVVRA-DKIVVMQQGRVVEEG 567
Cdd:COG1119   149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKlaAEGAPTLVLVTHHVEEIPPGiTHVLLLKDGRVVAAG 225

PhnL

COG4778

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...

366-562

2.08e-26

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: 107.52 E-value: 2.08e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 366 VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQ----DIAHITKK---SLRQQ-LAYVSQ----- 432
Cdd:COG4778    26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPReilALRRRtIGYVSQflrvi 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 433 ----------QPYLFEGTirdniryGRPEAtDAEVEEA-ARLAYAHDFISAQPqgyetpvgengVTLSGGQRQRLSIARA 501
Cdd:COG4778   106 prvsaldvvaEPLLERGV-------DREEA-RARARELlARLNLPERLWDLPP-----------ATFSGGEQQRVNIARG 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 502 LVRNAPILLLDEATSALDTESEAAVQKALDEAM-SGRTVVVIAHRLSTVVR-ADKIVVMQQGR 562
Cdd:COG4778   167 FIADPPLLLLDEPTASLDAANRAVVVELIEEAKaRGTAIIGIFHDEEVREAvADRVVDVTPFS 229

PRK14258

phosphate ABC transporter ATP-binding protein; Provisional

352-551

2.51e-26

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 108.20 E-value: 2.51e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDpREGEILIDG------QDI--AHITKKSL 423
Cdd:PRK14258    8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNE-LESEVRVEGrveffnQNIyeRRVNLNRL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 424 RQQLAYVSQQPYLFEGTIRDNIRYG------RPEAT-DAEVEEAARLAYAHDFISAQpqgyetpVGENGVTLSGGQRQRL 496
Cdd:PRK14258   87 RRQVSMVHPKPNLFPMSVYDNVAYGvkivgwRPKLEiDDIVESALKDADLWDEIKHK-------IHKSALDLSGGQQQRL 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1582666899 497 SIARALVRNAPILLLDEATSALDTESEAAVQKALDEAM--SGRTVVVIAHRLSTVVR 551
Cdd:PRK14258  160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlrSELTMVIVSHNLHQVSR 216

NupO

COG3845

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...

348-574

2.71e-26

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

Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 112.81 E-value: 2.71e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 348 TQARIEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIaHIT--KKSLRQ 425
Cdd:COG3845     2 MPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV-RIRspRDAIAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 426 QLAYVSQQPYLFEG-TIRDNIRYGRPEA------TDAEVEEAARLAYAHDFiSAQPqgyETPVGEngvtLSGGQRQRLSI 498
Cdd:COG3845    81 GIGMVHQHFMLVPNlTVAENIVLGLEPTkggrldRKAARARIRELSERYGL-DVDP---DAKVED----LSVGEQQRVEI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 499 ARALVRNAPILLLDEATSALdTESEA----AVQKALdeAMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG-----N 568
Cdd:COG3845   153 LKALYRGARILILDEPTAVL-TPQEAdelfEILRRL--AAEGKSIIFITHKLREVMAiADRVTVLRRGKVVGTVdtaetS 229


                  ....*.
gi 1582666899 569 HETLAK 574
Cdd:COG3845   230 EEELAE 235

ABC_6TM_LmrA_like

cd18551

Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...

36-281

3.07e-26

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: 108.67 E-value: 3.07e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  36 VFAIACLIVVALSTAFTAWIMRAIIDEAFANR-RADVVWIICLSIFIAFVLRGFASYgqavALSKVGNDIVARYQRRLYA 114
Cdd:cd18551     2 ILALLLSLLGTAASLAQPLLVKNLIDALSAGGsSGGLLALLVALFLLQAVLSALSSY----LLGRTGERVVLDLRRRLWR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 115 HLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYVS 194
Cdd:cd18551    78 RLLRLPVSFFDRRRSGDLVSRVTNDTTLLRELITSGLPQLVTGVLTVVGAVVLMFLLDWVLTLVTLAVVPLAFLIILPLG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 195 KRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSPLTESFAGFAVASV 274
Cdd:cd18551   158 RRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAERLYRAGLKAAKIEALIGPLMGLAVQLALLVV 237


                  ....*..
gi 1582666899 275 LAYAAYR 281
Cdd:cd18551   238 LGVGGAR 244

potG

PRK11607

putrescine ABC transporter ATP-binding subunit PotG;

331-570

4.84e-26

putrescine ABC transporter ATP-binding subunit PotG;

Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 110.31 E-value: 4.84e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 331 DMEPRqrdlPDARPLTVTQARIEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILI 410
Cdd:PRK11607    3 DAIPR----PQAKTRKALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIML 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 411 DGQDIAHItkKSLRQQLAYVSQQPYLF-EGTIRDNIRYG-------RPEATDaEVEEAARLAYAHDFISAQPQgyetpvg 482
Cdd:PRK11607   79 DGVDLSHV--PPYQRPINMMFQSYALFpHMTVEQNIAFGlkqdklpKAEIAS-RVNEMLGLVHMQEFAKRKPH------- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 483 engvTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMS--GRTVVVIAH-RLSTVVRADKIVVMQ 559
Cdd:PRK11607  149 ----QLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILErvGVTCVMVTHdQEEAMTMAGRIAIMN 224

                         250
                  ....*....|.
gi 1582666899 560 QGRVVEEGNHE 570
Cdd:PRK11607  225 RGKFVQIGEPE 235

modC_ABC

TIGR02142

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...

370-592

7.00e-26

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]

Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 109.05 E-value: 7.00e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 370 VSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSL----RQQLAYVSQQPYLFEG-TIRDN 444
Cdd:TIGR02142  16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFlppeKRRIGYVFQEARLFPHlSVRGN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 445 IRYG----RPEATDAEVEEAARLAyahdfisaqpqGYETPVGENGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDT 520
Cdd:TIGR02142  96 LRYGmkraRPSERRISFERVIELL-----------GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDD 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582666899 521 ESEAAVQKALDE--AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHETLAKVSDglyarLNNLQRPSAS 592
Cdd:TIGR02142 165 PRKYEILPYLERlhAEFGIPILYVSHSLQEVLRlADRVVVLEDGRVAAAGPIAEVWASPD-----LPWLAREDQG 234

ABC_YhbG

cd03218

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...

352-573

7.72e-26

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: 106.09 E-value: 7.72e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHIT-KKSLRQQLAYV 430
Cdd:cd03218     1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmHKRARLGIGYL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 431 SQQPYLFEG-TIRDNIRYGRPEATDAEVEEAARLAYA-HDFisaqpqGYETPVGENGVTLSGGQRQRLSIARALVRNAPI 508
Cdd:cd03218    81 PQEASIFRKlTVEENILAVLEIRGLSKKEREEKLEELlEEF------HITHLRKSKASSLSGGERRRVEIARALATNPKF 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582666899 509 LLLDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLS-TVVRADKIVVMQQGRVVEEGNHETLA 573
Cdd:cd03218   155 LLLDEPFAGVDPIAVQDIQKIIKIlKDRGIGVLITDHNVReTLSITDRAYIIYEGKVLAEGTPEEIA 221

PvdE

COG4615

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...

29-573

1.08e-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: 111.04 E-value: 1.08e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  29 RDHLWGYVFAIACLIVVALSTAFT-AWIMRAIIDEAFANRRadVVWIICLSIFIAFVLRGFASygqaVALSKVGNDIVAR 107
Cdd:COG4615     9 RESRWLLLLALLLGLLSGLANAGLiALINQALNATGAALAR--LLLLFAGLLVLLLLSRLASQ----LLLTRLGQHAVAR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 108 YQRRLYAHLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLtITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLL 187
Cdd:COG4615    83 LRLRLSRRILAAPLERLERIGAARLLAALTEDVRTISQAFVR-LPELLQSVALVLGCLAYLAWLSPPLFLLTLVLLGLGV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 188 YALRYVSKRLRSATREAVHLNSHVLGAMQETIQGIAIVK-------AFtMEEELERKVNKlIKGAESRANRIARLSERts 260
Cdd:COG4615   162 AGYRLLVRRARRHLRRAREAEDRLFKHFRALLEGFKELKlnrrrrrAF-FDEDLQPTAER-YRDLRIRADTIFALANN-- 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 261 pLTESFAGFAVASVLAYAAyrsIYFNVPPGAFFSFVTALLLAYDPARRLARLQVQMERAVVNARMIYEL-LDMEPRQRDL 339
Cdd:COG4615   238 -WGNLLFFALIGLILFLLP---ALGWADPAVLSGFVLVLLFLRGPLSQLVGALPTLSRANVALRKIEELeLALAAAEPAA 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 340 PDARPLTVTQA--RIEFRNVSFAYGNESVLSG-----VSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDG 412
Cdd:COG4615   314 ADAAAPPAPADfqTLELRGVTYRYPGEDGDEGftlgpIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDG 393

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 413 QDIAHITKKSLRQQLAYVSQQPYLFEGTirdnirYGRP-EATDAEVEE-AARLAYAHdfisaqpqgyETPVGENGVT--- 487
Cdd:COG4615   394 QPVTADNREAYRQLFSAVFSDFHLFDRL------LGLDgEADPARARElLERLELDH----------KVSVEDGRFSttd 457

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 488 LSGGQRQRLSIARALVRNAPILLLDEAtsaldteseAAVQ----------------KALdeamsGRTVVVIAH--RLSTV 549
Cdd:COG4615   458 LSQGQRKRLALLVALLEDRPILVFDEW---------AADQdpefrrvfytellpelKAR-----GKTVIAISHddRYFDL 523

                         570       580
                  ....*....|....*....|....
gi 1582666899 550 vrADKIVVMQQGRVVEEGNHETLA 573
Cdd:COG4615   524 --ADRVLKMDYGKLVELTGPAALA 545

ABC_6TM_Rv0194_D1_like

cd18543

Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ...

36-319

1.16e-25

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: 107.18 E-value: 1.16e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  36 VFAIACLIVVALSTAFTAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYAH 115
Cdd:cd18543     2 ILALLAALLATLAGLAIPLLTRRAIDGPIAHGDRSALWPLVLLLLALGVAEAVLSFLRRYLAGRLSLGVEHDLRTDLFAH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 116 LMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITsTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYVSK 195
Cdd:cd18543    82 LQRLDGAFHDRWQSGQLLSRATSDLSLVQRFLAFGPF-LLGNLLTLVVGLVVMLVLSPPLALVALASLPPLVLVARRFRR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 196 RLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSPLTESFAGFAVASVL 275
Cdd:cd18543   161 RYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRFEAAARRLRATRLRAARLRARFWPLLEALPELGLAAVL 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1582666899 276 AYAAYRSIYFNVPPGAFFSFVTALLLAYDPARRLARLQVQMERA 319
Cdd:cd18543   241 ALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRA 284

ModC

COG4148

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...

370-573

1.16e-25

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: 108.65 E-value: 1.16e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 370 VSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDG---QDIAhiTKKSL---RQQLAYVSQQPYLFEG-TIR 442
Cdd:COG4148    18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSA--RGIFLpphRRRIGYVFQEARLFPHlSVR 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 443 DNIRYGRPEATDAEveEAARLAYAHDF--ISA----QPQgyetpvgengvTLSGGQRQRLSIARALVRNAPILLLDEATS 516
Cdd:COG4148    96 GNLLYGRKRAPRAE--RRISFDEVVELlgIGHlldrRPA-----------TLSGGERQRVAIGRALLSSPRLLLMDEPLA 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1582666899 517 ALDTESEAAVQKALdEAMSGRT---VVVIAHRLSTVVR-ADKIVVMQQGRVVEEGN-HETLA 573
Cdd:COG4148   163 ALDLARKAEILPYL-ERLRDELdipILYVSHSLDEVARlADHVVLLEQGRVVASGPlAEVLS 223

CFTR_protein

TIGR01271

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...

366-561

1.56e-25

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: 112.31 E-value: 1.56e-25

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  366 VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEIlidgqdiahitKKSLRqqLAYVSQQPYLFEGTIRDNI 445
Cdd:TIGR01271  441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-----------KHSGR--ISFSPQTSWIMPGTIKDNI 507

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  446 RYGRP--EATDAEVEEAARLayaHDFISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESE 523
Cdd:TIGR01271  508 IFGLSydEYRYTSVIKACQL---EEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1582666899  524 AAV-QKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQG 561
Cdd:TIGR01271  585 KEIfESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEG 623

cbiO

PRK13646

energy-coupling factor transporter ATPase;

352-572

1.94e-25

energy-coupling factor transporter ATPase;

Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 106.40 E-value: 1.94e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES-----VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITK----KS 422
Cdd:PRK13646    3 IRFDNVSYTYQKGTpyehqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyiRP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 423 LRQQLAYVSQQP--YLFEGTIRDNIRYGrPEATDAEVEEAArlAYAHDFIsaQPQGYETPVGENG-VTLSGGQRQRLSIA 499
Cdd:PRK13646   83 VRKRIGMVFQFPesQLFEDTVEREIIFG-PKNFKMNLDEVK--NYAHRLL--MDLGFSRDVMSQSpFQMSGGQMRKIAIV 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582666899 500 RALVRNAPILLLDEATSALDTESEAAVQKALDEAM--SGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHETL 572
Cdd:PRK13646  158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARyADEVIVMKEGSIVSQTSPKEL 233

AztA

NF040873

zinc ABC transporter ATP-binding protein AztA;

360-558

2.05e-25

zinc ABC transporter ATP-binding protein AztA;

Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 103.47 E-value: 2.05e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 360 AYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGqdiahitkkslRQQLAYVSQQ---PYL 436
Cdd:NF040873    1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG-----------GARVAYVPQRsevPDS 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 437 FEGTIRDNIRYG---------RPEATD-AEVEEAARLAYAHDFISAQPQgyetpvgengvTLSGGQRQRLSIARALVRNA 506
Cdd:NF040873   70 LPLTVRDLVAMGrwarrglwrRLTRDDrAAVDDALERVGLADLAGRQLG-----------ELSGGQRQRALLAQGLAQEA 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 507 PILLLDEATSALDTESEAAVQKAL-DEAMSGRTVVVIAHRLSTVVRADKIVVM 558
Cdd:NF040873  139 DLLLLDEPTTGLDAESRERIIALLaEEHARGATVVVVTHDLELVRRADPCVLL 191

ABC_ModC_molybdenum_transporter

cd03297

ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...

370-567

2.17e-25

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: 104.30 E-value: 2.17e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 370 VSFTAEGGaTTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQdIAHITKKSL-----RQQLAYVSQQPYLFEG-TIRD 443
Cdd:cd03297    17 IDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGT-VLFDSRKKInlppqQRKIGLVFQQYALFPHlNVRE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 444 NIRYGRPEATDAE--VEEAARLAYAHdfisAQPQGYETPVgengvTLSGGQRQRLSIARALVRNAPILLLDEATSALDTE 521
Cdd:cd03297    95 NLAFGLKRKRNREdrISVDELLDLLG----LDHLLNRYPA-----QLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1582666899 522 SEAAVQKALDEAMS--GRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:cd03297   166 LRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214

ABC_6TM_TAP_ABCB8_10_like

cd18557

Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...

38-296

3.27e-25

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: 105.72 E-value: 3.27e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  38 AIACLIVVALSTAFTAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYAHLM 117
Cdd:cd18557     1 GLLFLLISSAAQLLLPYLIGRLIDTIIKGGDLDVLNELALILLAIYLLQSVFTFVRYYLFNIAGERIVARLRRDLFSSLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 118 TLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYVSKRL 197
Cdd:cd18557    81 RQEIAFFDKHKTGELTSRLSSDTSVLQSAVTDNLSQLLRNILQVIGGLIILFILSWKLTLVLLLVIPLLLIASKIYGRYI 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 198 RSATR---EAVHLNSHVLgamQETIQGIAIVKAFTMEEELERKVNKLIkgaeSRANRIARLSERTSPLTESFAGF----A 270
Cdd:cd18557   161 RKLSKevqDALAKAGQVA---EESLSNIRTVRSFSAEEKEIRRYSEAL----DRSYRLARKKALANALFQGITSLliylS 233

                         250       260
                  ....*....|....*....|....*.
gi 1582666899 271 VASVLAYAAYRSIYFNVPPGAFFSFV 296
Cdd:cd18557   234 LLLVLWYGGYLVLSGQLTVGELTSFI 259

cbiO

PRK13649

energy-coupling factor transporter ATPase;

352-567

4.02e-25

energy-coupling factor transporter ATPase;

Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 105.21 E-value: 4.02e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES-----VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITK----KS 422
Cdd:PRK13649    3 INLQNVSYTYQAGTpfegrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 423 LRQQLAYVSQQP--YLFEGTIRDNIRYGrPEATDAEVEEAARLA---YAHDFISaqpqgyETPVGENGVTLSGGQRQRLS 497
Cdd:PRK13649   83 IRKKVGLVFQFPesQLFEETVLKDVAFG-PQNFGVSQEEAEALArekLALVGIS------ESLFEKNPFELSGGQMRRVA 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1582666899 498 IARALVRNAPILLLDEATSALDTESEAAVQ---KALDEamSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:PRK13649  156 IAGILAMEPKILVLDEPTAGLDPKGRKELMtlfKKLHQ--SGMTIVLVTHLMDDVANyADFVYVLEKGKLVLSG 227

ABC_6TM_Tm288_like

cd18547

Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...

36-297

4.26e-25

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: 105.56 E-value: 4.26e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  36 VFAIACLIVVALSTAFTAWIMRAIIDEAFANRRA------DVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQ 109
Cdd:cd18547     2 ILVIILAIISTLLSVLGPYLLGKAIDLIIEGLGGgggvdfSGLLRILLLLLGLYLLSALFSYLQNRLMARVSQRTVYDLR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 110 RRLYAHLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYA 189
Cdd:cd18547    82 KDLFEKLQRLPLSYFDTHSHGDIMSRVTNDVDNISQALSQSLTQLISSILTIVGTLIMMLYISPLLTLIVLVTVPLSLLV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 190 LRYVSKRLR---SATREAV-HLNSHVlgamQETIQGIAIVKAFTMEEELE---RKVNKLIKGAESRANRIARLserTSPL 262
Cdd:cd18547   162 TKFIAKRSQkyfRKQQKALgELNGYI----EEMISGQKVVKAFNREEEAIeefDEINEELYKASFKAQFYSGL---LMPI 234

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1582666899 263 TESFAGFAVASVLAYAAYRSIYFNVPPGAFFSFVT 297
Cdd:cd18547   235 MNFINNLGYVLVAVVGGLLVINGALTVGVIQAFLQ 269

cbiO

PRK13641

energy-coupling factor transporter ATPase;

352-592

4.84e-25

energy-coupling factor transporter ATPase;

Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 105.30 E-value: 4.84e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESV-----LSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITK----KS 422
Cdd:PRK13641    3 IKFENVDYIYSPGTPmekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnknlKK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 423 LRQQLAYVSQQP--YLFEGTIRDNIRYGrPE---ATDAEVEEAA-----RLAYAHDFISAQPqgYEtpvgengvtLSGGQ 492
Cdd:PRK13641   83 LRKKVSLVFQFPeaQLFENTVLKDVEFG-PKnfgFSEDEAKEKAlkwlkKVGLSEDLISKSP--FE---------LSGGQ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 493 RQRLSIARALVRNAPILLLDEATSALDTES-EAAVQKALDEAMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEegnHE 570
Cdd:PRK13641  151 MRRVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVAEyADDVLVLEHGKLIK---HA 227

                         250       260
                  ....*....|....*....|...
gi 1582666899 571 TLAKV-SDGLYARLNNLQRPSAS 592
Cdd:PRK13641  228 SPKEIfSDKEWLKKHYLDEPATS 250

ABC_6TM_PCAT1_LagD_like

cd18570

Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...

36-321

5.67e-25

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: 105.22 E-value: 5.67e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  36 VFAIACLIVVALSTAFtawIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYAH 115
Cdd:cd18570     8 LLLSLLITLLGIAGSF---FFQILIDDIIPSGDINLLNIISIGLILLYLFQSLLSYIRSYLLLKLSQKLDIRLILGYFKH 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 116 LMTLSVGFFSEARSAHIAAQVSqNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPplLYALRYVS- 194
Cdd:cd18570    85 LLKLPLSFFETRKTGEIISRFN-DANKIREAISSTTISLFLDLLMVIISGIILFFYNWKLFLITLLIIP--LYILIILLf 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 195 -KRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEE----ELERKVNKLIKgaesRANRIARLSERTSPLTESFAGF 269
Cdd:cd18570   162 nKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEqflkKIEKKFSKLLK----KSFKLGKLSNLQSSIKGLISLI 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1582666899 270 AVASVLAYAAYRSIYFNVPPGAFFSFVTalLLAY--DPARRLARLQVQMERAVV 321
Cdd:cd18570   238 GSLLILWIGSYLVIKGQLSLGQLIAFNA--LLGYflGPIENLINLQPKIQEAKV 289

PRK10619

histidine ABC transporter ATP-binding protein HisP;

361-572

7.30e-25

histidine ABC transporter ATP-binding protein HisP;

Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 103.90 E-value: 7.30e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 361 YGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKK-------------SLRQQL 427
Cdd:PRK10619   15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknqlrLLRTRL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 428 AYVSQQPYLFEG-TIRDNIRYGRPEA---TDAEVEEAARLAYAHDFISAQPQGyETPVgengvTLSGGQRQRLSIARALV 503
Cdd:PRK10619   95 TMVFQHFNLWSHmTVLENVMEAPIQVlglSKQEARERAVKYLAKVGIDERAQG-KYPV-----HLSGGQQQRVSIARALA 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582666899 504 RNAPILLLDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHETL 572
Cdd:PRK10619  169 MEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHvSSHVIFLHQGKIEEEGAPEQL 239

ABCC_CFTR2

cd03289

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...

351-563

7.83e-25

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: 104.55 E-value: 7.83e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 351 RIEFRNVSFAY--GNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPrEGEILIDGQDIAHITKKSLRQQLA 428
Cdd:cd03289     2 QMTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNT-EGDIQIDGVSWNSVPLQKWRKAFG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 429 YVSQQPYLFEGTIRDNIR-YGRpeATDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAP 507
Cdd:cd03289    81 VIPQKVFIFSGTFRKNLDpYGK--WSDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAK 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1582666899 508 ILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRV 563
Cdd:cd03289   159 ILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214

ABCC_CFTR1

cd03291

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...

366-561

8.01e-25

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

Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 104.55 E-value: 8.01e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 366 VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEIlidgqdiahitKKSLRqqLAYVSQQPYLFEGTIRDNI 445
Cdd:cd03291    52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI-----------KHSGR--ISFSSQFSWIMPGTIKENI 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 446 RYG--RPEATDAEVEEAARLayaHDFISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESE 523
Cdd:cd03291   119 IFGvsYDEYRYKSVVKACQL---EEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1582666899 524 AAV-QKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQG 561
Cdd:cd03291   196 KEIfESCVCKLMANKTRILVTSKMEHLKKADKILILHEG 234

potA

TIGR01187

spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...

382-572

8.17e-25

spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]

Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 105.65 E-value: 8.17e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 382 LVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKslRQQLAYVSQQPYLF-EGTIRDNIRYG-----RPEAT-D 454
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH--LRHINMVFQSYALFpHMTVEENVAFGlkmrkVPRAEiK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 455 AEVEEAARLAYAHDFISAQPqgyetpvgengVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQ---KALD 531
Cdd:TIGR01187  79 PRVLEALRLVQLEEFADRKP-----------HQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQlelKTIQ 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1582666899 532 EAMsGRTVVVIAHRLS-TVVRADKIVVMQQGRVVEEGNHETL 572
Cdd:TIGR01187 148 EQL-GITFVFVTHDQEeAMTMSDRIAIMRKGKIAQIGTPEEI 188

ABC_6TM_Sav1866_like

cd18554

Six-transmembrane helical domain of the bacterial ABC multidrug exporter Sav1866 and similar ...

54-309

1.19e-24

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: 104.42 E-value: 1.19e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  54 WIMRAIIDEAFAN-------RRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYAHLMTLSVGFFSE 126
Cdd:cd18554    20 LILKYIVDDVIQGssltldeKVYKLFTIIGIMFFIFLILRPPVEYYRQYFAQWIANKILYDIRKDLFDHLQKLSLRYYAN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 127 ARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYVSKRLRSATREAVH 206
Cdd:cd18554   100 NRSGEIISRVINDVEQTKDFITTGLMNIWLDMITIIIAICIMLVLNPKLTFVSLVIFPFYILAVKYFFGRLRKLTKERSQ 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 207 LNSHVLGAMQETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSPLTESFAGFAVASVLAYAAYRSIYFN 286
Cdd:cd18554   180 ALAEVQGFLHERIQGMSVIKSFALEKHEQKQFDKRNGHFLTRALKHTRWNAKTFSAVNTITDLAPLLVIGFAAYLVIEGN 259

                         250       260
                  ....*....|....*....|...
gi 1582666899 287 VPPGAFFSFVTALLLAYDPARRL 309
Cdd:cd18554   260 LTVGTLVAFVGYMERMYSPLRRL 282

cbiO

PRK13640

energy-coupling factor transporter ATPase;

352-567

1.36e-24

energy-coupling factor transporter ATPase;

Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 103.73 E-value: 1.36e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGN--ESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGE---ILIDGQDIAHITKKSLRQQ 426
Cdd:PRK13640    6 VEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIREK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 427 LAYVSQQP-YLFEG-TIRDNIRYG-------RPEATDAEVEEAARLAYAhDFISAQPQgyetpvgengvTLSGGQRQRLS 497
Cdd:PRK13640   86 VGIVFQNPdNQFVGaTVGDDVAFGlenravpRPEMIKIVRDVLADVGML-DYIDSEPA-----------NLSGGQKQRVA 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1582666899 498 IARALVRNAPILLLDEATSALDTESEAAVQKALDEAM--SGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEG 567
Cdd:PRK13640  154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKkkNNLTVISITHDIDEANMADQVLVLDDGKLLAQG 225

cbiO

PRK13637

energy-coupling factor transporter ATPase;

352-575

2.09e-24

energy-coupling factor transporter ATPase;

Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 103.59 E-value: 2.09e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES-----VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIA--HITKKSLR 424
Cdd:PRK13637    3 IKIENLTHIYMEGTpfekkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 425 QQLAYVSQQP--YLFEGTIRDNIRYGrPE---ATDAEVEEAARLAYAHDFISaqpqgYETPVGENGVTLSGGQRQRLSIA 499
Cdd:PRK13637   83 KKVGLVFQYPeyQLFEETIEKDIAFG-PInlgLSEEEIENRVKRAMNIVGLD-----YEDYKDKSPFELSGGQKRRVAIA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 500 RALVRNAPILLLDEATSALDTeseaavqKALDEAMS---------GRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG-- 567
Cdd:PRK13637  157 GVVAMEPKILILDEPTAGLDP-------KGRDEILNkikelhkeyNMTIILVSHSMEDVAKlADRIIVMNKGKCELQGtp 229

                         250
                  ....*....|...
gi 1582666899 568 -----NHETLAKV 575
Cdd:PRK13637  230 revfkEVETLESI 242

urea_trans_UrtE

TIGR03410

urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...

353-572

2.59e-24

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

Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 101.45 E-value: 2.59e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 353 EFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKST----VISLIPrfydPREGEILIDGQDIAHI-TKKSLRQQL 427
Cdd:TIGR03410   2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTllktLMGLLP----VKSGSIRLDGEDITKLpPHERARAGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 428 AYVSQQ----PYLfegTIRDNIRYG---RPEATDAEVEEA-ARLAYAHDFISAQpqgyetpvgenGVTLSGGQRQRLSIA 499
Cdd:TIGR03410  78 AYVPQGreifPRL---TVEENLLTGlaaLPRRSRKIPDEIyELFPVLKEMLGRR-----------GGDLSGGQQQQLAIA 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582666899 500 RALVRNAPILLLDEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHETL 572
Cdd:TIGR03410 144 RALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRlrAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219

PRK13539

cytochrome c biogenesis protein CcmA; Provisional

351-543

2.66e-24

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 100.72 E-value: 2.66e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 351 RIEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDiahITKKSLRQQLAYV 430
Cdd:PRK13539    2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD---IDDPDVAEACHYL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 431 SQQ----PYLfegTIRDNIR-----YGrpeATDAEVEEA-ARLAYAHdfISAQPQGYetpvgengvtLSGGQRQRLSIAR 500
Cdd:PRK13539   79 GHRnamkPAL---TVAENLEfwaafLG---GEELDIAAAlEAVGLAP--LAHLPFGY----------LSAGQKRRVALAR 140

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1582666899 501 ALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIA 543
Cdd:PRK13539  141 LLVSNRPIWILDEPTAALDAAAVALFAELIRAHLAQGGIVIAA 183

SufC

COG0396

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...

353-574

2.71e-24

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

Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 102.07 E-value: 2.71e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 353 EFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKST---VISLIPRfYDPREGEILIDGQDIAH--ITKKSlRQQL 427
Cdd:COG0396     2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTlakVLMGHPK-YEVTSGSILLDGEDILElsPDERA-RAGI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 428 AYVSQQPYLFEG--------TIRDNIRYGRPEATDAE---VEEAARLAYAHDFIsaqpqgyETPVGENgvtLSGGQRQRL 496
Cdd:COG0396    80 FLAFQYPVEIPGvsvsnflrTALNARRGEELSAREFLkllKEKMKELGLDEDFL-------DRYVNEG---FSGGEKKRN 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 497 SIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMS-GRTVVVIAH--RLSTVVRADKIVVMQQGRVVEEGNHEtLA 573
Cdd:COG0396   150 EILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSpDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKE-LA 228


                  .
gi 1582666899 574 K 574
Cdd:COG0396   229 L 229

PRK13536

nodulation factor ABC transporter ATP-binding protein NodI;

315-572

2.79e-24

nodulation factor ABC transporter ATP-binding protein NodI;

Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 104.14 E-value: 2.79e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 315 QMERAVVN-ARMIYELLDMEPRQRDLPDA---RPLTVTQARIEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGK 390
Cdd:PRK13536    1 LLTRAVAEeAPRRLELSPIERKHQGISEAkasIPGSMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 391 STVISLIPRFYDPREGEILIDGQDIAHiTKKSLRQQLAYVSQQPYL-FEGTIRDNI----RYGRPEATDAE-----VEEA 460
Cdd:PRK13536   81 STIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQFDNLdLEFTVRENLlvfgRYFGMSTREIEavipsLLEF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 461 ARLAYAHDfisaqpqgyeTPVGEngvtLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMS-GRTV 539
Cdd:PRK13536  160 ARLESKAD----------ARVSD----LSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLArGKTI 225

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1582666899 540 VVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHETL 572
Cdd:PRK13536  226 LLTTHFMEEAERlCDRLCVLEAGRKIAEGRPHAL 259

PRK10253

iron-enterobactin ABC transporter ATP-binding protein;

345-567

1.19e-23

iron-enterobactin ABC transporter ATP-binding protein;

Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 100.83 E-value: 1.19e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 345 LTVTQARIEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLR 424
Cdd:PRK10253    1 MTESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 425 QQLAYVSQQPYL-FEGTIRDNIRYGR----PEATDAEVEEAARLAYAhdfisAQPQGYETPVGENGVTLSGGQRQRLSIA 499
Cdd:PRK10253   81 RRIGLLAQNATTpGDITVQELVARGRyphqPLFTRWRKEDEEAVTKA-----MQATGITHLADQSVDTLSGGQRQRAWIA 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582666899 500 RALVRNAPILLLDEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:PRK10253  156 MVLAQETAIMLLDEPTTWLDISHQIDLLELLSElnREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQG 226

PRK11264

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

352-572

1.45e-23

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

Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 100.21 E-value: 1.45e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDP-----REGEILID-----GQDIAHItkK 421
Cdd:PRK11264    4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPeagtiRVGDITIDtarslSQQKGLI--R 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 422 SLRQQLAYVSQQPYLF-EGTIRDNIRYGrPEATDAEVEEAArLAYAHDFISAqpqgyetpVGENGVT------LSGGQRQ 494
Cdd:PRK11264   82 QLRQHVGFVFQNFNLFpHRTVLENIIEG-PVIVKGEPKEEA-TARARELLAK--------VGLAGKEtsyprrLSGGQQQ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 495 RLSIARALVRNAPILLLDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLStVVR--ADKIVVMQQGRVVEEGNHET 571
Cdd:PRK11264  152 RVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQlAQEKRTMVIVTHEMS-FARdvADRAIFMDQGRIVEQGPAKA 230


                  .
gi 1582666899 572 L 572
Cdd:PRK11264  231 L 231

PRK10070

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

371-582

1.57e-23

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

Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 103.19 E-value: 1.57e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 371 SFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQ----QLAYVSQQPYLF-EGTIRDNI 445
Cdd:PRK10070   48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrkKIAMVFQSFALMpHMTVLDNT 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 446 RYGRPEA--TDAEVEEAARLAYAHDFISAQPQGYETpvgengvTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESE 523
Cdd:PRK10070  128 AFGMELAgiNAEERREKALDALRQVGLENYAHSYPD-------ELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1582666899 524 AAVQKALD--EAMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHETLAKVSDGLYAR 582
Cdd:PRK10070  201 TEMQDELVklQAKHQRTIVFISHDLDEAMRiGDRIAIMQNGEVVQVGTPDEILNNPANDYVR 262

cbiO

PRK13642

energy-coupling factor transporter ATPase;

352-579

1.59e-23

energy-coupling factor transporter ATPase;

Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 100.55 E-value: 1.59e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES---VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLA 428
Cdd:PRK13642    5 LEVENLVFKYEKESdvnQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 429 YVSQQP--YLFEGTIRDNIRYGRP------EATDAEVEEAARLAYAHDFISAQPqgyetpvgengVTLSGGQRQRLSIAR 500
Cdd:PRK13642   85 MVFQNPdnQFVGATVEDDVAFGMEnqgiprEEMIKRVDEALLAVNMLDFKTREP-----------ARLSGGQKQRVAVAG 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 501 ALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGR--TVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETLAKVSDG 578
Cdd:PRK13642  154 IIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYqlTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATSED 233


                  .
gi 1582666899 579 L 579
Cdd:PRK13642  234 M 234

PRK15134

microcin C ABC transporter ATP-binding protein YejF; Provisional

328-582

1.59e-23

microcin C ABC transporter ATP-binding protein YejF; Provisional

Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 104.40 E-value: 1.59e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 328 ELLDMEPRQRDLP---DARP-LTVTQARIEF--------RNVsfayGNESVLSGVSFTAEGGATTALVGPSGAGKST--- 392
Cdd:PRK15134  255 KLLNSEPSGDPVPlpePASPlLDVEQLQVAFpirkgilkRTV----DHNVVVKNISFTLRPGETLGLVGESGSGKSTtgl 330

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 393 -VISLIPRfydprEGEILIDGQDIAHITKKSL---RQQLAYVSQQPYL-------FEGTIRDNIRYGRPEATDAEVEEAA 461
Cdd:PRK15134  331 aLLRLINS-----QGEIWFDGQPLHNLNRRQLlpvRHRIQVVFQDPNSslnprlnVLQIIEEGLRVHQPTLSAAQREQQV 405

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 462 RLAYAHdfisaqpqgyetpVGENGVT-------LSGGQRQRLSIARALVRNAPILLLDEATSALDTESEA---AVQKALD 531
Cdd:PRK15134  406 IAVMEE-------------VGLDPETrhrypaeFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAqilALLKSLQ 472

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 532 EAmSGRTVVVIAHRLStVVRA--DKIVVMQQGRVVEEGNHETLAKVSDGLYAR 582
Cdd:PRK15134  473 QK-HQLAYLFISHDLH-VVRAlcHQVIVLRQGEVVEQGDCERVFAAPQQEYTR 523

cbiO

PRK13631

cobalt transporter ATP-binding subunit; Provisional

366-567

2.13e-23

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.08 E-value: 2.13e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 366 VLSGVSFTAEGGATTALVGPSGAGKSTVIS-----LIPRFYDPREGEILI------DGQDIAHITKK-----SLRQQLAY 429
Cdd:PRK13631   41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVThfnglIKSKYGTIQVGDIYIgdkknnHELITNPYSKKiknfkELRRRVSM 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 430 VSQQP--YLFEGTIRDNIRYGrPEATDAEVEEAARLAYAH--------DFISAQPQGyetpvgengvtLSGGQRQRLSIA 499
Cdd:PRK13631  121 VFQFPeyQLFKDTIEKDIMFG-PVALGVKKSEAKKLAKFYlnkmglddSYLERSPFG-----------LSGGQKRRVAIA 188

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 500 RALVRNAPILLLDEATSALDTESEAA-VQKALDEAMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:PRK13631  189 GILAIQPEILIFDEPTAGLDPKGEHEmMQLILDAKANNKTVFVITHTMEHVLEvADEVIVMDKGKILKTG 258

araG

PRK11288

L-arabinose ABC transporter ATP-binding protein AraG;

348-576

2.68e-23

L-arabinose ABC transporter ATP-binding protein AraG;

Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 103.45 E-value: 2.68e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 348 TQARIEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHI-TKKSLRQQ 426
Cdd:PRK11288    1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAsTTAALAAG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 427 LAYVSQQPYLF-EGTIRDNIRYGR-PEA----TDAEVEEAARLAYAHDFISAQPQgyeTPVGEngvtLSGGQRQRLSIAR 500
Cdd:PRK11288   81 VAIIYQELHLVpEMTVAENLYLGQlPHKggivNRRLLNYEAREQLEHLGVDIDPD---TPLKY----LSIGQRQMVEIAK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 501 ALVRNAPILLLDEATSAL---DTESEAAVQKAL-DEamsGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEgnHETLAKV 575
Cdd:PRK11288  154 ALARNARVIAFDEPTSSLsarEIEQLFRVIRELrAE---GRVILYVSHRMEEIFAlCDAITVFKDGRYVAT--FDDMAQV 228


                  .
gi 1582666899 576 S 576
Cdd:PRK11288  229 D 229

YbbA

COG4181

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...

352-566

4.20e-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: 98.27 E-value: 4.20e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES----VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSL---- 423
Cdd:COG4181     9 IELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARarlr 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 424 RQQLAYVSQQ----PYLfegTIRDNI-----RYGRPEATDAEVEEAARLAYAHDfISAQPQGyetpvgengvtLSGGQRQ 494
Cdd:COG4181    89 ARHVGFVFQSfqllPTL---TALENVmlpleLAGRRDARARARALLERVGLGHR-LDHYPAQ-----------LSGGEQQ 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1582666899 495 RLSIARALVRNAPILLLDEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEE 566
Cdd:COG4181   154 RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFElnRERGTTLVLVTHDPALAARCDRVLRLRAGRLVED 227

fbpC

PRK11432

ferric ABC transporter ATP-binding protein;

352-572

4.38e-23

ferric ABC transporter ATP-binding protein;

Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 100.95 E-value: 4.38e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDiahITKKSLRQQ-LAYV 430
Cdd:PRK11432    7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGED---VTHRSIQQRdICMV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 431 SQQPYLF-EGTIRDNIRYG-----RPEATDAE-VEEAARLAyahDFIsaqpqGYEtpvgENGV-TLSGGQRQRLSIARAL 502
Cdd:PRK11432   84 FQSYALFpHMSLGENVGYGlkmlgVPKEERKQrVKEALELV---DLA-----GFE----DRYVdQISGGQQQRVALARAL 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 503 VRNAPILLLDEATSALDTESEAAVQKALDEAMS--GRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHETL 572
Cdd:PRK11432  152 ILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSEAFAvSDTVIVMNKGKIMQIGSPQEL 224

BtuD

COG4138

ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...

367-568

4.70e-23

ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];

Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 98.37 E-value: 4.70e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 367 LSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYdPREGEILIDGQDIAHITKKSLRQQLAYVSQQ-PYLFEGTIRDNI 445
Cdd:COG4138    12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYLSQQqSPPFAMPVFQYL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 446 RYGRPEATDAEVEEAARLAYAHDFisaqpqGYETPVGENGVTLSGGQRQRLSIARALVR-------NAPILLLDEATSAL 518
Cdd:COG4138    91 ALHQPAGASSEAVEQLLAQLAEAL------GLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1582666899 519 DTESEAAVQKALDE-AMSGRTVVVIAHRLS-TVVRADKIVVMQQGRVVEEGN 568
Cdd:COG4138   165 DVAQQAALDRLLRElCQQGITVVMSSHDLNhTLRHADRVWLLKQGKLVASGE 216

ABC_putative_ATPase

cd03269

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...

352-567

5.17e-23

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: 97.35 E-value: 5.17e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQ--DIAHitkkslRQQLAY 429
Cdd:cd03269     1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKplDIAA------RNRIGY 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 430 VSQQPYLFEG-TIRDNIRY-GR-----PEATDAEVEE-AARLAYAHdfisaqpqgYETPVGEngvTLSGGQRQRLSIARA 501
Cdd:cd03269    75 LPEERGLYPKmKVIDQLVYlAQlkglkKEEARRRIDEwLERLELSE---------YANKRVE---ELSKGNQQKVQFIAA 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1582666899 502 LVRNAPILLLDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:cd03269   143 VIHDPELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEElCDRVLLLNKGRAVLYG 210

ABCG_White

cd03234

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...

364-567

5.53e-23

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: 97.73 E-value: 5.53e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 364 ESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPRE---GEILIDGQDIahiTKKSLRQQLAYVSQQPYLFEG- 439
Cdd:cd03234    20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPR---KPDQFQKCVAYVRQDDILLPGl 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 440 TIRDNIRYG--------RPEATDAEVEEAARLAYAHDfisaqpqgyeTPVGENGVT-LSGGQRQRLSIARALVRNAPILL 510
Cdd:cd03234    97 TVRETLTYTailrlprkSSDAIRKKRVEDVLLRDLAL----------TRIGGNLVKgISGGERRRVSIAVQLLWDPKVLI 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 511 LDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHR-LSTVVRA-DKIVVMQQGRVVEEG 567
Cdd:cd03234   167 LDEPTSGLDSFTALNLVSTLSQlARRNRIVILTIHQpRSDLFRLfDRILLLSSGEIVYSG 226

PRK10851

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;

352-567

6.58e-23

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;

Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 100.54 E-value: 6.58e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSlrQQLAYVS 431
Cdd:PRK10851    3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD--RKVGFVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYLFEG-TIRDNIRYG--------RP--EATDAEVE---EAARLAYAHDFISAQpqgyetpvgengvtLSGGQRQRLS 497
Cdd:PRK10851   81 QHYALFRHmTVFDNIAFGltvlprreRPnaAAIKAKVTqllEMVQLAHLADRYPAQ--------------LSGGQKQRVA 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 498 IARALVRNAPILLLDEATSALDTESEAAVQ---KALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEG 567
Cdd:PRK10851  147 LARALAVEPQILLLDEPFGALDAQVRKELRrwlRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAG 219

YejF

COG4172

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...

352-572

8.07e-23

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];

Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 102.46 E-value: 8.07e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES----VLSGVSFTAEGGATTALVGPSGAGKS----TVISLIPRFYDPREGEILIDGQDIAHITKKSL 423
Cdd:COG4172     7 LSVEDLSVAFGQGGgtveAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSEREL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 424 RQ----QLAYVSQQPY-----LFegTIRDNI--------RYGRPEATD------AEV---EEAARL-AYAHDfisaqpqg 476
Cdd:COG4172    87 RRirgnRIAMIFQEPMtslnpLH--TIGKQIaevlrlhrGLSGAAARAralellERVgipDPERRLdAYPHQ-------- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 477 yetpvgengvtLSGGQRQRLSIARALVrNAPILLL-DEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRLStVVR-- 551
Cdd:COG4172   157 -----------LSGGQRQRVMIAMALA-NEPDLLIaDEPTTALDVTVQAQILDLLKDlqRELGMALLLITHDLG-VVRrf 223

                         250       260
                  ....*....|....*....|.
gi 1582666899 552 ADKIVVMQQGRVVEEGNHETL 572
Cdd:COG4172   224 ADRVAVMRQGEIVEQGPTAEL 244

Uup

COG0488

ATPase components of ABC transporters with duplicated ATPase domains [General function ...

354-568

1.22e-22

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

Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 101.68 E-value: 1.22e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 354 FRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDgqdiahitkKSLRqqLAYVSQQ 433
Cdd:COG0488     1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------KGLR--IGYLPQE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 434 PYLFEG-TIRDNIRYGRPEATDAEVE-------------EAARLAYAHDFISAQpQGYE--------------------T 479
Cdd:COG0488    70 PPLDDDlTVLDTVLDGDAELRALEAEleeleaklaepdeDLERLAELQEEFEAL-GGWEaearaeeilsglgfpeedldR 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 480 PVGEngvtLSGGQRQRLSIARALVRNAPILLLDEATSALDTESeaaVQKaLDEAMSGR--TVVVIAH-R--LSTVVraDK 554
Cdd:COG0488   149 PVSE----LSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEW-LEEFLKNYpgTVLVVSHdRyfLDRVA--TR 218

                         250
                  ....*....|....*
gi 1582666899 555 IVVMQQGRVVE-EGN 568
Cdd:COG0488   219 ILELDRGKLTLyPGN 233

CFTR_protein

TIGR01271

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...

357-563

1.66e-22

Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 102.68 E-value: 1.66e-22

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  357 VSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPrEGEILIDGQDIAHITKKSLRQQLAYVSQQPYL 436
Cdd:TIGR01271 1225 AKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLST-EGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFI 1303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  437 FEGTIRDNIRygrPEA--TDAEVEEAARLAYAHDFISAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAPILLLDEA 514
Cdd:TIGR01271 1304 FSGTFRKNLD---PYEqwSDEEIWKVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEP 1380

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1582666899  515 TSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRV 563
Cdd:TIGR01271 1381 SAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVIEGSSV 1429

PRK14246

phosphate ABC transporter ATP-binding protein; Provisional

356-568

2.04e-22

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 97.04 E-value: 2.04e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 356 NVSFAY---GNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRF---YDPR---EGEILIDGQDIAHITKKSLRQQ 426
Cdd:PRK14246   12 NISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSKikvDGKVLYFGKDIFQIDAIKLRKE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 427 LAYVSQQPYLFEG-TIRDNIRY-----GRPEATDAE--VEEAAR----LAYAHDFISaqpqgyeTPVGEngvtLSGGQRQ 494
Cdd:PRK14246   92 VGMVFQQPNPFPHlSIYDNIAYplkshGIKEKREIKkiVEECLRkvglWKEVYDRLN-------SPASQ----LSGGQQQ 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582666899 495 RLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGN 568
Cdd:PRK14246  161 RLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARvADYVAFLYNGELVEWGS 235

3a01204

TIGR00955

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

365-574

2.63e-22

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

Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 101.28 E-value: 2.63e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 365 SVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPrFYDP----REGEILIDGQdiaHITKKSLRQQLAYVsQQPYLFEG- 439
Cdd:TIGR00955  39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPkgvkGSGSVLLNGM---PIDAKEMRAISAYV-QQDDLFIPt 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 440 -TIRDNI------RYGRPEATDAEVEEAARLAYAHDFISAQpqgyETPVGENGVT--LSGGQRQRLSIARALVRNAPILL 510
Cdd:TIGR00955 114 lTVREHLmfqahlRMPRRVTKKEKRERVDEVLQALGLRKCA----NTRIGVPGRVkgLSGGERKRLAFASELLTDPPLLF 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582666899 511 LDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLSTVVRA--DKIVVMQQGRVVEEGNHETLAK 574
Cdd:TIGR00955 190 CDEPTSGLDSFMAYSVVQVLKGlAQKGKTIICTIHQPSSELFElfDKIILMAEGRVAYLGSPDQAVP 256

YhaQ

COG4152

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

352-568

2.87e-22

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

Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 97.49 E-value: 2.87e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITkkslRQQLAyvs 431
Cdd:COG4152     2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED----RRRIG--- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 qqpYLFE--G-----TIRDNIRY-----GRPEatdAEVEEAA-----RL---AYAHDFISaqpqgyetpvgengvTLSGG 491
Cdd:COG4152    75 ---YLPEerGlypkmKVGEQLVYlarlkGLSK---AEAKRRAdewleRLglgDRANKKVE---------------ELSKG 133

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582666899 492 QRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKAL-DEAMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGN 568
Cdd:COG4152   134 NQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIrELAAKGTTVIFSSHQMELVEElCDRIVIINKGRKVLSGS 212

nickel_nikE

TIGR02769

nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...

360-566

3.14e-22

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: 96.41 E-value: 3.14e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 360 AYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQ---------QLAYV 430
Cdd:TIGR02769  20 AKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrdvqlvfQDSPS 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 431 SQQPylfEGTIRDNIRYGRPEATD-AEVEEAARLAYAHDFISAQPQGYETPVGEngvtLSGGQRQRLSIARALVRNAPIL 509
Cdd:TIGR02769 100 AVNP---RMTVRQIIGEPLRHLTSlDESEQKARIAELLDMVGLRSEDADKLPRQ----LSGGQLQRINIARALAVKPKLI 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 510 LLDEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEE 566
Cdd:TIGR02769 173 VLDEAVSNLDMVLQAVILELLRKlqQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEE 232

PRK15439

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

352-574

3.40e-22

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 100.13 E-value: 3.40e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKkSLRQQLA--Y 429
Cdd:PRK15439   12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP-AKAHQLGiyL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 430 VSQQPYLFEG-TIRDNIRYGRPEATDAEVEEAARLAYAHDFISAQPQGyetpvgengVTLSGGQRQRLSIARALVRNAPI 508
Cdd:PRK15439   91 VPQEPLLFPNlSVKENILFGLPKRQASMQKMKQLLAALGCQLDLDSSA---------GSLEVADRQIVEILRGLMRDSRI 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582666899 509 LLLDEATSALD-TESEA---AVQKALDEamsGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHETLAK 574
Cdd:PRK15439  162 LILDEPTASLTpAETERlfsRIRELLAQ---GVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADLST 229

cbiO

PRK13644

energy-coupling factor transporter ATPase;

352-572

3.52e-22

energy-coupling factor transporter ATPase;

Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.59 E-value: 3.52e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES-VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITK-KSLRQQLAY 429
Cdd:PRK13644    2 IRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 430 VSQQPYL-FEG-TIRDNIRYGRPEATDAEVEEAARLAYAHDFISAQPQGYETPVgengvTLSGGQRQRLSIARALVRNAP 507
Cdd:PRK13644   82 VFQNPETqFVGrTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPK-----TLSGGQGQCVALAGILTMEPE 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1582666899 508 ILLLDEATSALDTESEAAVQ---KALDEamSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGNHETL 572
Cdd:PRK13644  157 CLIFDEVTSMLDPDSGIAVLeriKKLHE--KGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENV 222

cbiO

PRK13638

energy-coupling factor ABC transporter ATP-binding protein;

359-567

3.89e-22

energy-coupling factor ABC transporter ATP-binding protein;

Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 96.61 E-value: 3.89e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 359 FAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKK--SLRQQLAYVSQQP-- 434
Cdd:PRK13638    9 FRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGllALRQQVATVFQDPeq 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 435 YLFEGTIRDNIRYGRPEATDAEVEEAARLAYAHDFISAQpQGYETPVGengvTLSGGQRQRLSIARALVRNAPILLLDEA 514
Cdd:PRK13638   89 QIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQ-HFRHQPIQ----CLSHGQKKRVAIAGALVLQARYLLLDEP 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1582666899 515 TSALDTESEA---AVQKALdeAMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:PRK13638  164 TAGLDPAGRTqmiAIIRRI--VAQGNHVIISSHDIDLIYEiSDAVYVLRQGQILTHG 218

PRK14271

phosphate ABC transporter ATP-binding protein; Provisional

356-572

6.34e-22

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 95.93 E-value: 6.34e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 356 NVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDP-----REGEILIDGQDIAHITKK-SLRQQLAY 429
Cdd:PRK14271   26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVlEFRRRVGM 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 430 VSQQPYLFEGTIRDNIRYG--------RPE---ATDAEVEEAARLAYAHDFISAQPqgyetpvgengVTLSGGQRQRLSI 498
Cdd:PRK14271  106 LFQRPNPFPMSIMDNVLAGvrahklvpRKEfrgVAQARLTEVGLWDAVKDRLSDSP-----------FRLSGGQQQLLCL 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582666899 499 ARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHETL 572
Cdd:PRK14271  175 ARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARiSDRAALFFDGRLVEEGPTEQL 249

cbiO

PRK13652

cobalt transporter ATP-binding subunit; Provisional

352-570

7.00e-22

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 96.03 E-value: 7.00e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAY-GNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYV 430
Cdd:PRK13652    4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 431 SQQP--YLFEGTIRDNIRYG------RPEATDAEVEEAARLAYAHDFISAQPQgyetpvgengvTLSGGQRQRLSIARAL 502
Cdd:PRK13652   84 FQNPddQIFSPTVEQDIAFGpinlglDEETVAHRVSSALHMLGLEELRDRVPH-----------HLSGGEKKRVAIAGVI 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582666899 503 VRNAPILLLDEATSALDTESEAAVQKALDEAMS--GRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHE 570
Cdd:PRK13652  153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEmADYIYVMDKGRIVAYGTVE 223

ABC_FeS_Assembly

cd03217

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...

352-567

8.32e-22

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

Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 93.36 E-value: 8.32e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKST---VISLIPRfYDPREGEILIDGQDIahitkkslrqqla 428
Cdd:cd03217     1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTlakTIMGHPK-YEVTEGEILFKGEDI------------- 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 429 yvsqqpylfegtirdnirygrpeaTDAEVEEAARLAYahdFISAQpqgyeTPVGENGVTL-----------SGGQRQRLS 497
Cdd:cd03217    67 ------------------------TDLPPEERARLGI---FLAFQ-----YPPEIPGVKNadflryvnegfSGGEKKRNE 114

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 498 IARALVRNAPILLLDEATSALDTESEAAVQKALDE-AMSGRTVVVIAH--RLSTVVRADKIVVMQQGRVVEEG 567
Cdd:cd03217   115 ILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHyqRLLDYIKPDRVHVLYDGRIVKSG 187

TauB

COG4525

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

350-565

8.60e-22

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

Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 95.31 E-value: 8.60e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 350 ARIEFRNVSFAYGNES----VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIahiTKKSLRQ 425
Cdd:COG4525     2 SMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV---TGPGADR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 426 qlAYVSQQ----PYLfegTIRDNIRYGrpeATDAEVEEAARLAYAHDFISAQP-QGYET-PVGEngvtLSGGQRQRLSIA 499
Cdd:COG4525    79 --GVVFQKdallPWL---NVLDNVAFG---LRLRGVPKAERRARAEELLALVGlADFARrRIWQ----LSGGMRQRVGIA 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582666899 500 RALVRNAPILLLDEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRL-STVVRADKIVVM--QQGRVVE 565
Cdd:COG4525   147 RALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITHSVeEALFLATRLVVMspGPGRIVE 217

ABC_DrrA

cd03265

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...

352-572

1.11e-21

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: 93.59 E-value: 1.11e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKsLRQQLAYVS 431
Cdd:cd03265     1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE-VRRRIGIVF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYLFEG-TIRDNIR-----YGRPEATDAE-VEEAARLAYAHDFISAQPQGYetpvgengvtlSGGQRQRLSIARALVR 504
Cdd:cd03265    80 QDLSVDDElTGWENLYiharlYGVPGAERRErIDELLDFVGLLEAADRLVKTY-----------SGGMRRRLEIARSLVH 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582666899 505 NAPILLLDEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHETL 572
Cdd:cd03265   149 RPEVLFLDEPTIGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219

PRK14267

phosphate ABC transporter ATP-binding protein; Provisional

352-567

1.49e-21

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 94.14 E-value: 1.49e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPR-----EGEILIDGQDI--AHITKKSLR 424
Cdd:PRK14267    5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEVR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 425 QQLAYVSQQPYLFEG-TIRDNIRYG--------RPEATDAEVEEAARLAYAHDFISAQPQGYETpvgengvTLSGGQRQR 495
Cdd:PRK14267   85 REVGMVFQYPNPFPHlTIYDNVAIGvklnglvkSKKELDERVEWALKKAALWDEVKDRLNDYPS-------NLSGGQRQR 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 496 LSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:PRK14267  158 LVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARvSDYVAFLYLGKLIEVG 230

ABC_CcmA_heme_exporter

cd03231

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...

352-561

3.30e-21

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: 91.79 E-value: 3.30e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIaHITKKSLRQQLAYVS 431
Cdd:cd03231     1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIARGLLYLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYLFEG-TIRDNIRYGRPEATDAEVEEAarLAyahdfiSAQPQGYE-TPVGengvTLSGGQRQRLSIARALVRNAPIL 509
Cdd:cd03231    80 HAPGIKTTlSVLENLRFWHADHSDEQVEEA--LA------RVGLNGFEdRPVA----QLSAGQQRRVALARLLLSGRPLW 147

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1582666899 510 LLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQG 561
Cdd:cd03231   148 ILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLG 199

PRK10908

cell division ATP-binding protein FtsE;

352-570

5.14e-21

cell division ATP-binding protein FtsE;

Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 91.86 E-value: 5.14e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAY-GNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKS---LRQQL 427
Cdd:PRK10908    2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 428 AYVSQQPYLF-EGTIRDNIRYGRPEATDAEVEEAARLAYAHDFISAQPQGYETPvgengVTLSGGQRQRLSIARALVRNA 506
Cdd:PRK10908   82 GMIFQDHHLLmDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFP-----IQLSGGEQQRVGIARAVVNKP 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582666899 507 PILLLDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLSTVVRAD-KIVVMQQGRVVEEGNHE 570
Cdd:PRK10908  157 AVLLADEPTGNLDDALSEGILRLFEEfNRVGVTVLMATHDIGLISRRSyRMLTLSDGHLHGGVGGE 222

ABCD_peroxisomal_ALDP

cd03223

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...

352-545

5.42e-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: 90.29 E-value: 5.42e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVL-SGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEIlidgqdiahitKKSLRQQLAYV 430
Cdd:cd03223     1 IELENLSLATPDGRVLlKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----------GMPEGEDLLFL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 431 SQQPYLFEGTIRDNIRYgrpeatdaeveeaarlayahdfisaqpqgyetPVGEngvTLSGGQRQRLSIARALVRNAPILL 510
Cdd:cd03223    70 PQRPYLPLGTLREQLIY--------------------------------PWDD---VLSGGEQQRLAFARLLLHKPKFVF 114

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1582666899 511 LDEATSALDTESEAAVQKALDEAMSgrTVVVIAHR 545
Cdd:cd03223   115 LDEATSALDEESEDRLYQLLKELGI--TVISVGHR 147

ABC_6TM_YwjA_like

cd18549

Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...

39-318

7.12e-21

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: 93.28 E-value: 7.12e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  39 IACLIVVALSTAFTAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYAHLMT 118
Cdd:cd18549     8 LFCAVLIAALDLVFPLIVRYIIDDLLPSKNLRLILIIGAILLALYILRTLLNYFVTYWGHVMGARIETDMRRDLFEHLQK 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 119 LSVGFFSEARSAHIAAQVSQNVSGIRDVL-----NLTITstvrdLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYV 193
Cdd:cd18549    88 LSFSFFDNNKTGQLMSRITNDLFDISELAhhgpeDLFIS-----IITIIGSFIILLTINVPLTLIVFALLPLMIIFTIYF 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 194 SKRLRSA---TREAV-HLNSHVlgamQETIQGIAIVKAFTMEE-ELER--KVNKLIKGAESRANRI-ARLsertSPLTES 265
Cdd:cd18549   163 NKKMKKAfrrVREKIgEINAQL----EDSLSGIRVVKAFANEEyEIEKfdEGNDRFLESKKKAYKAmAYF----FSGMNF 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1582666899 266 FAGFAVASVLAYAAYRSIYFNVPPGAFFSFV--TALLLAydPARRLARLQVQMER 318
Cdd:cd18549   235 FTNLLNLVVLVAGGYFIIKGEITLGDLVAFLlyVNVFIK--PIRRLVNFTEQYQK 287

ABCG_PDR_domain2

cd03232

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...

351-561

1.21e-20

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: 90.00 E-value: 1.21e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 351 RIEFRNVSF----AYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDP--REGEILIDGQDIahitKKSLR 424
Cdd:cd03232     3 VLTWKNLNYtvpvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPL----DKNFQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 425 QQLAYVSQQPYLFegtirdnirygrPEATdaeVEEAARLayahdfiSAQPQGyetpvgengvtLSGGQRQRLSIARALVR 504
Cdd:cd03232    79 RSTGYVEQQDVHS------------PNLT---VREALRF-------SALLRG-----------LSVEQRKRLTIGVELAA 125

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 505 NAPILLLDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLSTVV--RADKIVVMQQG 561
Cdd:cd03232   126 KPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSASIfeKFDRLLLLKRG 185

ABCF_EF-3

cd03221

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...

352-562

1.24e-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: 88.27 E-value: 1.24e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGqdiahitkkslRQQLAYVS 431
Cdd:cd03221     1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS-----------TVKIGYFE 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QqpylfegtirdnirygrpeatdaeveeaarlayahdfisaqpqgyetpvgengvtLSGGQRQRLSIARALVRNAPILLL 511
Cdd:cd03221    70 Q-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1582666899 512 DEATSALDTESEAAVQKALDEamSGRTVVVIAH-R--LSTVvrADKIVVMQQGR 562
Cdd:cd03221    95 DEPTNHLDLESIEALEEALKE--YPGTVILVSHdRyfLDQV--ATKIIELEDGK 144

YnjD

COG4136

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...

353-521

1.36e-20

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

Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 90.23 E-value: 1.36e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 353 EFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPR---EGEILIDGQDIAHItkKSLRQQLAY 429
Cdd:COG4136     3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTAL--PAEQRRIGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 430 VSQQPYLFEG-TIRDNIRYGRPEAT-----DAEVEEAARLAYAHDFISAQPQgyetpvgengvTLSGGQRQRLSIARALV 503
Cdd:COG4136    81 LFQDDLLFPHlSVGENLAFALPPTIgraqrRARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVALLRALL 149

                         170
                  ....*....|....*...
gi 1582666899 504 RNAPILLLDEATSALDTE 521
Cdd:COG4136   150 AEPRALLLDEPFSKLDAA 167

phnK

PRK11701

phosphonate C-P lyase system protein PhnK; Provisional

355-567

1.54e-20

phosphonate C-P lyase system protein PhnK; Provisional

Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 91.53 E-value: 1.54e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 355 RNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQ-----DIAHITKKS----LRQ 425
Cdd:PRK11701   10 RGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAErrrlLRT 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 426 QLAYVSQQPylfegtiRDNIR--------------------YG--RPEATD--AEVE-EAARlayahdfISAQPQgyetp 480
Cdd:PRK11701   90 EWGFVHQHP-------RDGLRmqvsaggnigerlmavgarhYGdiRATAGDwlERVEiDAAR-------IDDLPT----- 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 481 vgengvTLSGGQRQRLSIARALVRNAPILLLDEATSALDTeseaAVQKALDEAMSGRT------VVVIAHRLStVVR--A 552
Cdd:PRK11701  151 ------TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDV----SVQARLLDLLRGLVrelglaVVIVTHDLA-VARllA 219

                         250
                  ....*....|....*
gi 1582666899 553 DKIVVMQQGRVVEEG 567
Cdd:PRK11701  220 HRLLVMKQGRVVESG 234

PRK13537

nodulation factor ABC transporter ATP-binding protein NodI;

350-567

1.88e-20

nodulation factor ABC transporter ATP-binding protein NodI;

Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 92.18 E-value: 1.88e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 350 ARIEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSlRQQLAY 429
Cdd:PRK13537    6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 430 VSQQPYLF-EGTIRDNIR-YGRPEATDAEvEEAARLAYAHDFISAQPQGyETPVGEngvtLSGGQRQRLSIARALVRNAP 507
Cdd:PRK13537   85 VPQFDNLDpDFTVRENLLvFGRYFGLSAA-AARALVPPLLEFAKLENKA-DAKVGE----LSGGMKRRLTLARALVNDPD 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1582666899 508 ILLLDEATSALDTESEAAVQKALDEAM-SGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:PRK13537  159 VLVLDEPTTGLDPQARHLMWERLRSLLaRGKTILLTTHFMEEAERlCDRLCVIEEGRKIAEG 220

cbiO

PRK13636

cobalt transporter ATP-binding subunit; Provisional

352-574

2.13e-20

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 91.45 E-value: 2.13e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES-VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKK--SLRQQLA 428
Cdd:PRK13636    6 LKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGlmKLRESVG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 429 YVSQQP--YLFEGTIRDNIRYGR-----PEatdAEVEEAARLAYAHDFISA---QPQGYetpvgengvtLSGGQRQRLSI 498
Cdd:PRK13636   86 MVFQDPdnQLFSASVYQDVSFGAvnlklPE---DEVRKRVDNALKRTGIEHlkdKPTHC----------LSFGQKKRVAI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 499 ARALVRNAPILLLDEATSALDTESEAAVQKALDEAMS--GRTVVVIAHRLSTV-VRADKIVVMQQGRVVEEGN-HETLAK 574
Cdd:PRK13636  153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVpLYCDNVFVMKEGRVILQGNpKEVFAE 232

PRK15056

manganese/iron ABC transporter ATP-binding protein;

345-571

2.28e-20

manganese/iron ABC transporter ATP-binding protein;

Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 91.48 E-value: 2.28e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 345 LTVTQARIEFRNvsfaygNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDiahiTKKSLR 424
Cdd:PRK15056    7 IVVNDVTVTWRN------GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP----TRQALQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 425 QQL-AYVSQQ-------PYLFEGTIRDNiRYG------RPEATDAEVEEAA-----RLAYAHDFIsaqpqgyetpvGEng 485
Cdd:PRK15056   77 KNLvAYVPQSeevdwsfPVLVEDVVMMG-RYGhmgwlrRAKKRDRQIVTAAlarvdMVEFRHRQI-----------GE-- 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 486 vtLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMS-GRTVVVIAHRLSTVVRADKIVVMQQGRVV 564
Cdd:PRK15056  143 --LSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDeGKTMLVSTHNLGSVTEFCDYTVMVKGTVL 220


                  ....*..
gi 1582666899 565 EEGNHET 571
Cdd:PRK15056  221 ASGPTET 227

PRK10535

macrolide ABC transporter ATP-binding protein/permease MacB;

350-564

2.77e-20

macrolide ABC transporter ATP-binding protein/permease MacB;

Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 94.79 E-value: 2.77e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 350 ARIEFRNVSFAY--GNES--VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSL-- 423
Cdd:PRK10535    3 ALLELKDIRRSYpsGEEQveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALaq 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 424 --RQQLAYVSQQPYLFEG-TIRDNIRYgrpEATDAEVEEAARLAYAHDFIsaQPQGYETPVGENGVTLSGGQRQRLSIAR 500
Cdd:PRK10535   83 lrREHFGFIFQRYHLLSHlTAAQNVEV---PAVYAGLERKQRLLRAQELL--QRLGLEDRVEYQPSQLSGGQQQRVSIAR 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582666899 501 ALVRNAPILLLDEATSALDTESEAAVQKALDEAMS-GRTVVVIAHRLSTVVRADKIVVMQQGRVV 564
Cdd:PRK10535  158 ALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222

ABC_6TM_bac_exporter_ABCB8_10_like

cd18575

Six-transmembrane helical domain of putative bacterial ABC exporters, similar to ABCB8 and ...

38-296

3.12e-20

Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 91.39 E-value: 3.12e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  38 AIACLIVVALSTAFTAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYAHLM 117
Cdd:cd18575     1 ALIALLIAAAATLALGQGLRLLIDQGFAAGNTALLNRAFLLLLAVALVLALASALRFYLVSWLGERVVADLRKAVFAHLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 118 TLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYVSKRL 197
Cdd:cd18575    81 RLSPSFFETTRTGEVLSRLTTDTTLIQTVVGSSLSIALRNLLLLIGGLVMLFITSPKLTLLVLLVIPLVVLPIILFGRRV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 198 RSATREAvhlNSHV--LGAM-QETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLSertSPLTES--FAGF-AV 271
Cdd:cd18575   161 RRLSRAS---QDRLadLSAFaEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALRRIRAR---ALLTALviFLVFgAI 234

                         250       260
                  ....*....|....*....|....*
gi 1582666899 272 ASVLAYAAYRSIYFNVPPGAFFSFV 296
Cdd:cd18575   235 VFVLWLGAHDVLAGRMSAGELSQFV 259

ABC_6TM_T1SS_like

cd18555

Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ...

33-252

5.69e-20

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: 90.65 E-value: 5.69e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  33 WGYVFAIACL-IVVALSTAFTAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRR 111
Cdd:cd18555     1 KKLLISILLLsLLLQLLTLLIPILTQYVIDNVIVPGNLNLLNVLGIGILILFLLYGLFSFLRGYIIIKLQTKLDKSLMSD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 112 LYAHLMTLSVGFFsEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMApPLLYALR 191
Cdd:cd18555    81 FFEHLLKLPYSFF-ENRSSGDLLFRANSNVYIRQILSNQVISLIIDLLLLVIYLIYMLYYSPLLTLIVLLLG-LLIVLLL 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582666899 192 YVSKR-LRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEEL----ERKVNKLIKgAESRANRI 252
Cdd:cd18555   159 LLTRKkIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEKNIykkwENLFKKQLK-AFKKKERL 223

cbiO

PRK13645

energy-coupling factor transporter ATPase;

356-575

6.87e-20

energy-coupling factor transporter ATPase;

Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 90.45 E-value: 6.87e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 356 NVSFAYGNES-----VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDI-AHITK----KSLRQ 425
Cdd:PRK13645   11 NVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKikevKRLRK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 426 QLAYVSQQP--YLFEGTIRDNIRYGrPEATDAEVEEA-ARLAYAHDFISAqPQGYetpVGENGVTLSGGQRQRLSIARAL 502
Cdd:PRK13645   91 EIGLVFQFPeyQLFQETIEKDIAFG-PVNLGENKQEAyKKVPELLKLVQL-PEDY---VKRSPFELSGGQKRRVALAGII 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 503 VRNAPILLLDEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG-------NHETL 572
Cdd:PRK13645  166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERlnKEYKKRIIMVTHNMDQVLRiADEVIVMHEGKVISIGspfeifsNQELL 245


                  ...
gi 1582666899 573 AKV 575
Cdd:PRK13645  246 TKI 248

ABC_KpsT_Wzt

cd03220

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...

366-567

7.21e-20

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: 88.74 E-value: 7.21e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 366 VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITkkslrqqlAYVSQQPYLfegTIRDNI 445
Cdd:cd03220    37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG--------LGGGFNPEL---TGRENI 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 446 R-----YGRpeaTDAEVEEaaRLAYAHDFiSAQPQGYETPVGengvTLSGGQRQRL--SIARALvrNAPILLLDEATSAL 518
Cdd:cd03220   106 YlngrlLGL---SRKEIDE--KIDEIIEF-SELGDFIDLPVK----TYSSGMKARLafAIATAL--EPDILLIDEVLAVG 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1582666899 519 DTESEAAVQKALDEAMS-GRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:cd03220   174 DAAFQEKCQRRLRELLKqGKTVILVSHDPSSIKRlCDRALVLEKGKIRFDG 224

PRK13549

xylose transporter ATP-binding subunit; Provisional

352-562

8.08e-20

xylose transporter ATP-binding subunit; Provisional

Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 92.68 E-value: 8.08e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKST---VISLI-PrfYDPREGEILIDGQDI-AHITKKSLR-- 424
Cdd:PRK13549    6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTlmkVLSGVyP--HGTYEGEIIFEGEELqASNIRDTERag 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 425 -----QQLAYVsqqPYLfegTIRDNIRYGRpeatdaEVEEAARLAYAHDFISAQ-----------PqgyETPVGEngvtL 488
Cdd:PRK13549   84 iaiihQELALV---KEL---SVLENIFLGN------EITPGGIMDYDAMYLRAQkllaqlkldinP---ATPVGN----L 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582666899 489 SGGQRQRLSIARALVRNAPILLLDEATSALdTESEAAVQKAL--DEAMSGRTVVVIAHRLSTVVR-ADKIVVMQQGR 562
Cdd:PRK13549  145 GLGQQQLVEIAKALNKQARLLILDEPTASL-TESETAVLLDIirDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220

PRK15134

microcin C ABC transporter ATP-binding protein YejF; Provisional

348-572

8.67e-20

microcin C ABC transporter ATP-binding protein YejF; Provisional

Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 92.85 E-value: 8.67e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 348 TQARIEFRNVSFAYGNE----SVLSGVSFTAEGGATTALVGPSGAGKS-TVISLIPRFYDP----REGEILIDGQDIAHI 418
Cdd:PRK15134    2 TQPLLAIENLSVAFRQQqtvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 419 TKKSLRQ----QLAYVSQQPYLFEG---TIRDNI-------RYGRPEATDAEV----------EEAARLA-YAHDfisaq 473
Cdd:PRK15134   82 SEQTLRGvrgnKIAMIFQEPMVSLNplhTLEKQLyevlslhRGMRREAARGEIlncldrvgirQAAKRLTdYPHQ----- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 474 pqgyetpvgengvtLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMS--GRTVVVIAHRLSTVVR 551
Cdd:PRK15134  157 --------------LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRK 222

                         250       260
                  ....*....|....*....|..
gi 1582666899 552 -ADKIVVMQQGRVVEEGNHETL 572
Cdd:PRK15134  223 lADRVAVMQNGRCVEQNRAATL 244

PRK11000

maltose/maltodextrin ABC transporter ATP-binding protein MalK;

350-567

1.11e-19

maltose/maltodextrin ABC transporter ATP-binding protein MalK;

Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 91.24 E-value: 1.11e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 350 ARIEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKslRQQLAY 429
Cdd:PRK11000    2 ASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVGM 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 430 VSQQ----PYLfegTIRDNIRYGRPEA------TDAEVEEAAR-LAYAHdFISAQPQgyetpvgengvTLSGGQRQRLSI 498
Cdd:PRK11000   80 VFQSyalyPHL---SVAENMSFGLKLAgakkeeINQRVNQVAEvLQLAH-LLDRKPK-----------ALSGGQRQRVAI 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582666899 499 ARALVRNAPILLLDEATSALDteseAAVQKALDEAMS------GRTVVVIAH-RLSTVVRADKIVVMQQGRVVEEG 567
Cdd:PRK11000  145 GRTLVAEPSVFLLDEPLSNLD----AALRVQMRIEISrlhkrlGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216

PRK15079

oligopeptide ABC transporter ATP-binding protein OppF; Provisional

369-572

1.33e-19

oligopeptide ABC transporter ATP-binding protein OppF; Provisional

Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 90.15 E-value: 1.33e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 369 GVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQ---------QLAYVSQQPYLfeg 439
Cdd:PRK15079   39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAvrsdiqmifQDPLASLNPRM--- 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 440 TIRDNI----RYGRPEATDAEVEEAARLA-------------YAHDFisaqpqgyetpvgengvtlSGGQRQRLSIARAL 502
Cdd:PRK15079  116 TIGEIIaeplRTYHPKLSRQEVKDRVKAMmlkvgllpnlinrYPHEF-------------------SGGQCQRIGIARAL 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1582666899 503 VRNAPILLLDEATSALDTESEAAV---QKALDEAMsGRTVVVIAHRLStVVR--ADKIVVMQQGRVVEEGNHETL 572
Cdd:PRK15079  177 ILEPKLIICDEPVSALDVSIQAQVvnlLQQLQREM-GLSLIFIAHDLA-VVKhiSDRVLVMYLGHAVELGTYDEV 249

PRK13633

energy-coupling factor transporter ATPase;

352-568

1.47e-19

energy-coupling factor transporter ATPase;

Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 88.99 E-value: 1.47e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES------VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDiahiTKK---- 421
Cdd:PRK13633    5 IKCKNVSYKYESNEesteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD----TSDeenl 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 422 -SLRQQLAYVSQQP--YLFEGTIRDNIRYG------RPEATDAEVEEAARLAYAHDFISAQPQgyetpvgengvTLSGGQ 492
Cdd:PRK13633   81 wDIRNKAGMVFQNPdnQIVATIVEEDVAFGpenlgiPPEEIRERVDESLKKVGMYEYRRHAPH-----------LLSGGQ 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1582666899 493 RQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGN 568
Cdd:PRK13633  150 KQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKElnKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGT 227

ABC_6TM_CvaB_RaxB_like

cd18567

Six-transmembrane helical domain (6-TMD) of the ABC transporter subunit of the type 1 ...

36-280

1.70e-19

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: 89.06 E-value: 1.70e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  36 VFAIACLI-VVALSTAFtawIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYA 114
Cdd:cd18567     7 ILLLSLALeLFALASPL---YLQLVIDEVIVSGDRDLLTVLAIGFGLLLLLQALLSALRSWLVLYLSTSLNLQWTSNLFR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 115 HLMTLSVGFFsEARsaHIAAQVS--QNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAppLLYA-LR 191
Cdd:cd18567    84 HLLRLPLSYF-EKR--HLGDIVSrfGSLDEIQQTLTTGFVEALLDGLMAILTLVMMFLYSPKLALIVLAAV--ALYAlLR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 192 YVS-KRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERK-VNKLIKGAESRAnRIARLSERTSPLTESFAGF 269
Cdd:cd18567   159 LALyPPLRRATEEQIVASAKEQSHFLETIRGIQTIKLFGREAEREARwLNLLVDAINADI-RLQRLQILFSAANGLLFGL 237

                         250
                  ....*....|.
gi 1582666899 270 AVASVLAYAAY 280
Cdd:cd18567   238 ENILVIYLGAL 248

LptB

COG1137

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...

350-513

1.82e-19

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

Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 87.78 E-value: 1.82e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 350 ARIEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKST----VISLIPrfydPREGEILIDGQDIAH--ITKKSl 423
Cdd:COG1137     2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTtfymIVGLVK----PDSGRIFLDGEDITHlpMHKRA- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 424 RQQLAYVSQQPYLFEG-TIRDNI----------RYGRPEATDAEVEEaarLAYAHdfISAQPqgyetpvgenGVTLSGGQ 492
Cdd:COG1137    77 RLGIGYLPQEASIFRKlTVEDNIlavlelrklsKKEREERLEELLEE---FGITH--LRKSK----------AYSLSGGE 141

                         170       180
                  ....*....|....*....|.
gi 1582666899 493 RQRLSIARALVRNAPILLLDE 513
Cdd:COG1137   142 RRRVEIARALATNPKFILLDE 162

cbiO

PRK13634

cobalt transporter ATP-binding subunit; Provisional

352-567

2.59e-19

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 88.54 E-value: 2.59e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES-----VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITK----KS 422
Cdd:PRK13634    3 ITFQKVEHRYQYKTpferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKnkklKP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 423 LRQQLAYVSQQP--YLFEGTIRDNIRYGrPEATDAEVEEAARLAYA--------HDFISAQPqgYEtpvgengvtLSGGQ 492
Cdd:PRK13634   83 LRKKVGIVFQFPehQLFEETVEKDICFG-PMNFGVSEEDAKQKAREmielvglpEELLARSP--FE---------LSGGQ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 493 RQRLSIARALVRNAPILLLDEATSALDTeseaavqKALDEAMS---------GRTVVVIAHRLSTVVR-ADKIVVMQQGR 562
Cdd:PRK13634  151 MRRVAIAGVLAMEPEVLVLDEPTAGLDP-------KGRKEMMEmfyklhkekGLTTVLVTHSMEDAARyADQIVVMHKGT 223


                  ....*
gi 1582666899 563 VVEEG 567
Cdd:PRK13634  224 VFLQG 228

TagH

COG1134

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...

366-568

3.76e-19

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

Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 87.06 E-value: 3.76e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 366 VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQdIAhitkkSLrqqLAY-VSQQPYLfegTIRDN 444
Cdd:COG1134    41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VS-----AL---LELgAGFHPEL---TGREN 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 445 IR-----YG-RPEATDAEVEEAARLAYAHDFIsaqpqgyETPVGengvTLSGGQRQRLSIARALVRNAPILLLDEATSAL 518
Cdd:COG1134   109 IYlngrlLGlSRKEIDEKFDEIVEFAELGDFI-------DQPVK----TYSSGMRARLAFAVATAVDPDILLVDEVLAVG 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1582666899 519 DtesEAAVQKALDEAM----SGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGN 568
Cdd:COG1134   178 D---AAFQKKCLARIRelreSGRTVIFVSHSMGAVRRlCDRAIWLEKGRLVMDGD 229

PRK11831

phospholipid ABC transporter ATP-binding protein MlaF;

352-577

4.65e-19

phospholipid ABC transporter ATP-binding protein MlaF;

Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 87.51 E-value: 4.65e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSL---RQQLA 428
Cdd:PRK11831    8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytvRKRMS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 429 YVSQQPYLF-EGTIRDNIRYGRPEATDAEVE----------EAARLAYAHDFISAQpqgyetpvgengvtLSGGQRQRLS 497
Cdd:PRK11831   88 MLFQSGALFtDMNVFDNVAYPLREHTQLPAPllhstvmmklEAVGLRGAAKLMPSE--------------LSGGMARRAA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 498 IARALVRNAPILLLDEATSALDTESEAAVQKALDEAMS--GRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHETLAK 574
Cdd:PRK11831  154 LARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSalGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQALQA 233


                  ...
gi 1582666899 575 VSD 577
Cdd:PRK11831  234 NPD 236

cbiO

PRK13643

energy-coupling factor transporter ATPase;

352-592

8.53e-19

energy-coupling factor transporter ATPase;

Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 87.10 E-value: 8.53e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNES-----VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITK----KS 422
Cdd:PRK13643    2 IKFEKVNYTYQPNSpfasrALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqkeiKP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 423 LRQQLAYVSQQP--YLFEGTIRDNIRYGrPEATDAEVEEAARLAYAH-DFISAQPQGYETPVGEngvtLSGGQRQRLSIA 499
Cdd:PRK13643   82 VRKKVGVVFQFPesQLFEETVLKDVAFG-PQNFGIPKEKAEKIAAEKlEMVGLADEFWEKSPFE----LSGGQMRRVAIA 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 500 RALVRNAPILLLDEATSALDTESEAAVQKALDEA-MSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHETLAKVSD 577
Cdd:PRK13643  157 GILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVADyADYVYLLEKGHIISCGTPSDVFQEVD 236

                         250
                  ....*....|....*
gi 1582666899 578 GLYArlNNLQRPSAS 592
Cdd:PRK13643  237 FLKA--HELGVPKAT 249

ABC_6TM_exporter_like

cd18565

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...

68-326

2.38e-18

Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 86.08 E-value: 2.38e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  68 RADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYAHLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVL 147
Cdd:cd18565    49 PRGQLWLLGGLTVAAFLLESLFQYLSGVLWRRFAQRVQHDLRTDTYDHVQRLDMAFFEDRQTGDLMSVLNNDVNQLERFL 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 148 NLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYVSKRLR---SATREAV-HLNSHvlgaMQETIQGIA 223
Cdd:cd18565   129 DDGANSIIRVVVTVLGIGAILFYLNWQLALVALLPVPLIIAGTYWFQRRIEpryRAVREAVgDLNAR----LENNLSGIA 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 224 IVKAFTMEE-ELERkvnklIKGAESR---ANRIA-RLSERTSPLTESFAGFAVASVLAYAAYRSIyfNVPPGAFF----- 293
Cdd:cd18565   205 VIKAFTAEDfERER-----VADASEEyrdANWRAiRLRAAFFPVIRLVAGAGFVATFVVGGYWVL--DGPPLFTGtltvg 277

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1582666899 294 SFVTALLLA---YDPARRLARLQVQMERAVVNARMI 326
Cdd:cd18565   278 TLVTFLFYTqrlLWPLTRLGDLIDQYQRAMASAKRV 313

PRK10522

multidrug transporter membrane component/ATP-binding component; Provisional

330-565

2.93e-18

multidrug transporter membrane component/ATP-binding component; Provisional

Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 88.11 E-value: 2.93e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 330 LDMEPRQRDLPDARPLTVTQaRIEFRNVSFAYGNESVLSG-VSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEI 408
Cdd:PRK10522  302 LALAPYKAEFPRPQAFPDWQ-TLELRNVTFAYQDNGFSVGpINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEI 380

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 409 LIDGQDIAHITKKSLRQQLAYVSQQPYLFEGTIrdnirygRPEATDAEVEEA----ARLAYAHdfisaqpqgyETPVGEN 484
Cdd:PRK10522  381 LLDGKPVTAEQPEDYRKLFSAVFTDFHLFDQLL-------GPEGKPANPALVekwlERLKMAH----------KLELEDG 443

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 485 GVT---LSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAM--SGRTVVVIAHRLSTVVRADKIVVMQ 559
Cdd:PRK10522  444 RISnlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLqeMGKTIFAISHDDHYFIHADRLLEMR 523


                  ....*.
gi 1582666899 560 QGRVVE 565
Cdd:PRK10522  524 NGQLSE 529

PRK13651

cobalt transporter ATP-binding subunit; Provisional

351-589

2.95e-18

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 85.91 E-value: 2.95e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 351 RIEFRNVSFAYGNES-----VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITK----- 420
Cdd:PRK13651    2 QIKVKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKtkeke 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 421 -------------------KSLRQQLAYVSQ--QPYLFEGTIRDNIRYGrPEATDAEVEEAARLAYAHDFISAQPQGY-- 477
Cdd:PRK13651   82 kvleklviqktrfkkikkiKEIRRRVGVVFQfaEYQLFEQTIEKDIIFG-PVSMGVSKEEAKKRAAKYIELVGLDESYlq 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 478 ETPVGengvtLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEA-MSGRTVVVIAHRLSTVV-RADKI 555
Cdd:PRK13651  161 RSPFE-----LSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVLeWTKRT 235

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1582666899 556 VVMQQGRVVEEGN-HETLakvSDGLYARLNNLQRP 589
Cdd:PRK13651  236 IFFKDGKIIKDGDtYDIL---SDNKFLIENNMEPP 267

PhnK

COG1101

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

366-564

2.95e-18

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

Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 84.75 E-value: 2.95e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 366 VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIahiTKKSLRQQLAYVS---QQPYLfeGTir 442
Cdd:COG1101    21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDV---TKLPEYKRAKYIGrvfQDPMM--GT-- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 443 dnirygrpeATDAEVEE-------------------AARLAYAHDFISAQPQGYE----TPVGengvTLSGGQRQRLSIA 499
Cdd:COG1101    94 ---------APSMTIEEnlalayrrgkrrglrrgltKKRRELFRELLATLGLGLEnrldTKVG----LLSGGQRQALSLL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1582666899 500 RALVRNAPILLLDEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVV 564
Cdd:COG1101   161 MATLTKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNMEQALDyGNRLIMMHEGRII 228

lolD

PRK11629

lipoprotein-releasing ABC transporter ATP-binding protein LolD;

366-566

3.00e-18

lipoprotein-releasing ABC transporter ATP-binding protein LolD;

Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 84.10 E-value: 3.00e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 366 VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHIT---KKSLR-QQLAYVSQQPYLF-EGT 440
Cdd:PRK11629   24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSsaaKAELRnQKLGFIYQFHHLLpDFT 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 441 IRDNIryGRP----EATDAEVEEAARlayahDFISAqpQGYETPVGENGVTLSGGQRQRLSIARALVRNAPILLLDEATS 516
Cdd:PRK11629  104 ALENV--AMPlligKKKPAEINSRAL-----EMLAA--VGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTG 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1582666899 517 ALDTESEAAVQKALDE--AMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEE 566
Cdd:PRK11629  175 NLDARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226

PRK13540

cytochrome c biogenesis protein CcmA; Provisional

356-553

3.44e-18

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 83.08 E-value: 3.44e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 356 NVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIahitKKSL---RQQLAYVSQ 432
Cdd:PRK13540    6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLctyQKQLCFVGH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 433 Q----PYLfegTIRDNIRYG-RPEATDAEVEEAARLAYAHDFIsaqpqgyETPVGengvTLSGGQRQRLSIARALVRNAP 507
Cdd:PRK13540   82 RsginPYL---TLRENCLYDiHFSPGAVGITELCRLFSLEHLI-------DYPCG----LLSSGQKRQVALLRLWMSKAK 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1582666899 508 ILLLDEATSALDTES-EAAVQKALDEAMSGRTVVVIAHRLSTVVRAD 553
Cdd:PRK13540  148 LWLLDEPLVALDELSlLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194

nikD

PRK10418

nickel transporter ATP-binding protein NikD; Provisional

351-572

6.98e-18

nickel transporter ATP-binding protein NikD; Provisional

Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 83.60 E-value: 6.98e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 351 RIEFRNVSFAYGNESVlSGVSFTAEGGATTALVGPSGAGKS----TVISLIPRFYDPREGEILIDGQDIAhitKKSLR-Q 425
Cdd:PRK10418    4 QIELRNIALQAAQPLV-HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA---PCALRgR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 426 QLAYVSQQP-YLFEG--TIRDNIR-----YGRP--EATDAEVEEAARLAYAHDFISAQPqgYEtpvgengvtLSGGQRQR 495
Cdd:PRK10418   80 KIATIMQNPrSAFNPlhTMHTHARetclaLGKPadDATLTAALEAVGLENAARVLKLYP--FE---------MSGGMLQR 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 496 LSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGRT--VVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHETL 572
Cdd:PRK10418  149 MMIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRAlgMLLVTHDMGVVARlADDVAVMSHGRIVEQGDVETL 228

nikE

PRK10419

nickel ABC transporter ATP-binding protein NikE;

356-566

7.16e-18

nickel ABC transporter ATP-binding protein NikE;

Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 83.97 E-value: 7.16e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 356 NVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHIT---KKSLRQQLAYVSQ 432
Cdd:PRK10419   17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNraqRKAFRRDIQMVFQ 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 433 QPYLF---EGTIRDNIRYGRPEATDaeVEEAARLAYAHDFISA----------QPQgyetpvgengvTLSGGQRQRLSIA 499
Cdd:PRK10419   97 DSISAvnpRKTVREIIREPLRHLLS--LDKAERLARASEMLRAvdlddsvldkRPP-----------QLSGGQLQRVCLA 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 500 RALVRNAPILLLDEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEE 566
Cdd:PRK10419  164 RALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKlqQQFGTACLFITHDLRLVERfCQRVMVMDNGQIVET 233

ccmA

TIGR01189

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...

352-524

8.22e-18

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: 82.02 E-value: 8.22e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHiTKKSLRQQLAYVS 431
Cdd:TIGR01189   1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAE-QRDEPHENILYLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYL-FEGTIRDNIRYGRP--EATDAEVEEAARLAYAHDFisaqpqgYETPVGengvTLSGGQRQRLSIARALVRNAPI 508
Cdd:TIGR01189  80 HLPGLkPELSALENLHFWAAihGGAQRTIEDALAAVGLTGF-------EDLPAA----QLSAGQQRRLALARLWLSRRPL 148

                         170
                  ....*....|....*.
gi 1582666899 509 LLLDEATSALDTESEA 524
Cdd:TIGR01189 149 WILDEPTTALDKAGVA 164

rim_protein

TIGR01257

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...

380-567

1.14e-17

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]

Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 87.38 E-value: 1.14e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  380 TALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIaHITKKSLRQQLAYVSQQPYLFEG-TIRDNIRY-----GRPEaT 453
Cdd:TIGR01257  959 TAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-ETNLDAVRQSLGMCPQHNILFHHlTVAEHILFyaqlkGRSW-E 1036

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  454 DAEVEEAARLayahdfisaQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEA 533
Cdd:TIGR01257 1037 EAQLEMEAML---------EDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY 1107

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1582666899  534 MSGRTVVVIAHRLSTV-VRADKIVVMQQGRVVEEG 567
Cdd:TIGR01257 1108 RSGRTIIMSTHHMDEAdLLGDRIAIISQGRLYCSG 1142

tauB

PRK11248

taurine ABC transporter ATP-binding subunit;

356-565

3.68e-17

taurine ABC transporter ATP-binding subunit;

Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 81.67 E-value: 3.68e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 356 NVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIahitkKSLRQQLAYVSQQPY 435
Cdd:PRK11248    6 HLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-----EGPGAERGVVFQNEG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 436 LFE-GTIRDNIRYGRPEATdaeVEEAARLAYAHDFISAqpqgyetpVGENGV------TLSGGQRQRLSIARALVRNAPI 508
Cdd:PRK11248   81 LLPwRNVQDNVAFGLQLAG---VEKMQRLEIAHQMLKK--------VGLEGAekryiwQLSGGQRQRVGIARALAANPQL 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1582666899 509 LLLDEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRL-STVVRADKIVVMQ--QGRVVE 565
Cdd:PRK11248  150 LLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITHDIeEAVFMATELVLLSpgPGRVVE 211

PRK09984

phosphonate ABC transporter ATP-binding protein;

349-588

4.02e-17

phosphonate ABC transporter ATP-binding protein;

Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 81.60 E-value: 4.02e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 349 QARIEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVI----SLIPRFYDPrEGEILIDGQDI------AHI 418
Cdd:PRK09984    2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLrhlsGLITGDKSA-GSHIELLGRTVqregrlARD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 419 TKKSlRQQLAYVSQQPYLFEG-TIRDNI---------------RYGRPEATDAEVEEAARLA---YAHDFISaqpqgyet 479
Cdd:PRK09984   81 IRKS-RANTGYIFQQFNLVNRlSVLENVligalgstpfwrtcfSWFTREQKQRALQALTRVGmvhFAHQRVS-------- 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 480 pvgengvTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRLSTVVR-ADKIV 556
Cdd:PRK09984  152 -------TLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDinQNDGITVVVTLHQVDYALRyCERIV 224

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1582666899 557 VMQQGRVVEEGNHETLAKVS-DGLYARLNNLQR 588
Cdd:PRK09984  225 ALRQGHVFYDGSSQQFDNERfDHLYRSINRVEE 257

ABC_6TM_exporter_like

cd18540

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar ...

35-323

4.98e-17

Pssm-ID: 349984 [Multi-domain] Cd Length: 295 Bit Score: 81.76 E-value: 4.98e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  35 YVFAIACLIVVALSTAFTAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYA 114
Cdd:cd18540     4 LILLIILMLLVALLDAVFPLLTKYAIDHFITPGTLDGLTGFILLYLGLILIQALSVFLFIRLAGKIEMGVSYDLRKKAFE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 115 HLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYVS 194
Cdd:cd18540    84 HLQTLSFSYFDKTPVGWIMARVTSDTQRLGEIISWGLVDLVWGITYMIGILIVMLILNWKLALIVLAVVPVLAVVSIYFQ 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 195 KRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSPLTESFAGFAVASV 274
Cdd:cd18540   164 KKILKAYRKVRKINSRITGAFNEGITGAKTTKTLVREEKNLREFKELTEEMRRASVRAARLSALFLPIVLFLGSIATALV 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1582666899 275 LAYAAYRSIYFNVPPGAFFSFVTALLLAYDPARRLARLQVQMERAVVNA 323
Cdd:cd18540   244 LWYGGILVLAGAITIGTLVAFISYATQFFEPIQQLARVLAELQSAQASA 292

PRK03695

vitamin B12-transporter ATPase; Provisional

367-575

5.69e-17

vitamin B12-transporter ATPase; Provisional

Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 80.75 E-value: 5.69e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 367 LSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYdPREGEILIDGQDIAHITKKSLRQQLAYVSQQP------------ 434
Cdd:PRK03695   12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQtppfampvfqyl 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 435 --YLFEGTirdnirygRPEATDAEVEEAARLAYAHDFIsaqpqgyETPVGengvTLSGGQRQR-------LSIARALVRN 505
Cdd:PRK03695   91 tlHQPDKT--------RTEAVASALNEVAEALGLDDKL-------GRSVN----QLSGGEWQRvrlaavvLQVWPDINPA 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1582666899 506 APILLLDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG------NHETLAKV 575
Cdd:PRK03695  152 GQLLLLDEPMNSLDVAQQAALDRLLSElCQQGIAVVMSSHDLNHTLRhADRVWLLKQGKLLASGrrdevlTPENLAQV 229

met_CoM_red_A2

TIGR03269

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...

352-575

6.13e-17

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: 84.08 E-value: 6.13e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRF--YDPREGEIL-------------------- 409
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvge 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 410 -------------IDGQDIAHITKKSLRQQLAYVSQQPYLFEG--TIRDNIRYGRPEAtDAEVEEAarLAYAHDFISAQP 474
Cdd:TIGR03269  81 pcpvcggtlepeeVDFWNLSDKLRRRIRKRIAIMLQRTFALYGddTVLDNVLEALEEI-GYEGKEA--VGRAVDLIEMVQ 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 475 QGYE-TPVGENgvtLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAM--SGRTVVVIAHRLSTVVR 551
Cdd:TIGR03269 158 LSHRiTHIARD---LSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkaSGISMVLTSHWPEVIED 234

                         250       260
                  ....*....|....*....|....*
gi 1582666899 552 -ADKIVVMQQGRVVEEGNHETLAKV 575
Cdd:TIGR03269 235 lSDKAIWLENGEIKEEGTPDEVVAV 259

ugpC

PRK11650

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

350-563

6.33e-17

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

Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 82.58 E-value: 6.33e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 350 ARIEFRNVSFAY-GNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSlrQQLA 428
Cdd:PRK11650    2 AGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD--RDIA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 429 YVSQQ----PYLfegTIRDNIRYG---R--PEAT-DAEVEEAARLAYAHDFISAQPQgyetpvgengvTLSGGQRQRLSI 498
Cdd:PRK11650   80 MVFQNyalyPHM---SVRENMAYGlkiRgmPKAEiEERVAEAARILELEPLLDRKPR-----------ELSGGQRQRVAM 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 499 ARALVRNAPILLLDEATSALDTESEAA-------VQKALdeamsGRTVVVIAH-RLSTVVRADKIVVMQQGRV 563
Cdd:PRK11650  146 GRAIVREPAVFLFDEPLSNLDAKLRVQmrleiqrLHRRL-----KTTSLYVTHdQVEAMTLADRVVVMNGGVA 213

ABC_Carb_Monos_II

cd03215

Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...

350-563

6.53e-17

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: 79.01 E-value: 6.53e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 350 ARIEFRNVSFAygneSVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHIT-KKSLRQQLA 428
Cdd:cd03215     3 PVLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSpRDAIRAGIA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 429 YVSqqpylfegtirdnirygrpeatdaevEEAARLAYAHDFisaqpqgyetPVGEN---GVTLSGGQRQRLSIARALVRN 505
Cdd:cd03215    79 YVP--------------------------EDRKREGLVLDL----------SVAENialSSLLSGGNQQKVVLARWLARD 122

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 506 APILLLDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRV 563
Cdd:cd03215   123 PRVLILDEPTRGVDVGAKAEIYRLIRElADAGKAVLLISSELDELLGlCDRILVMYEGRI 182

ABC_ABC_ChvD

TIGR03719

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...

352-548

1.01e-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: 83.45 E-value: 1.01e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIdGQDIahitkkslrqQLAYVS 431
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLAYVD 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYLFEG--TIRDNIRYGRPEATDAEVEEAARlAYAHDF-ISAQPQgyETPVGEngvtLSGGQRQRLSIARALVRNAPI 508
Cdd:TIGR03719 392 QSRDALDPnkTVWEEISGGLDIIKLGKREIPSR-AYVGRFnFKGSDQ--QKKVGQ----LSGGERNRVHLAKTLKSGGNV 464

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1582666899 509 LLLDEATSALDTESEAAVQKALDEaMSGrTVVVIAH------RLST 548
Cdd:TIGR03719 465 LLLDEPTNDLDVETLRALEEALLN-FAG-CAVVISHdrwfldRIAT 508

livG

PRK11300

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

348-567

1.44e-16

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

Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 79.65 E-value: 1.44e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 348 TQARIEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHIT-KKSLRQQ 426
Cdd:PRK11300    2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPgHQIARMG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 427 LAYVSQQPYLF-EGTIRDNIRYGR---------------PEATDAEVEEAARLAYAHDFIsaqpqGYETPVGENGVTLSG 490
Cdd:PRK11300   82 VVRTFQHVRLFrEMTVIENLLVAQhqqlktglfsgllktPAFRRAESEALDRAATWLERV-----GLLEHANRQAGNLAY 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 491 GQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMS--GRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:PRK11300  157 GQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNehNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANG 236

livF

PRK11614

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

349-572

2.24e-16

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

Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 78.77 E-value: 2.24e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 349 QARIEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRfyDPR--EGEILIDGQDIAHI-TKKSLRQ 425
Cdd:PRK11614    3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG--DPRatSGRIVFDGKDITDWqTAKIMRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 426 QLAYVSQQPYLFEG-TIRDNIRYGRPEATDAEVEEaaRLAYAHDFIsaqPQGYETPVGENGvTLSGGQRQRLSIARALVR 504
Cdd:PRK11614   81 AVAIVPEGRRVFSRmTVEENLAMGGFFAERDQFQE--RIKWVYELF---PRLHERRIQRAG-TMSGGEQQMLAIGRALMS 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 505 NAPILLLDEATSALdteSEAAVQKALDEAM----SGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHETL 572
Cdd:PRK11614  155 QPRLLLLDEPSLGL---APIIIQQIFDTIEqlreQGMTIFLVEQNANQALKlADRGYVLENGHVVLEDTGDAL 224

ABCG_PDR_domain1

cd03233

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...

354-564

3.67e-16

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: 77.30 E-value: 3.67e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 354 FRNVSF----AYGNESVLSGVSFTAEGGATTALVGPSGAGKST---VISLIPRFYDPREGEILIDGQDiAHITKKSLRQQ 426
Cdd:cd03233     6 WRNISFttgkGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkALANRTEGNVSVEGDIHYNGIP-YKEFAEKYPGE 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 427 LAYVSQQ----PYLfegTIRDNIrygrpeatdaeveEAARLAYAHDFISaqpqgyetpvgenGVtlSGGQRQRLSIARAL 502
Cdd:cd03233    85 IIYVSEEdvhfPTL---TVRETL-------------DFALRCKGNEFVR-------------GI--SGGERKRVSIAEAL 133

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 503 VRNAPILLLDEATSALDTESeaavqkALDEAMSGRTVVVIAhRLSTVVRA-----------DKIVVMQQGRVV 564
Cdd:cd03233   134 VSRASVLCWDNSTRGLDSST------ALEILKCIRTMADVL-KTTTFVSLyqasdeiydlfDKVLVLYEGRQI 199

ABC_6TM_Pgp_ABCB1_D1_like

cd18577

Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...

35-256

5.44e-16

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: 79.06 E-value: 5.44e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  35 YVFAIACLIVVALSTAFTAWIMRAIIDeAFANRRA---------DVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIV 105
Cdd:cd18577     1 LIIGLLAAIAAGAALPLMTIVFGDLFD-AFTDFGSgesspdeflDDVNKYALYFVYLGIGSFVLSYIQTACWTITGERQA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 106 ARYQRRLYAHLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPP 185
Cdd:cd18577    80 RRIRKRYLKALLRQDIAWFDKNGAGELTSRLTSDTNLIQDGIGEKLGLLIQSLSTFIAGFIIAFIYSWKLTLVLLATLPL 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582666899 186 LLYALRYVSKRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLS 256
Cdd:cd18577   160 IAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALEKARKAGIKKGLVS 230

PRK10895

lipopolysaccharide ABC transporter ATP-binding protein; Provisional

350-572

6.74e-16

lipopolysaccharide ABC transporter ATP-binding protein; Provisional

Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 77.63 E-value: 6.74e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 350 ARIEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKST----VISLIPRfydpREGEILIDGQDIAHIT-KKSLR 424
Cdd:PRK10895    2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTtfymVVGIVPR----DAGNIIIDDEDISLLPlHARAR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 425 QQLAYVSQQPYLFEG-----------TIRDNIRYGRPEATDAEVEEAARLAYAHDFIsaqpqgyetpvgenGVTLSGGQR 493
Cdd:PRK10895   78 RGIGYLPQEASIFRRlsvydnlmavlQIRDDLSAEQREDRANELMEEFHIEHLRDSM--------------GQSLSGGER 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 494 QRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAM-SGRTVVVIAHRL-STVVRADKIVVMQQGRVVEEGNHET 571
Cdd:PRK10895  144 RRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTE 223


                  .
gi 1582666899 572 L 572
Cdd:PRK10895  224 I 224

ABC_NatA_like

cd03267

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...

366-567

1.01e-15

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: 76.99 E-value: 1.01e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 366 VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDG-----QDIAHITKKSL----RQQLAY---VSQQ 433
Cdd:cd03267    36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpwkRRKKFLRRIGVvfgqKTQLWWdlpVIDS 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 434 PYLfegtIRD--NIRYGRPEATDAEVEEAARLAYAHDfisaqpqgyeTPVGEngvtLSGGQRQRLSIARALVRNAPILLL 511
Cdd:cd03267   116 FYL----LAAiyDLPPARFKKRLDELSELLDLEELLD----------TPVRQ----LSLGQRMRAEIAAALLHEPEILFL 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1582666899 512 DEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:cd03267   178 DEPTIGLDVVAQENIRNFLKEynRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236

PRK10261

glutathione transporter ATP-binding protein; Provisional

370-567

1.10e-15

glutathione transporter ATP-binding protein; Provisional

Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 80.28 E-value: 1.10e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 370 VSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITK---KSLRQQLAYVSQQPYLF---EGTIRD 443
Cdd:PRK10261  343 VSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQDPYASldpRQTVGD 422

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 444 NIR-----YGRPEATDAeveeAARLAYAHDFISAQPQ-GYETPVgengvTLSGGQRQRLSIARALVRNAPILLLDEATSA 517
Cdd:PRK10261  423 SIMeplrvHGLLPGKAA----AARVAWLLERVGLLPEhAWRYPH-----EFSGGQRQRICIARALALNPKVIIADEAVSA 493

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 518 LDTESEAAVQKALDEAMS--GRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:PRK10261  494 LDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVERiSHRVAVMYLGQIVEIG 546

PRK11819

putative ABC transporter ATP-binding protein; Reviewed

352-544

1.83e-15

putative ABC transporter ATP-binding protein; Reviewed

Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 79.39 E-value: 1.83e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIdGQDIahitkkslrqQLAYVS 431
Cdd:PRK11819  325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETV----------KLAYVD 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQpylfegtiRDNIRygrPEATDAEV-------------EEAARlAY--AHDFISAQPQgyeTPVGengvTLSGGQRQRL 496
Cdd:PRK11819  394 QS--------RDALD---PNKTVWEEisggldiikvgnrEIPSR-AYvgRFNFKGGDQQ---KKVG----VLSGGERNRL 454

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1582666899 497 SIARALVRNAPILLLDEATSALDTESEAAVQKALDEaMSGrTVVVIAH 544
Cdd:PRK11819  455 HLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLE-FPG-CAVVISH 500

ssuB

PRK11247

aliphatic sulfonates transport ATP-binding subunit; Provisional

355-563

3.08e-15

aliphatic sulfonates transport ATP-binding subunit; Provisional

Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 75.87 E-value: 3.08e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 355 RNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHItkkslRQQLAYVSQQP 434
Cdd:PRK11247   16 NAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEA-----REDTRLMFQDA 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 435 YLFE-GTIRDNIRYG-----RPEATDAEveEAARLA-YAHDFISAqpqgyetpvgengvtLSGGQRQRLSIARALVRNAP 507
Cdd:PRK11247   91 RLLPwKKVIDNVGLGlkgqwRDAALQAL--AAVGLAdRANEWPAA---------------LSGGQKQRVALARALIHRPG 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 508 ILLLDEATSALDTESEAAVQKaLDEAM---SGRTVVVIAHRLS-TVVRADKIVVMQQGRV 563
Cdd:PRK11247  154 LLLLDEPLGALDALTRIEMQD-LIESLwqqHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212

ntrCD

TIGR01184

nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...

367-561

6.18e-15

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: 74.42 E-value: 6.18e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 367 LSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYvSQQPYLfegTIRDNIR 446
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMVVFQNY-SLLPWL---TVRENIA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 447 YGRPEAT-DAEVEEAARLAYAHDFISAQPQGYETPVGEngvtLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAA 525
Cdd:TIGR01184  77 LAVDRVLpDLSKSERRAIVEEHIALVGLTEAADKRPGQ----LSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1582666899 526 VQKALDEAM--SGRTVVVIAHRL-STVVRADKIVVMQQG 561
Cdd:TIGR01184 153 LQEELMQIWeeHRVTVLMVTHDVdEALLLSDRVVMLTNG 191

MglA

COG1129

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

328-566

6.27e-15

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

Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 77.37 E-value: 6.27e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 328 ELLDMEPRqRDLPDARPLtvtqarIEFRNVSfaygNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGE 407
Cdd:COG1129   240 ELEDLFPK-RAAAPGEVV------LEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGE 308

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 408 ILIDGQDIAHIT-KKSLRQQLAYVS----QQPYLFEGTIRDNI------RYGRPEATD--AEVEEAARlaYAHDFiSAQP 474
Cdd:COG1129   309 IRLDGKPVRIRSpRDAIRAGIAYVPedrkGEGLVLDLSIRENItlasldRLSRGGLLDrrRERALAEE--YIKRL-RIKT 385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 475 QGYETPVGengvTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLSTVVR-A 552
Cdd:COG1129   386 PSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRElAAEGKAVIVISSELPELLGlS 461

                         250
                  ....*....|....
gi 1582666899 553 DKIVVMQQGRVVEE 566
Cdd:COG1129   462 DRILVMREGRIVGE 475

znuC

PRK09544

high-affinity zinc transporter ATPase; Reviewed

352-560

1.09e-14

high-affinity zinc transporter ATPase; Reviewed

Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 73.99 E-value: 1.09e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQdiahitkksLRqqLAYVS 431
Cdd:PRK09544    5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------LR--IGYVP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYL---FEGTIRDNIRYgRPEATDAEVEEAARLAYAHDFISAQPQgyetpvgengvTLSGGQRQRLSIARALVRNAPI 508
Cdd:PRK09544   74 QKLYLdttLPLTVNRFLRL-RPGTKKEDILPALKRVQAGHLIDAPMQ-----------KLSGGETQRVLLARALLNRPQL 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1582666899 509 LLLDEATSALDTESEAAVQKALDEAMS--GRTVVVIAHRLSTVV-RADKIVVMQQ 560
Cdd:PRK09544  142 LVLDEPTQGVDVNGQVALYDLIDQLRRelDCAVLMVSHDLHLVMaKTDEVLCLNH 196

GguA

NF040905

sugar ABC transporter ATP-binding protein;

367-565

2.15e-14

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 75.98 E-value: 2.15e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 367 LSGVSFTAEGGATTALVGPSGAGKST---VISLI-PrfYDPREGEILIDGQDIAHitkKSLR-----------QQLAYVs 431
Cdd:NF040905   17 LDDVNLSVREGEIHALCGENGAGKSTlmkVLSGVyP--HGSYEGEILFDGEVCRF---KDIRdsealgiviihQELALI- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 qqPYLfegTIRDNIRYGRPEAT------DAEVEEAARLaYAHDFISAQPQgyeTPVGENGVtlsgGQRQRLSIARALVRN 505
Cdd:NF040905   91 --PYL---SIAENIFLGNERAKrgvidwNETNRRAREL-LAKVGLDESPD---TLVTDIGV----GKQQLVEIAKALSKD 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1582666899 506 APILLLDEATSAL-DTESEAAVQKALDEAMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVE 565
Cdd:NF040905  158 VKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219

3a01205

TIGR00956

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

353-561

2.64e-14

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

Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 76.69 E-value: 2.64e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  353 EFRNVSFAYGNES----VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDP---REGEILIDGQDIahitKKSLRQ 425
Cdd:TIGR00956  761 HWRNLTYEVKIKKekrvILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPL----DSSFQR 836

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  426 QLAYVSQQP-YLFEGTIRDNIRYG----RP-EATDAE----VEEAARLAYAHDFISAQpqgyetpVGENGVTLSGGQRQR 495
Cdd:TIGR00956  837 SIGYVQQQDlHLPTSTVRESLRFSaylrQPkSVSKSEkmeyVEEVIKLLEMESYADAV-------VGVPGEGLNVEQRKR 909

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  496 LSIARALVRNAPILL-LDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLSTVVRA--DKIVVMQQG 561
Cdd:TIGR00956  910 LTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKlADHGQAILCTIHQPSAILFEefDRLLLLQKG 979

ABC_6TM_HetC_like

cd18568

Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ...

36-312

3.42e-14

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: 73.36 E-value: 3.42e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  36 VFAIACLI-VVALSTAFTAWImraIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYA 114
Cdd:cd18568     7 ILLASLLLqLLGLALPLFTQI---ILDRVLVHKNISLLNLILIGLLIVGIFQILLSAVRQYLLDYFANRIDLSLLSDFYK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 115 HLMTLSVGFFSEARSAHIAAQVSQNvSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYVS 194
Cdd:cd18568    84 HLLSLPLSFFASRKVGDIITRFQEN-QKIRRFLTRSALTTILDLLMVFIYLGLMFYYNLQLTLIVLAFIPLYVLLTLLSS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 195 KRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEEL----ERKVNKLIKgAESRANRIARLSERTSPLTESFAGfa 270
Cdd:cd18568   163 PKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAERPIrwrwENKFAKALN-TRFRGQKLSIVLQLISSLINHLGT-- 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1582666899 271 vASVLAYAAYRSIYFNVPPGAFFSFVTALLLAYDPARRLARL 312
Cdd:cd18568   240 -IAVLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGL 280

met_CoM_red_A2

TIGR03269

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...

352-570

3.74e-14

Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 75.22 E-value: 3.74e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAY-----GNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILID-GQDIAHITKKSL-- 423
Cdd:TIGR03269 280 IKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPdg 359

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 424 ----RQQLAYVSQQPYLF-EGTIRDNIrygrPEATDAEV-EEAARLAYAHDFISAqpqGYETPVGENGV-----TLSGGQ 492
Cdd:TIGR03269 360 rgraKRYIGILHQEYDLYpHRTVLDNL----TEAIGLELpDELARMKAVITLKMV---GFDEEKAEEILdkypdELSEGE 432

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 493 RQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMS--GRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNH 569
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDvCDRAALMRDGKIVKIGDP 512


                  .
gi 1582666899 570 E 570
Cdd:TIGR03269 513 E 513

ABC_6TM_PrtD_LapB_HlyB_like

cd18783

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...

38-326

6.02e-14

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: 72.55 E-value: 6.02e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  38 AIACLIVVALSTAfTAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYAHLM 117
Cdd:cd18783     8 AIASLILHVLALA-PPIFFQIVIDKVLVHQSYSTLYVLTIGVVIALLFEGILGYLRRYLLLVATTRIDARLALRTFDRLL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 118 TLSVGFFSEARSAHIAAQVSQnVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYVSKRL 197
Cdd:cd18783    87 SLPIDFFERTPAGVLTKHMQQ-IERIRQFLTGQLFGTLLDATSLLVFLPVLFFYSPTLALVVLAFSALIALIILAFLPPF 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 198 RSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSPLTESFAGFAVASVLAY 277
Cdd:cd18783   166 RRRLQALYRAEGERQAFLVETVHGIRTVKSLALEPRQRREWDERVARAIRARFAVGRLSNWPQTLTGPLEKLMTVGVIWV 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1582666899 278 AAYRSIYFNVPPGAFFSF------VTAlllaydPARRLARLQVQMERAVVNARMI 326
Cdd:cd18783   246 GAYLVFAGSLTVGALIAFnmlagrVAG------PLVQLAGLVQEYQEARLSVRML 294

PRK09700

D-allose ABC transporter ATP-binding protein AlsA;

352-567

6.95e-14

D-allose ABC transporter ATP-binding protein AlsA;

Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 74.44 E-value: 6.95e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKK-SLRQQLAYV 430
Cdd:PRK09700    6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGII 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 431 SQQPYLF-EGTIRDNIRYGR---------PEATDAEVEEAA-----RLAYAHDFisaqpqgyETPVGEngvtLSGGQRQR 495
Cdd:PRK09700   86 YQELSVIdELTVLENLYIGRhltkkvcgvNIIDWREMRVRAammllRVGLKVDL--------DEKVAN----LSISHKQM 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582666899 496 LSIARALVRNAPILLLDEATSALdTESEA----AVQKALDEamSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:PRK09700  154 LEIAKTLMLDAKVIIMDEPTSSL-TNKEVdylfLIMNQLRK--EGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227

NupO

COG3845

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...

341-566

1.05e-13

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

Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 73.52 E-value: 1.05e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 341 DARPLTVTQARIEFRNVSFA-YGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHIT 419
Cdd:COG3845   247 EKAPAEPGEVVLEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 420 KKSLRQQ-LAYVSQQPyLFEG-----TIRDNI---RYGRPE-ATDAEVEEAARLAYAHDFISA---QPQGYETPVGengv 486
Cdd:COG3845   327 PRERRRLgVAYIPEDR-LGRGlvpdmSVAENLilgRYRRPPfSRGGFLDRKAIRAFAEELIEEfdvRTPGPDTPAR---- 401

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 487 TLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAM-SGRTVVVIAHRLSTVVR-ADKIVVMQQGRVV 564
Cdd:COG3845   402 SLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRdAGAAVLLISEDLDEILAlSDRIAVMYEGRIV 481


                  ..
gi 1582666899 565 EE 566
Cdd:COG3845   482 GE 483

modC

PRK11144

molybdenum ABC transporter ATP-binding protein ModC;

380-570

1.06e-13

molybdenum ABC transporter ATP-binding protein ModC;

Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 72.60 E-value: 1.06e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 380 TALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKK-SL---RQQLAYVSQQPYLF-EGTIRDNIRYGRPEATD 454
Cdd:PRK11144   27 TAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiCLppeKRRIGYVFQDARLFpHYKVRGNLRYGMAKSMV 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 455 AEVEEAARLAyahdfisaqpqGYETPVGENGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALdEAM 534
Cdd:PRK11144  107 AQFDKIVALL-----------GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYL-ERL 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1582666899 535 SGRT---VVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHE 570
Cdd:PRK11144  175 AREInipILYVSHSLDEILRlADRVVVLEQGKVKAFGPLE 214

xylG

TIGR02633

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...

352-564

1.38e-13

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: 73.32 E-value: 1.38e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYdPR---EGEILIDGQDI-AHITKKSLRQQL 427
Cdd:TIGR02633   2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLkASNIRDTERAGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 428 AYVSQQPYLF-EGTIRDNIRYGRpEATdaevEEAARLAYAHDFISAQPQGYETPVGENGVT-----LSGGQRQRLSIARA 501
Cdd:TIGR02633  81 VIIHQELTLVpELSVAENIFLGN-EIT----LPGGRMAYNAMYLRAKNLLRELQLDADNVTrpvgdYGGGQQQLVEIAKA 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582666899 502 LVRNAPILLLDEATSALdTESEAAVQKAL--DEAMSGRTVVVIAHRLSTV-VRADKIVVMQQGRVV 564
Cdd:TIGR02633 156 LNKQARLLILDEPSSSL-TEKETEILLDIirDLKAHGVACVYISHKLNEVkAVCDTICVIRDGQHV 220

PRK11147

ABC transporter ATPase component; Reviewed

353-521

1.57e-13

ABC transporter ATPase component; Reviewed

Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 73.45 E-value: 1.57e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 353 EFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEIlidgqdiaHITKKslrQQLAYVSQ 432
Cdd:PRK11147  321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI--------HCGTK---LEVAYFDQ 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 433 -----QPylfEGTIRDNIRYGRPEATdaeVEEAAR--LAYAHDFISAqPQGYETPVGengvTLSGGQRQRLSIARALVRN 505
Cdd:PRK11147  390 hraelDP---EKTVMDNLAEGKQEVM---VNGRPRhvLGYLQDFLFH-PKRAMTPVK----ALSGGERNRLLLARLFLKP 458

                         170
                  ....*....|....*.
gi 1582666899 506 APILLLDEATSALDTE 521
Cdd:PRK11147  459 SNLLILDEPTNDLDVE 474

ABC_RNaseL_inhibitor_domain2

cd03237

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...

367-557

1.81e-13

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.

Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 70.51 E-value: 1.81e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 367 LSGVSFTAEGGATT-----ALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHitkkslRQQlaYVSQQpylFEGTI 441
Cdd:cd03237    10 LGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSY------KPQ--YIKAD---YEGTV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 442 RDNIRygrpeatdaeveEAARLAYAHDFIS---AQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAPILLLDEATSAL 518
Cdd:cd03237    79 RDLLS------------SITKDFYTHPYFKteiAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYL 146

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1582666899 519 DTESEAAVQKALDE-AMSG-RTVVVIAHR--LSTVVrADKIVV 557
Cdd:cd03237   147 DVEQRLMASKVIRRfAENNeKTAFVVEHDiiMIDYL-ADRLIV 188

ABC_6TM_ABCB10_like

cd18573

Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...

38-236

1.95e-13

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: 71.01 E-value: 1.95e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  38 AIACLIVVALSTAFTAWIMRAIIDEAFANRRADVVW-----IICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRL 112
Cdd:cd18573     1 ALALLLVSSAVTMSVPFAIGKLIDVASKESGDIEIFglslkTFALALLGVFVVGAAANFGRVYLLRIAGERIVARLRKRL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 113 YAHLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRY 192
Cdd:cd18573    81 FKSILRQDAAFFDKNKTGELVSRLSSDTSVVGKSLTQNLSDGLRSLVSGVGGIGMMLYISPKLTLVMLLVVPPIAVGAVF 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1582666899 193 VSKRLRSATREavHLNShvLGAM----QETIQGIAIVKAFTMEE-ELER 236
Cdd:cd18573   161 YGRYVRKLSKQ--VQDA--LADAtkvaEERLSNIRTVRAFAAERkEVER 205

ABC_6TM_Tm287_like

cd18548

Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...

36-297

2.99e-13

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: 70.51 E-value: 2.99e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  36 VFAIACLIVVALSTAFTAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYAH 115
Cdd:cd18548     2 ILAPLFKLLEVLLELLLPTLMADIIDEGIANGDLSYILRTGLLMLLLALLGLIAGILAGYFAAKASQGFGRDLRKDLFEK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 116 LMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYVSK 195
Cdd:cd18548    82 IQSFSFAEIDKFGTSSLITRLTNDVTQVQNFVMMLLRMLVRAPIMLIGAIIMAFRINPKLALILLVAIPILALVVFLIMK 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 196 RLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEE-ELER--KVNKLIKGAESRANRIARLserTSPLTESFAGFAVA 272
Cdd:cd18548   162 KAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDyEEERfdKANDDLTDTSLKAGRLMAL---LNPLMMLIMNLAIV 238

                         250       260
                  ....*....|....*....|....*
gi 1582666899 273 SVLAYAAYRSIYFNVPPGAFFSFVT 297
Cdd:cd18548   239 AILWFGGHLINAGSLQVGDLVAFIN 263

PRK13538

cytochrome c biogenesis heme-transporting ATPase CcmA;

368-544

5.81e-13

cytochrome c biogenesis heme-transporting ATPase CcmA;

Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.91 E-value: 5.81e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 368 SGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHItKKSLRQQLAYVSQQPYLF-EGTIRDNIR 446
Cdd:PRK13538   18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ-RDEYHQDLLYLGHQPGIKtELTALENLR 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 447 Y---GRPEATDAEVEEA-ARLAYAhdfisaqpqGYE-TPVGengvTLSGGQRQRLSIARALVRNAPILLLDEATSALDTE 521
Cdd:PRK13538   97 FyqrLHGPGDDEALWEAlAQVGLA---------GFEdVPVR----QLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163

                         170       180
                  ....*....|....*....|....
gi 1582666899 522 SEAAVQKALDE-AMSGRTVVVIAH 544
Cdd:PRK13538  164 GVARLEALLAQhAEQGGMVILTTH 187

oppD

PRK09473

oligopeptide transporter ATP-binding component; Provisional

345-568

6.92e-13

oligopeptide transporter ATP-binding component; Provisional

Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 70.14 E-value: 6.92e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 345 LTVTQARIEFRNVSfayGNESVLSGVSFTAEGGATTALVGPSGAGKS-TVISLIPRFydPREGEI----LIDGQDIAHIT 419
Cdd:PRK09473   13 LDVKDLRVTFSTPD---GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLL--AANGRIggsaTFNGREILNLP 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 420 KKSLR----QQLAYVSQ------QPYLFEGT-----IRDNIRYGRPEATDAEVE--EAARLAYAHDFISAQPQGYetpvg 482
Cdd:PRK09473   88 EKELNklraEQISMIFQdpmtslNPYMRVGEqlmevLMLHKGMSKAEAFEESVRmlDAVKMPEARKRMKMYPHEF----- 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 483 engvtlSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMS--GRTVVVIAHRLSTVVR-ADKIVVMQ 559
Cdd:PRK09473  163 ------SGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKRefNTAIIMITHDLGVVAGiCDKVLVMY 236


                  ....*....
gi 1582666899 560 QGRVVEEGN 568
Cdd:PRK09473  237 AGRTMEYGN 245

ycf16

CHL00131

sulfate ABC transporter protein; Validated

352-574

7.80e-13

sulfate ABC transporter protein; Validated

Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 68.51 E-value: 7.80e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKST---VISLIPRfYDPREGEILIDGQDIAHITKKSLRQQ-- 426
Cdd:CHL00131    8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTlskVIAGHPA-YKILEGDILFKGESILDLEPEERAHLgi 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 427 -LAYvsQQPYLFEG-TIRDNIR---------YGRPEATDAEVEEAarLAYAHDFISAQPQGYETPVGENgvtLSGGQRQR 495
Cdd:CHL00131   87 fLAF--QYPIEIPGvSNADFLRlaynskrkfQGLPELDPLEFLEI--INEKLKLVGMDPSFLSRNVNEG---FSGGEKKR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 496 LSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAM-SGRTVVVIAH--RLSTVVRADKIVVMQQGRVVEEGNhETL 572
Cdd:CHL00131  160 NEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMtSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGD-AEL 238


                  ..
gi 1582666899 573 AK 574
Cdd:CHL00131  239 AK 240

PLN03211

ABC transporter G-25; Provisional

365-567

1.05e-12

ABC transporter G-25; Provisional

Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.06 E-value: 1.05e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 365 SVLSGVSFTAEGGATTALVGPSGAGKSTVISLIP-RFY-DPREGEILIDGQDIahiTKKSLRQqLAYVSQQPYLFEG-TI 441
Cdd:PLN03211   82 TILNGVTGMASPGEILAVLGPSGSGKSTLLNALAgRIQgNNFTGTILANNRKP---TKQILKR-TGFVTQDDILYPHlTV 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 442 RDNIRYGRPEATDAEVEEAARLAYAHDFIS--AQPQGYETPVGENGVT-LSGGQRQRLSIARALVRNAPILLLDEATSAL 518
Cdd:PLN03211  158 RETLVFCSLLRLPKSLTKQEKILVAESVISelGLTKCENTIIGNSFIRgISGGERKRVSIAHEMLINPSLLILDEPTSGL 237

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1582666899 519 D-TESEAAVQKALDEAMSGRTVVVIAHRLSTVVRA--DKIVVMQQGRVVEEG 567
Cdd:PLN03211  238 DaTAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQmfDSVLVLSEGRCLFFG 289

PRK10261

glutathione transporter ATP-binding protein; Provisional

334-570

1.28e-12

glutathione transporter ATP-binding protein; Provisional

Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 70.65 E-value: 1.28e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 334 PRQRDLPDARPLTVTQARIEFRNVSfayGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQ 413
Cdd:PRK10261    2 PHSDELDARDVLAVENLNIAFMQEQ---QKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKM 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 414 ----------DIAHITKKSLRQ----QLAYVSQQP-------YLFEGTIRDNIR----YGRPEATdAEVE---EAARLAY 465
Cdd:PRK10261   79 llrrrsrqviELSEQSAAQMRHvrgaDMAMIFQEPmtslnpvFTVGEQIAESIRlhqgASREEAM-VEAKrmlDQVRIPE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 466 AHDFISAQPQgyetpvgengvTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQ---KALDEAMSgRTVVVI 542
Cdd:PRK10261  158 AQTILSRYPH-----------QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILqliKVLQKEMS-MGVIFI 225

                         250       260
                  ....*....|....*....|....*....
gi 1582666899 543 AHRLSTVVR-ADKIVVMQQGRVVEEGNHE 570
Cdd:PRK10261  226 THDMGVVAEiADRVLVMYQGEAVETGSVE 254

PRK15112

peptide ABC transporter ATP-binding protein SapF;

370-568

1.69e-12

peptide ABC transporter ATP-binding protein SapF;

Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.89 E-value: 1.69e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 370 VSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYVSQQP-----------YLFE 438
Cdd:PRK15112   32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPstslnprqrisQILD 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 439 GTIRDNIRYGRPEATDAEVEEAARLAYAHDFISAQPQgyetpvgengvTLSGGQRQRLSIARALVRNAPILLLDEATSAL 518
Cdd:PRK15112  112 FPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPH-----------MLAPGQKQRLGLARALILRPKVIIADEALASL 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 519 DTESEAAV---QKALDEAMSGRTVVVIAHRLSTVVRADKIVVMQQGRVVEEGN 568
Cdd:PRK15112  181 DMSMRSQLinlMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233

PRK10982

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

355-564

1.80e-12

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 69.76 E-value: 1.80e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 355 RNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIA-HITKKSLRQQLAYVSQQ 433
Cdd:PRK10982    2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 434 PYLF-EGTIRDNIRYGRPEATDAEVEEA-----ARLAYAHDFISAQPQgyetpvgENGVTLSGGQRQRLSIARALVRNAP 507
Cdd:PRK10982   82 LNLVlQRSVMDNMWLGRYPTKGMFVDQDkmyrdTKAIFDELDIDIDPR-------AKVATLSVSQMQMIEIAKAFSYNAK 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1582666899 508 ILLLDEATSALdTESEA----AVQKALDEamSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVV 564
Cdd:PRK10982  155 IVIMDEPTSSL-TEKEVnhlfTIIRKLKE--RGCGIVYISHKMEEIFQlCDEITILRDGQWI 213

PRK10762

D-ribose transporter ATP binding protein; Provisional

367-572

2.01e-12

D-ribose transporter ATP binding protein; Provisional

Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 69.65 E-value: 2.01e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 367 LSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSlrQQLAYVS---QQPYLF-EGTIR 442
Cdd:PRK10762   20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKS--SQEAGIGiihQELNLIpQLTIA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 443 DNIRYGRpEATDA--------EVEEA----ARLAYAHDfisaqpqgYETPVGEngvtLSGGQRQRLSIARALVRNAPILL 510
Cdd:PRK10762   98 ENIFLGR-EFVNRfgridwkkMYAEAdkllARLNLRFS--------SDKLVGE----LSIGEQQMVEIAKVLSFESKVII 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582666899 511 LDEATSAL-DTESEA--AVQKALDEamSGRTVVVIAHRLSTVVR-ADKIVVMQQG-----RVVEEGNHETL 572
Cdd:PRK10762  165 MDEPTDALtDTETESlfRVIRELKS--QGRGIVYISHRLKEIFEiCDDVTVFRDGqfiaeREVADLTEDSL 233

ABC_6TM_AarD_CydD

cd18584

Six-transmembrane helical domain (6TM) of the CydD, a component of the ABC cysteine/GSH ...

38-310

4.74e-12

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: 67.05 E-value: 4.74e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  38 AIACLIVVALSTAFTAWIMRAIIDEAFANRRA-DVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYAHL 116
Cdd:cd18584     1 AVLLGLLAALLIIAQAWLLARIIAGVFLEGAGlAALLPLLLLLLAALLLRALLAWAQERLAARAAARVKAELRRRLLARL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 117 MTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAP--PLLYALryVS 194
Cdd:cd18584    81 LALGPALLRRQSSGELATLLTEGVDALDGYFARYLPQLVLAAIVPLLILVAVFPLDWVSALILLVTAPliPLFMIL--IG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 195 KRLRSATREAVH----LNSHVLgamqETIQGIAIVKAFtmeeelerkvnklikGAESR-ANRIARLSER----------- 258
Cdd:cd18584   159 KAAQAASRRQWAalsrLSGHFL----DRLRGLPTLKLF---------------GRARAqAARIARASEDyrrrtmkvlrv 219

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1582666899 259 ---TSPLTESFAGFAVASVLAYAAYRSIYFNVPpgaFFSFVTALLLA---YDPARRLA 310
Cdd:cd18584   220 aflSSAVLEFFATLSIALVAVYIGFRLLGGSLT---LFTALFVLLLApefYLPLRQLG 274

3a01203

TIGR00954

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...

339-547

5.77e-12

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: 68.62 E-value: 5.77e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 339 LPDARPLTVTQARIEFRNVSFAYGNESVL-SGVSFTAEGGATTALVGPSGAGKSTVISLI--------PRFYDPREGEIL 409
Cdd:TIGR00954 439 VPGRGIVEYQDNGIKFENIPLVTPNGDVLiESLSFEVPSGNNLLICGPNGCGKSSLFRILgelwpvygGRLTKPAKGKLF 518

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 410 idgqdiahitkkslrqqlaYVSQQPYLFEGTIRDNIRY-------GRPEATDAEVEEAARLAYAHDFIsaqpqgyETPVG 482
Cdd:TIGR00954 519 -------------------YVPQRPYMTLGTLRDQIIYpdssedmKRRGLSDKDLEQILDNVQLTHIL-------EREGG 572

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 483 ENGV-----TLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAmsGRTVVVIAHRLS 547
Cdd:TIGR00954 573 WSAVqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640

PRK10938

putative molybdenum transport ATP-binding protein ModF; Provisional

338-549

1.37e-11

putative molybdenum transport ATP-binding protein ModF; Provisional

Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 66.96 E-value: 1.37e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 338 DLPDARP-LTVTQARIEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLI----PRFYD-------PRE 405
Cdd:PRK10938  246 DEPSARHaLPANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhPQGYSndltlfgRRR 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 406 GEilidGQDIAHItkkslRQQLAYVSQQ---PYLFEGTIRDNIRYG-------RPEATDAEVEEA----ARLayahdfis 471
Cdd:PRK10938  326 GS----GETIWDI-----KKHIGYVSSSlhlDYRVSTSVRNVILSGffdsigiYQAVSDRQQKLAqqwlDIL-------- 388

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 472 aqpqGYETPVGENGV-TLSGGQrQRLS-IARALVRNAPILLLDEATSALDTESEAAVQKALDEAMS-GRTVVV------- 541
Cdd:PRK10938  389 ----GIDKRTADAPFhSLSWGQ-QRLAlIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISeGETQLLfvshhae 463

                         250
                  ....*....|...
gi 1582666899 542 -----IAHRLSTV 549
Cdd:PRK10938  464 dapacITHRLEFV 476

ABC_ABC_ChvD

TIGR03719

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...

356-544

1.73e-11

Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.88 E-value: 1.73e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 356 NVSFAY-GNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDgQDIahitkkslrqQLAYVSQQP 434
Cdd:TIGR03719   9 RVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-PGI----------KVGYLPQEP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 435 YLFEG-TIRDNI-------------------RYGRPEAT-DAEVEEAARL------AYAHDFISAQPQGYET---PVGEN 484
Cdd:TIGR03719  78 QLDPTkTVRENVeegvaeikdaldrfneisaKYAEPDADfDKLAAEQAELqeiidaADAWDLDSQLEIAMDAlrcPPWDA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582666899 485 GVT-LSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEaMSGrTVVVIAH 544
Cdd:TIGR03719 158 DVTkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQE-YPG-TVVAVTH 216

ABC_6TM_Pgp_ABCB1_D2_like

cd18578

Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...

29-335

2.07e-11

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: 65.17 E-value: 2.07e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  29 RDHLWGYVFAIACLIVVALSTAFTAWIMRAIIDeAFANRRADVVW----IICLSIFIAFVLRGFASYGQAVALSKVGNDI 104
Cdd:cd18578     5 KPEWPLLLLGLIGAIIAGAVFPVFAILFSKLIS-VFSLPDDDELRseanFWALMFLVLAIVAGIAYFLQGYLFGIAGERL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 105 VARYQRRLYAHLMTLSVGFFSEAR--SAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIM 182
Cdd:cd18578    84 TRRLRKLAFRAILRQDIAWFDDPEnsTGALTSRLSTDASDVRGLVGDRLGLILQAIVTLVAGLIIAFVYGWKLALVGLAT 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 183 APPLLYALRYVSKRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSPL 262
Cdd:cd18578   164 VPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEEPLKKGLRRALISGLGFGL 243

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 263 TESFAGFAVASVLAYAAYRSIYFNVPPGAFFSFVTALLLAYDPARRLARLQVQMERAVVNARMIYELLDMEPR 335
Cdd:cd18578   244 SQSLTFFAYALAFWYGGRLVANGEYTFEQFFIVFMALIFGAQSAGQAFSFAPDIAKAKAAAARIFRLLDRKPE 316

ABC_6TM_PrtD_LapB_HlyB_like

cd18782

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...

33-237

2.26e-11

Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 64.92 E-value: 2.26e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  33 WGYVFAIACLIVVALSTAFTAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRL 112
Cdd:cd18782     2 RALIEVLALSFVVQLLGLANPLLFQVIIDKVLVQQDLATLYVIGVVMLVAALLEAVLTALRTYLFTDTANRIDLELGGTI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 113 YAHLMTLSVGFFSEARSAHIAAQVSQnVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRY 192
Cdd:cd18782    82 IDHLLRLPLGFFDKRPVGELSTRISE-LDTIRGFLTGTALTTLLDVLFSVIYIAVLFSYSPLLTLVVLATVPLQLLLTFL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1582666899 193 VSKRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERK 237
Cdd:cd18782   161 FGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWR 205

PLN03140

ABC transporter G family member; Provisional

366-561

5.70e-11

ABC transporter G family member; Provisional

Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 65.64 E-value: 5.70e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  366 VLSGVSFTAEGGATTALVGPSGAGKSTVISLIP--RFYDPREGEILIDG----------------QDIAHITKKSLRQQL 427
Cdd:PLN03140   895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAgrKTGGYIEGDIRISGfpkkqetfarisgyceQNDIHSPQVTVRESL 974

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  428 AYVSQQPYLFEGTIRDNIRYgrpeaTDaEVEEAARLAYAHDFIsaqpqgyetpVGENGVT-LSGGQRQRLSIARALVRNA 506
Cdd:PLN03140   975 IYSAFLRLPKEVSKEEKMMF-----VD-EVMELVELDNLKDAI----------VGLPGVTgLSTEQRKRLTIAVELVANP 1038

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1582666899  507 PILLLDEATSALDTESEAAVQKALDEAM-SGRTVVVIAHRLST-VVRA-DKIVVMQQG 561
Cdd:PLN03140  1039 SIIFMDEPTSGLDARAAAIVMRTVRNTVdTGRTVVCTIHQPSIdIFEAfDELLLMKRG 1096

MK0520

COG2401

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...

366-569

6.81e-11

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

Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.28 E-value: 6.81e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 366 VLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDgqdiahitkkslrqqlayVSQQPYLFEGTIRDNI 445
Cdd:COG2401    45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD------------------VPDNQFGREASLIDAI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 446 ryGRPEATDAEVEEAARLAYAhdfisaQPQGYETPVGEngvtLSGGQRQRLSIARALVRNAPILLLDEATSALDTES--- 522
Cdd:COG2401   107 --GRKGDFKDAVELLNAVGLS------DAVLWLRRFKE----LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTakr 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1582666899 523 -EAAVQKALDEAmsGRTVVVIAHRlSTVVRA---DKIVVMQQGRVVEEGNH 569
Cdd:COG2401   175 vARNLQKLARRA--GITLVVATHH-YDVIDDlqpDLLIFVGYGGVPEEKRR 222

ABC_6TM_AarD_CydDC_like

cd18561

Six-transmembrane helical domain (6-TMD) of the ABC cysteine/GSH transporter CydDC, and ...

42-312

7.86e-11

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: 63.07 E-value: 7.86e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  42 LIVVALSTAfTAWIMRAIIDEAFANR-RADVVWIIcLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYAHLMTLS 120
Cdd:cd18561     6 LLITALYIA-QAWLLARALARIFAGGpWEDIMPPL-AGIAGVIVLRAALLWLRERVAHRAAQRVKQHLRRRLFAKLLKLG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 121 VGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYVSKRLRSA 200
Cdd:cd18561    84 PGYLEGERTGELQTTVVDGVEALEAYYGRYLPQLLVALLGPLLILIYLFFLDPLVALILLVFALLIPLSPALWDRLAKDT 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 201 TREAVHLNSHVLGAMQETIQGIAIVKAFTME----EELERKVNKLIKgaesRANRIARLSERTSPLTESFAGFAVASVLA 276
Cdd:cd18561   164 GRRHWAAYGRLSAQFLDSLQGMTTLKAFGASkrrgNELAARAEDLRQ----ATMKVLAVSLLSSGIMGLATALGTALALG 239

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1582666899 277 YAAYRsiYFNVPPGAfFSFVTALLLAYDPARRLARL 312
Cdd:cd18561   240 VGALR--VLGGQLTL-SSLLLILFLSREFFRPLRDL 272

Rli1

COG1245

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...

338-544

7.91e-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: 64.81 E-value: 7.91e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 338 DLPDARPLTVTQARIEFRNVSFAYGnesvlsGVSFTAEGGA-----TTALVGPSGAGKSTVISLIPRFYDPREGEIlidg 412
Cdd:COG1245   328 EVHAPRREKEEETLVEYPDLTKSYG------GFSLEVEGGEiregeVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---- 397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 413 qdiahitKKSLRqqLAYVSQqpYL---FEGTIRDNIRYGRPEATDAEVeeaarlaYAHDFIsaQPQG----YETPVGEng 485
Cdd:COG1245   398 -------DEDLK--ISYKPQ--YIspdYDGTVEEFLRSANTDDFGSSY-------YKTEII--KPLGleklLDKNVKD-- 455

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1582666899 486 vtLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAM--SGRTVVVIAH 544
Cdd:COG1245   456 --LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAenRGKTAMVVDH 514

3a01205

TIGR00956

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

366-567

8.29e-11

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

Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.13 E-value: 8.29e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  366 VLSGVSFTAEGGATTALVGPSGAGKSTVISLIP----RFYDPREGEILIDGQDIAHItKKSLRQQLAYVSQQ----PYLf 437
Cdd:TIGR00956   76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEI-KKHYRGDVVYNAETdvhfPHL- 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  438 egTIRDNIRYG--------RPEATDAEvEEAARLAYAHDFISAQPQGYETPVGENGVT-LSGGQRQRLSIARALVRNAPI 508
Cdd:TIGR00956  154 --TVGETLDFAarcktpqnRPDGVSRE-EYAKHIADVYMATYGLSHTRNTKVGNDFVRgVSGGERKRVSIAEASLGGAKI 230

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582666899  509 LLLDEATSALDTESEAAVQKALdeamsgRTVVVIAHRLSTVV----------RADKIVVMQQGRVVEEG 567
Cdd:TIGR00956  231 QCWDNATRGLDSATALEFIRAL------KTSANILDTTPLVAiyqcsqdayeLFDKVIVLYEGYQIYFG 293

COG4586

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

367-574

1.02e-10

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

Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 63.18 E-value: 1.02e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 367 LSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDG-----QDIAHITKKSL----RQQLayvsqqpyLF 437
Cdd:COG4586    38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpfkRRKEFARRIGVvfgqRSQL--------WW 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 438 EGTIRDNIR-----YGRPEAT-DAEVEEAARLAYAHDFISaqpqgyeTPVGEngvtLSGGQRQRLSIARALVRNAPILLL 511
Cdd:COG4586   110 DLPAIDSFRllkaiYRIPDAEyKKRLDELVELLDLGELLD-------TPVRQ----LSLGQRMRCELAAALLHRPKILFL 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582666899 512 DEATSALDTESEAAVQKALDE--AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHETLAK 574
Cdd:COG4586   179 DEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGRIIYDGSLEELKE 244

ABC_6TM_T1SS_like

cd18779

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ATP-binding ...

53-318

1.07e-10

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: 62.95 E-value: 1.07e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  53 AWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYAHLMTLSVGFFSEARSAHI 132
Cdd:cd18779    22 PLLTGVLVDRVIPRGDRDLLGVLGLGLAALVLTQLLAGLLRSHLLLRLRTRLDTQLTLGFLEHLLRLPYRFFQQRSTGDL 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 133 AAQVSQNVSgIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYVSKRLRSATREAVHLNSHVL 212
Cdd:cd18779   102 LMRLSSNAT-IRELLTSQTLSALLDGTLVLGYLALLFAQSPLLGLVVLGLAALQVALLLATRRRVRELMARELAAQAEAQ 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 213 GAMQETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSPLTESFAGFAVASVLAYAAYR----------S 282
Cdd:cd18779   181 SYLVEALSGIETLKASGAEDRALDRWSNLFVDQLNASLRRGRLDALVDALLATLRLAAPLVLLWVGAWQvldgqlslgtM 260

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1582666899 283 IYFNVPPGAFFSFVTALLLAydpARRLARLQVQMER 318
Cdd:cd18779   261 LALNALAGAFLAPLASLVGT---AQQLQLLGSHLER 293

PRK10584

putative ABC transporter ATP-binding protein YbbA; Provisional

365-566

1.53e-10

putative ABC transporter ATP-binding protein YbbA; Provisional

Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 61.33 E-value: 1.53e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 365 SVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKK---SLR-QQLAYVSQQ------- 433
Cdd:PRK10584   24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraKLRaKHVGFVFQSfmliptl 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 434 --------PYLFEGtirDNIRYGRPEAtdAEVEEAARLAYAHDFISAQpqgyetpvgengvtLSGGQRQRLSIARALVRN 505
Cdd:PRK10584  104 nalenvelPALLRG---ESSRQSRNGA--KALLEQLGLGKRLDHLPAQ--------------LSGGEQQRVALARAFNGR 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582666899 506 APILLLDEATSALDTESEaavQKALDEAMS-----GRTVVVIAHRLSTVVRADKIVVMQQGRVVEE 566
Cdd:PRK10584  165 PDVLFADEPTGNLDRQTG---DKIADLLFSlnrehGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227

Rli1

COG1245

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...

377-558

1.57e-10

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: 64.04 E-value: 1.57e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 377 GATTALVGPSGAGKSTVIS-----LIPRFYDPREG----EIL-----IDGQD-IAHITKKSLR--QQLAYVSQQPYLFEG 439
Cdd:COG1245    99 GKVTGILGPNGIGKSTALKilsgeLKPNLGDYDEEpswdEVLkrfrgTELQDyFKKLANGEIKvaHKPQYVDLIPKVFKG 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 440 TIRDNIrygrpEATDaeveEAARLAYAHDFISAQPQgYETPVGEngvtLSGGQRQRLSIARALVRNAPILLLDEATSALD 519
Cdd:COG1245   179 TVRELL-----EKVD----ERGKLDELAEKLGLENI-LDRDISE----LSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1582666899 520 TESEAAVQKALDE-AMSGRTVVVIAHRLSTV-VRADKIVVM 558
Cdd:COG1245   245 IYQRLNVARLIRElAEEGKYVLVVEHDLAILdYLADYVHIL 285

ABC_RNaseL_inhibitor_domain1

cd03236

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...

361-547

1.74e-10

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: 61.61 E-value: 1.74e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 361 YG-NESVLSGVSFTAEGGaTTALVGPSGAGKSTVI-----SLIP---RFYDPREGEILID---GQDIAHITKKSLRQQLA 428
Cdd:cd03236    10 YGpNSFKLHRLPVPREGQ-VLGLVGPNGIGKSTALkilagKLKPnlgKFDDPPDWDEILDefrGSELQNYFTKLLEGDVK 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 429 ------YVSQQPYLFEGTIRDNIrygrpEATDaeveEAARLAYAHDFISAqpqgyeTPVGENGVT-LSGGQRQRLSIARA 501
Cdd:cd03236    89 vivkpqYVDLIPKAVKGKVGELL-----KKKD----ERGKLDELVDQLEL------RHVLDRNIDqLSGGELQRVAIAAA 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1582666899 502 LVRNAPILLLDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLS 547
Cdd:cd03236   154 LARDADFYFFDEPSSYLDIKQRLNAARLIRElAEDDNYVLVVEHDLA 200

PRK13409

ribosome biogenesis/translation initiation ATPase RLI;

383-544

2.44e-10

ribosome biogenesis/translation initiation ATPase RLI;

Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.29 E-value: 2.44e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 383 VGPSGAGKSTVISLIPRFYDPREGEILIDgqdiahitkksLRqqLAYVSQqpYL---FEGTIRDNIRygrpeatdaevEE 459
Cdd:PRK13409  371 VGPNGIGKTTFAKLLAGVLKPDEGEVDPE-----------LK--ISYKPQ--YIkpdYDGTVEDLLR-----------SI 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 460 AARLA---YAHDFIsaQPQG----YETPVGEngvtLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDE 532
Cdd:PRK13409  425 TDDLGssyYKSEII--KPLQlerlLDKNVKD----LSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRR 498

                         170
                  ....*....|....
gi 1582666899 533 AM--SGRTVVVIAH 544
Cdd:PRK13409  499 IAeeREATALVVDH 512

AAA

smart00382

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...

377-562

3.13e-10

Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 58.92 E-value: 3.13e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  377 GATTALVGPSGAGKSTVISLIPRFYDPREGE-ILIDGQDIAHITKKSLRQqlayvsqqpylfegtirdnirygrpeatda 455
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGvIYIDGEDILEEVLDQLLL------------------------------ 51

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  456 eveeaarlayahdfisaqpqgyeTPVGENGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAM- 534
Cdd:smart00382  52 -----------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLl 108

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1582666899  535 ------SGRTVVVIAHRLSTVV------RADKIVVMQQGR 562
Cdd:smart00382 109 lllkseKNLTVILTTNDEKDLGpallrrRFDRRIVLLLIL 148

PRK13409

ribosome biogenesis/translation initiation ATPase RLI;

377-558

5.42e-10

ribosome biogenesis/translation initiation ATPase RLI;

Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.13 E-value: 5.42e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 377 GATTALVGPSGAGKSTVIS-----LIPRFYDPRE------------GEILidgQD-IAHITKKSLR--QQLAYVSQQPYL 436
Cdd:PRK13409   99 GKVTGILGPNGIGKTTAVKilsgeLIPNLGDYEEepswdevlkrfrGTEL---QNyFKKLYNGEIKvvHKPQYVDLIPKV 175

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 437 FEGTIRDNIrygrpEATDA-----EVEEAARLayahdfisaqpqgyeTPVGENGV-TLSGGQRQRLSIARALVRNAPILL 510
Cdd:PRK13409  176 FKGKVRELL-----KKVDErgkldEVVERLGL---------------ENILDRDIsELSGGELQRVAIAAALLRDADFYF 235

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1582666899 511 LDEATSALDTESEAAVQKALDEAMSGRTVVVIAHRLSTV-VRADKIVVM 558
Cdd:PRK13409  236 FDEPTSYLDIRQRLNVARLIRELAEGKYVLVVEHDLAVLdYLADNVHIA 284

PRK15439

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

367-566

5.43e-10

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.99 E-value: 5.43e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 367 LSG-----VSFTAEGGATTALVGPSGAGKS----TVISLIPrfydPREGEILIDGQDIAHI-TKKSLRQQLAYVS---QQ 433
Cdd:PRK15439  274 LTGegfrnISLEVRAGEILGLAGVVGAGRTelaeTLYGLRP----ARGGRIMLNGKEINALsTAQRLARGLVYLPedrQS 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 434 PYLF-EGTIRDNI---RYGRPEATDAEVEEAARLAYAHDFISAQPQGYETPVGengvTLSGGQRQRLSIARALVRNAPIL 509
Cdd:PRK15439  350 SGLYlDAPLAWNVcalTHNRRGFWIKPARENAVLERYRRALNIKFNHAEQAAR----TLSGGNQQKVLIAKCLEASPQLL 425

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1582666899 510 LLDEATSALDTESEAAVQKAL-DEAMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEE 566
Cdd:PRK15439  426 IVDEPTRGVDVSARNDIYQLIrSIAAQNVAVLFISSDLEEIEQmADRVLVMHQGEISGA 484

xylG

TIGR02633

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...

370-563

8.95e-10

Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 61.38 E-value: 8.95e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 370 VSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPR-EGEILIDGQDIAHIT-KKSLRQQLAYVSQQ-------PYLFEG- 439
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNpAQAIRAGIAMVPEDrkrhgivPILGVGk 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 440 --TIRDNIRYGRPEATDAEVEEAARLAyAHDFISAQPQGYETPVGengvTLSGGQRQRLSIARALVRNAPILLLDEATSA 517
Cdd:TIGR02633 359 niTLSVLKSFCFKMRIDAAAELQIIGS-AIQRLKVKTASPFLPIG----RLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1582666899 518 LDTESEAAVQKALDE-AMSGRTVVVIAHRLSTVVR-ADKIVVMQQGRV 563
Cdd:TIGR02633 434 VDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKL 481

PRK11819

putative ABC transporter ATP-binding protein; Reviewed

355-544

1.03e-09

putative ABC transporter ATP-binding protein; Reviewed

Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.29 E-value: 1.03e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 355 RNVSFAYG-NESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGE-ILIDGQDIAhitkkslrqqlaYVSQ 432
Cdd:PRK11819   10 NRVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEaRPAPGIKVG------------YLPQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 433 QPYLFEG-TIRDNI-------------------RYGRPEA-TDAEVEEAARL------AYAHDFISAQPQGYE---TPVG 482
Cdd:PRK11819   78 EPQLDPEkTVRENVeegvaevkaaldrfneiyaAYAEPDAdFDALAAEQGELqeiidaADAWDLDSQLEIAMDalrCPPW 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 483 ENGVT-LSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALdEAMSGrTVVVIAH 544
Cdd:PRK11819  158 DAKVTkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFL-HDYPG-TVVAVTH 218

hmuV

PRK13547

heme ABC transporter ATP-binding protein;

366-567

1.09e-09

heme ABC transporter ATP-binding protein;

Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.46 E-value: 1.09e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 366 VLSGVSFTAEGGATTALVGPSGAGKSTVISL----IPRFYDPR----EGEILIDGQDIAHITKKSL---RQQLAYVSQQP 434
Cdd:PRK13547   16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKAlagdLTGGGAPRgarvTGDVTLNGEPLAAIDAPRLarlRAVLPQAAQPA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 435 YLFegTIRDNIRYGR-PEAT--------DAEVEEAArLAYAhdfisaqpqGYETPVGENGVTLSGGQRQRLSIARALVRN 505
Cdd:PRK13547   96 FAF--SAREIVLLGRyPHARragalthrDGEIAWQA-LALA---------GATALVGRDVTTLSGGELARVQFARVLAQL 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582666899 506 AP---------ILLLDEATSALDTESE----AAVQKALDEAMSGrtVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:PRK13547  164 WPphdaaqpprYLLLDEPTAALDLAHQhrllDTVRRLARDWNLG--VLAIVHDPNLAARhADRIAMLADGAIVAHG 237

ABC_6TM_AtABCB27_like

cd18780

Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...

77-296

1.55e-09

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: 59.57 E-value: 1.55e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  77 LSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYAHLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVR 156
Cdd:cd18780    46 LILLGVVLIGSIATFLRSWLFTLAGERVVARLRKRLFSAIIAQEIAFFDVTRTGELLNRLSSDTQVLQNAVTVNLSMLLR 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 157 DLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYVSKRLRS---ATREAVHLNSHVlgaMQETIQGIAIVKAFTMEEE 233
Cdd:cd18780   126 YLVQIIGGLVFMFTTSWKLTLVMLSVVPPLSIGAVIYGKYVRKlskKFQDALAAASTV---AEESISNIRTVRSFAKETK 202

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 234 LERKVNKLIKGAESRANRIARLSERTSPLTESFAGFAVASVLAYAAYRSIYFNVPPGAFFSFV 296
Cdd:cd18780   203 EVSRYSEKINESYLLGKKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTGLLTSFL 265

sufC

PRK09580

cysteine desulfurase ATPase component; Reviewed

352-574

1.95e-09

cysteine desulfurase ATPase component; Reviewed

Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 58.65 E-value: 1.95e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIP--RFYDPREGEILIDGQDIAHITKKSLRQQ--- 426
Cdd:PRK09580    2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDRAGEgif 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 427 LAY--------VSQQpyLFEGTIRDNIRYGRpeatdaEVEEAARLAYAhDFISAQPQGYETP----VGENGVTLSGGQRQ 494
Cdd:PRK09580   82 MAFqypveipgVSNQ--FFLQTALNAVRSYR------GQEPLDRFDFQ-DLMEEKIALLKMPedllTRSVNVGFSGGEKK 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 495 RLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSG-RTVVVIAH--RLSTVVRADKIVVMQQGRVVEEGNHeT 571
Cdd:PRK09580  153 RNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHyqRILDYIKPDYVHVLYQGRIVKSGDF-T 231


                  ...
gi 1582666899 572 LAK 574
Cdd:PRK09580  232 LVK 234

PRK13543

heme ABC exporter ATP-binding protein CcmA;

341-521

2.58e-09

heme ABC exporter ATP-binding protein CcmA;

Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.55 E-value: 2.58e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 341 DARPLTVTQARIEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQdiaHITK 420
Cdd:PRK13543    1 MIEPLHTAPPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK---TATR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 421 KSLRQQLAYVSQQPYLFEG-TIRDNIRY------GRPEATDAEVEEAARLAYAHDFISAQpqgyetpvgengvtLSGGQR 493
Cdd:PRK13543   78 GDRSRFMAYLGHLPGLKADlSTLENLHFlcglhgRRAKQMPGSALAIVGLAGYEDTLVRQ--------------LSAGQK 143

                         170       180
                  ....*....|....*....|....*...
gi 1582666899 494 QRLSIARALVRNAPILLLDEATSALDTE 521
Cdd:PRK13543  144 KRLALARLWLSPAPLWLLDEPYANLDLE 171

PRK13549

xylose transporter ATP-binding subunit; Provisional

370-563

2.74e-09

xylose transporter ATP-binding subunit; Provisional

Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.56 E-value: 2.74e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 370 VSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPR-EGEILIDGQDIA-HITKKSLRQQLAYVSQQ-------PYLfegT 440
Cdd:PRK13549  281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDGKPVKiRNPQQAIAQGIAMVPEDrkrdgivPVM---G 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 441 IRDNI------RYGRPEATDaeveEAARLAYAHDFI------SAQPqgyETPVGengvTLSGGQRQRLSIARALVRNAPI 508
Cdd:PRK13549  358 VGKNItlaaldRFTGGSRID----DAAELKTILESIqrlkvkTASP---ELAIA----RLSGGNQQKAVLAKCLLLNPKI 426

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1582666899 509 LLLDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLSTVV-RADKIVVMQQGRV 563
Cdd:PRK13549  427 LILDEPTRGIDVGAKYEIYKLINQlVQQGVAIIVISSELPEVLgLSDRVLVMHEGKL 483

ABC_6TM_CyaB_HlyB_like

cd18588

Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ...

31-280

3.33e-09

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: 58.28 E-value: 3.33e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  31 HLWGYVFAIACLI-VVALSTAFtawIMRAIIDEAFANRRAD--VVWIICLSIFIAF--VLRGFASYgqavALSKVGNDIV 105
Cdd:cd18588     2 KLLGEVLLASLFLqLFALVTPL---FFQVIIDKVLVHRSLStlDVLAIGLLVVALFeaVLSGLRTY----LFSHTTNRID 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 106 ARYQRRLYAHLMTLSVGFFSEARSAHIAAQVsQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPp 185
Cdd:cd18588    75 AELGARLFRHLLRLPLSYFESRQVGDTVARV-RELESIRQFLTGSALTLVLDLVFSVVFLAVMFYYSPTLTLIVLASLP- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 186 lLYALRY--VSKRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSPLT 263
Cdd:cd18588   153 -LYALLSllVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELLARYVKASFKTANLSNLASQIV 231

                         250
                  ....*....|....*..
gi 1582666899 264 ESFAGFAVASVLAYAAY 280
Cdd:cd18588   232 QLIQKLTTLAILWFGAY 248

araG

PRK11288

L-arabinose ABC transporter ATP-binding protein AraG;

337-570

4.85e-09

L-arabinose ABC transporter ATP-binding protein AraG;

Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.77 E-value: 4.85e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 337 RDLPDA---RPLTVTQARIEFRNVSfaygNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQ 413
Cdd:PRK11288  240 REIGDIygyRPRPLGEVRLRLDGLK----GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGK 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 414 DIA-HITKKSLRQQLAYVSQQPYlFEG-----TIRDNI---------RYG-----RPEATDAEvEEAARLAYahdfisaq 473
Cdd:PRK11288  316 PIDiRSPRDAIRAGIMLCPEDRK-AEGiipvhSVADNInisarrhhlRAGclinnRWEAENAD-RFIRSLNI-------- 385

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 474 pqgyETPVGENG-VTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLSTVVR 551
Cdd:PRK11288  386 ----KTPSREQLiMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYElAAQGVAVLFVSSDLPEVLG 461

                         250       260
                  ....*....|....*....|
gi 1582666899 552 -ADKIVVMQQGRVVEEGNHE 570
Cdd:PRK11288  462 vADRIVVMREGRIAGELARE 481

dppD

PRK11022

dipeptide transporter ATP-binding subunit; Provisional

356-567

6.92e-09

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.83 E-value: 6.92e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 356 NVSFAYGNESV----LSGVSFTAEGGATTALVGPSGAGKS----TVISLIPRFYDPREGEILIDGQDIAHITKKSLRQ-- 425
Cdd:PRK11022    8 KLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNlv 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 426 --QLAYVSQQP-------YLFEGTIRDNIRygrpeaTDAEVEEAARLAYAHDFISAQpqGYETPVGENGV---TLSGGQR 493
Cdd:PRK11022   88 gaEVAMIFQDPmtslnpcYTVGFQIMEAIK------VHQGGNKKTRRQRAIDLLNQV--GIPDPASRLDVyphQLSGGMS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 494 QRLSIARALVRNAPILLLDEATSALDTESEAAVQKAL-----DEAMSgrtVVVIAHRLSTVVR-ADKIVVMQQGRVVEEG 567
Cdd:PRK11022  160 QRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLlelqqKENMA---LVLITHDLALVAEaAHKIIVMYAGQVVETG 236

uvra

TIGR00630

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...

454-573

7.03e-09

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]

Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 58.87 E-value: 7.03e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 454 DAEVEEAarlayaHDFISAQPQ-------------GYeTPVGENGVTLSGGQRQRLSIARALVRNA---PILLLDEATSA 517
Cdd:TIGR00630 790 DMTVEEA------YEFFEAVPSisrklqtlcdvglGY-IRLGQPATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTTG 862

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1582666899 518 LDTESeaaVQKALDEAMS----GRTVVVIAHRLSTVVRADKIVVM------QQGRVVEEGNHETLA 573
Cdd:TIGR00630 863 LHFDD---IKKLLEVLQRlvdkGNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEVA 925

ABC_UvrA_II

cd03271

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...

377-556

8.38e-09

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.

Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 56.85 E-value: 8.38e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 377 GATTALVGPSGAGKSTVI------SLIPRFYDPREGEILIDGQD-IAHITKkslrqqLAYVSQQP-----------Y--L 436
Cdd:cd03271    21 GVLTCVTGVSGSGKSSLIndtlypALARRLHLKKEQPGNHDRIEgLEHIDK------VIVIDQSPigrtprsnpatYtgV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 437 FEgTIRD----------------NIRY-GR--PEATDAEVEEAarlayaHDFISAQPQ-------------GYeTPVGEN 484
Cdd:cd03271    95 FD-EIRElfcevckgkrynretlEVRYkGKsiADVLDMTVEEA------LEFFENIPKiarklqtlcdvglGY-IKLGQP 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582666899 485 GVTLSGGQRQRLSIARALVRNAP---ILLLDEATSALDTESeaaVQKALDEAMS----GRTVVVIAHRLSTVVRADKIV 556
Cdd:cd03271   167 ATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHD---VKKLLEVLQRlvdkGNTVVVIEHNLDVIKCADWII 242

PRK15064

ABC transporter ATP-binding protein; Provisional

352-531

2.52e-08

ABC transporter ATP-binding protein; Provisional

Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.82 E-value: 2.52e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEIlidgqdiahitKKSLRQQLAYVS 431
Cdd:PRK15064  320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV-----------KWSENANIGYYA 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYL-FEG--TIRDNIRYGRPEATDAEVEEAA--RLAYAHDFISAQPQgyetpvgengvTLSGGQRQRLSIARALVRNA 506
Cdd:PRK15064  389 QDHAYdFENdlTLFDWMSQWRQEGDDEQAVRGTlgRLLFSQDDIKKSVK-----------VLSGGEKGRMLFGKLMMQKP 457

                         170       180
                  ....*....|....*....|....*
gi 1582666899 507 PILLLDEATSALDTESEAAVQKALD 531
Cdd:PRK15064  458 NVLVMDEPTNHMDMESIESLNMALE 482

ABC_6TM_ABCB8_like

cd18574

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ...

77-247

3.28e-08

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: 55.24 E-value: 3.28e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  77 LSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYAHLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVR 156
Cdd:cd18574    46 LKLLGLYLLQSLLTFAYISLLSVVGERVAARLRNDLFSSLLRQDIAFFDTHRTGELVNRLTADVQEFKSSFKQCVSQGLR 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 157 DLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYVSKRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELER 236
Cdd:cd18574   126 SVTQTVGCVVSLYLISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELE 205

                         170
                  ....*....|.
gi 1582666899 237 KVNKLIKGAES 247
Cdd:cd18574   206 LYEEEVEKAAK 216

ABC_6TM_NHLM_bacteriocin

cd18569

Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; ...

38-283

3.68e-08

Six-transmembrane helical domain (6-TMD) of NHLP family bacteriocin export ABC transporters; This group includes the six-transmembrane helical domain (6-TMD) of the ABC subunit of NHLM (Nitrile Hydratase Leader Microcin) bacteriocin system, which contains ABC transporter (permease/ATP-binding fused protein) with a peptidase domain. ABC-transporter proteins in this group are predicted to be a subunit of a bacteriocin processing and export system, and they 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: 350013 [Multi-domain] Cd Length: 294 Bit Score: 55.17 E-value: 3.68e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  38 AIACLIVVALSTAFTAWIM----RAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLY 113
Cdd:cd18569     3 ALLFVVLAGLLLVIPGLVIpvfsRIFIDDILVGGLPDWLRPLLLGMALTALLQGLLTWLQQYYLLRLETKLALSSSSRFF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 114 AHLMTLSVGFFSEARSAHIAAQVSQNVSgIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVFIMAPPLLYALRYV 193
Cdd:cd18569    83 WHVLRLPVEFFSQRYAGDIASRVQSNDR-VANLLSGQLATTVLNLVMAVFYALLMLQYDVPLTLIGIAIALLNLLVLRLV 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 194 SKRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKvnklIKGAESRAN----RIARLSERTSPLTESFAGF 269
Cdd:cd18569   162 SRKRVDLNRRLLQDSGKLTGTTMSGLQMIETLKASGAESDFFSR----WAGYQAKVLnaqqELGRTNQLLGALPTLLSAL 237

                         250
                  ....*....|....
gi 1582666899 270 AVASVLAYAAYRSI 283
Cdd:cd18569   238 TNAAILGLGGLLVM 251

ABC_6TM_ABCC_D2

cd18580

Six-transmembrane helical domain 2 (TMD2) of the ABC transporters, subfamily C; This group ...

36-242

4.32e-08

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: 54.82 E-value: 4.32e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  36 VFAIACLIVVALSTAFTAWIMRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYAH 115
Cdd:cd18580     2 LLLLLLLLLLAFLSQFSNIWLDWWSSDWSSSPNSSSGYYLGVYAALLVLASVLLVLLRWLLFVLAGLRASRRLHDKLLRS 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 116 LMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLslavFIMAPPLLYALRYVSK 195
Cdd:cd18580    82 VLRAPMSFFDTTPSGRILNRFSKDIGLIDEELPLALLDFLQSLFSVLGSLIVIAIVSPYF----LIVLPPLLVVYYLLQR 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1582666899 196 RLRSATREAVHL----NSHVLGAMQETIQGIAIVKAFTMEEELERKVNKLI 242
Cdd:cd18580   158 YYLRTSRQLRRLesesRSPLYSHFSETLSGLSTIRAFGWQERFIEENLRLL 208

ABC_6TM_ATM1_ABCB7_HMT1_ABCB6

cd18560

Six-transmembrane helical domain (6-TMD) of the Atm1/ABCB7/HMT1/ABCB6 subfamily; This group ...

40-305

1.59e-07

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: 53.38 E-value: 1.59e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  40 ACLIVVALstaFTAWIMRAIIDEAFANRRADVVWIICLSIFiaFVLRGFASYGQAVALSKVGNDIVARYQRRLYAHLMTL 119
Cdd:cd18560    10 ACNVLAPL---FLGRAVNALTLAKVKDLESAVTLILLYALL--RFSSKLLKELRSLLYRRVQQNAYRELSLKTFAHLHSL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 120 SVGFFSEARSAHIAAQVSQNVSGIRDVLN---LTITSTVRDLLTFVSLLAVMIlqDPLLSLAVFIMAPPLLYALRYVSKR 196
Cdd:cd18560    85 SLDWHLSKKTGEVVRIMDRGTESANTLLSylvFYLVPTLLELIVVSVVFAFHF--GAWLALIVFLSVLLYGVFTIKVTEW 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 197 LRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKVNKLIKgAESRANRIARLSerTSPLT---ESFAGFAVAS 273
Cdd:cd18560   163 RTKFRRAANKKDNEAHDIAVDSLLNFETVKYFTNEKYEVDRYGEAVK-EYQKSSVKVQAS--LSLLNvgqQLIIQLGLTL 239

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1582666899 274 VLAYAAYRSIYFNVPPGAFFSFVTALLLAYDP 305
Cdd:cd18560   240 GLLLAGYRVVDGGLSVGDFVAVNTYIFQLFQP 271

ABC_6TM_HMT1

cd18583

Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ...

41-323

1.68e-07

Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents the HMT1 subfamily of ATP Binding Cassette (ABC) transporters that are involved in transition metal homeostasis and detoxification processes. Heavy Metal Tolerance Factor-1 (HMT1) proteins are required for cadmium resistance in Caenorhabditis elegans and Drosophila melanogaster. HMT1 is closely related to 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.

Pssm-ID: 350027 [Multi-domain] Cd Length: 290 Bit Score: 52.92 E-value: 1.68e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  41 CLIVVALSTAFTAWIMRA--IIDEAFANRRADVVWIiclSIFIAFVLRGFASYG-----QAVALSKVGNDIVARYQRRLY 113
Cdd:cd18583     1 CFLCLLAERVLNVLVPRQlgIIVDSLSGGSGKSPWK---EIGLYVLLRFLQSGGglgllRSWLWIPVEQYSYRALSTAAF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 114 AHLMTLSVGFFSEARSAHIAAQVSQnVSGIRDVLNLTITS---TVRDLltFVSLLAVMILQDPLLSLAVFIMAPPLLYAL 190
Cdd:cd18583    78 NHVMNLSMDFHDSKKSGEVLKAIEQ-GSSINDLLEQILFQivpMIIDL--VIAIVYLYYLFDPYMGLIVAVVMVLYVWST 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 191 RYVSKRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEE-ELERKVNKLIkgAESRANRIARLSERTSPLTESF--- 266
Cdd:cd18583   155 IKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPyEKERYREAVK--NYQKAERKYLFSLNLLNAVQSLilt 232

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1582666899 267 AGFAVASVLayAAYRSIYFNVPPGAFFSFVTALLLAYDPARRLARLQVQMERAVVNA 323
Cdd:cd18583   233 LGLLAGCFL--AAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDLIDA 287

ABC_Class2

cd03227

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...

380-558

2.12e-07

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

Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 50.82 E-value: 2.12e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 380 TALVGPSGAGKSTVISLIprfydpregeILIDGQDIAHITKKSLRQQLAYVSQQpylfegtirdnirygrpEATdaevee 459
Cdd:cd03227    24 TIITGPNGSGKSTILDAI----------GLALGGAQSATRRRSGVKAGCIVAAV-----------------SAE------ 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 460 aarlayahdFISAQPQgyetpvgengvtLSGGQRQRLSIARAL----VRNAPILLLDEATSALDTESEAAVQKALDE-AM 534
Cdd:cd03227    71 ---------LIFTRLQ------------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEhLV 129

                         170       180
                  ....*....|....*....|....
gi 1582666899 535 SGRTVVVIAHRLSTVVRADKIVVM 558
Cdd:cd03227   130 KGAQVIVITHLPELAELADKLIHI 153

PRK13546

teichoic acids export ABC transporter ATP-binding subunit TagH;

367-572

2.91e-07

teichoic acids export ABC transporter ATP-binding subunit TagH;

Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.13 E-value: 2.91e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 367 LSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKSLRQQLAYVSQQPY--LFEGTIRDN 444
Cdd:PRK13546   40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTGIENIEFkmLCMGFKRKE 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 445 IRYGRPeatdaEVEEAARLAyahDFISAQPQGYetpvgengvtlSGGQRQRLSIARALVRNAPILLLDEATSALDtesEA 524
Cdd:PRK13546  120 IKAMTP-----KIIEFSELG---EFIYQPVKKY-----------SSGMRAKLGFSINITVNPDILVIDEALSVGD---QT 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 525 AVQKALDEAM----SGRTVVVIAHRLSTVVR-ADKIVVMQQGRVVEEGNHETL 572
Cdd:PRK13546  178 FAQKCLDKIYefkeQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDV 230

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

352-519

2.95e-07

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.59 E-value: 2.95e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAhitKKSLRQQL---- 427
Cdd:NF033858    2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA---DARHRRAVcpri 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 428 AYVSQ------QPYLfegTIRDNIRY-GRPEATDAEVEEA--ARLAYA---HDFIsaqpqgyETPVGEngvtLSGGQRQR 495
Cdd:NF033858   79 AYMPQglgknlYPTL---SVFENLDFfGRLFGQDAAERRRriDELLRAtglAPFA-------DRPAGK----LSGGMKQK 144

                         170       180
                  ....*....|....*....|....
gi 1582666899 496 LSIARALVRNAPILLLDEATSALD 519
Cdd:NF033858  145 LGLCCALIHDPDLLILDEPTTGVD 168

PRK09700

D-allose ABC transporter ATP-binding protein AlsA;

353-566

3.15e-07

D-allose ABC transporter ATP-binding protein AlsA;

Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 53.25 E-value: 3.15e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 353 EFRNVSfAYGNESVlSGVSFTAEGGATTALVGPSGAGKSTVISLIprF-YDPR-EGEILIDGQDIAHITK-KSLRQQLAY 429
Cdd:PRK09700  267 EVRNVT-SRDRKKV-RDISFSVCRGEILGFAGLVGSGRTELMNCL--FgVDKRaGGEIRLNGKDISPRSPlDAVKKGMAY 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 430 VSQQP----YLFEGTIRDNI---------RYGRPEATDAEVEEAARLAYAHDFISAQPQGYETPVGEngvtLSGGQRQRL 496
Cdd:PRK09700  343 ITESRrdngFFPNFSIAQNMaisrslkdgGYKGAMGLFHEVDEQRTAENQRELLALKCHSVNQNITE----LSGGNQQKV 418

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1582666899 497 SIARALVRNAPILLLDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLSTVVRA-DKIVVMQQGRVVEE 566
Cdd:PRK09700  419 LISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLTQI 490

PLN03073

ABC transporter F family; Provisional

340-563

4.42e-07

ABC transporter F family; Provisional

Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.94 E-value: 4.42e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 340 PDARPltvTQARIEFRNVSFAY-GNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILidgqdiahi 418
Cdd:PLN03073  500 PDDRP---GPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF--------- 567

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 419 tkKSLRQQLAYVSQQpylfegtirdnirygrpEATDAEVEEAARLAYAHDFISAQPQGYETPVGENGV----------TL 488
Cdd:PLN03073  568 --RSAKVRMAVFSQH-----------------HVDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVtgnlalqpmyTL 628

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1582666899 489 SGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAMSGrtVVVIAHR---LSTVVraDKIVVMQQGRV 563
Cdd:PLN03073  629 SGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMVSHDehlISGSV--DELWVVSEGKV 702

ABC_6TM_PrtD_LapB_HlyB_like

cd18566

Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ...

56-283

4.68e-07

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: 51.81 E-value: 4.68e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  56 MRAIIDEAFANRRADVVWIICLSIFIAFVLRGFASYGQAVALSKVGNDIVARYQRRLYAHLMTLSVGFFSEARSAHIAAQ 135
Cdd:cd18566    25 ILQVYDRVIPNESIPTLQVLVIGVVIAILLESLLRLLRSYILAWIGARFDHRLSNAAFEHLLSLPLSFFEREPSGAHLER 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 136 VSQnVSGIRDVLNLTITSTVRDL------LTFVSLLAVMILQDPLLSLAVFIMAPPLLyalryvSKRLRSATREAVHLNS 209
Cdd:cd18566   105 LNS-LEQIREFLTGQALLALLDLpfvlifLGLIWYLGGKLVLVPLVLLGLFVLVAILL------GPILRRALKERSRADE 177

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1582666899 210 HVLGAMQETIQGIAIVKAFTMEEELERKVNKLIKGAESRANRIARLSERTSPLTESFAGFAVASVLAYAAYRSI 283
Cdd:cd18566   178 RRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGFKVAKINAVAQTLGQLFSQVSMVAVVAFGALLVI 251

ABC_UvrA

cd03238

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...

476-567

7.97e-07

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.

Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 49.63 E-value: 7.97e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 476 GYETPvGENGVTLSGGQRQRLSIARALVRNAP--ILLLDEATSALDTESEAAVQKALDEAMS-GRTVVVIAHRLSTVVRA 552
Cdd:cd03238    77 GYLTL-GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDlGNTVILIEHNLDVLSSA 155

                          90       100
                  ....*....|....*....|.
gi 1582666899 553 DKIVVM------QQGRVVEEG 567
Cdd:cd03238   156 DWIIDFgpgsgkSGGKVVFSG 176

ABC_RNaseL_inhibitor

cd03222

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...

486-559

9.95e-07

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.

Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 49.11 E-value: 9.95e-07

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1582666899 486 VTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAM--SGRTVVVIAHRLSTVVR-ADKIVVMQ 559
Cdd:cd03222    70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeeGKKTALVVEHDLAVLDYlSDRIHVFE 146

PRK10636

putative ABC transporter ATP-binding protein; Provisional

357-541

1.08e-06

putative ABC transporter ATP-binding protein; Provisional

Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.71 E-value: 1.08e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 357 VSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIdgqdiahitKKSLRqqLAYVSQQpyl 436
Cdd:PRK10636  318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------AKGIK--LGYFAQH--- 383

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 437 fegtirdNIRYGRpeATDAEVEEAARLAyahdfisaqPQGYET--------------PVGENGVTLSGGQRQRLSIARAL 502
Cdd:PRK10636  384 -------QLEFLR--ADESPLQHLARLA---------PQELEQklrdylggfgfqgdKVTEETRRFSGGEKARLVLALIV 445

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1582666899 503 VRNAPILLLDEATSALDTESEAAVQKALDEaMSGRTVVV 541
Cdd:PRK10636  446 WQRPNLLLLDEPTNHLDLDMRQALTEALID-FEGALVVV 483

PRK10636

putative ABC transporter ATP-binding protein; Provisional

352-569

1.11e-06

putative ABC transporter ATP-binding protein; Provisional

Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.71 E-value: 1.11e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIprfydprEGEILIDGQDIAHITKkslrQQLAYVS 431
Cdd:PRK10636    2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALL-------KNEISADGGSYTFPGN----WQLAWVN 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQ-PYL----FEGTIRDNIRYGRPEATDAEVEE---AARLAYAH---DFISA-----------------QPQgYETPVGE 483
Cdd:PRK10636   71 QEtPALpqpaLEYVIDGDREYRQLEAQLHDANErndGHAIATIHgklDAIDAwtirsraasllhglgfsNEQ-LERPVSD 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 484 ngvtLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALdEAMSGrTVVVIAHR---LSTVVraDKIVVMQQ 560
Cdd:PRK10636  150 ----FSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWL-KSYQG-TLILISHDrdfLDPIV--DKIIHIEQ 221

                         250
                  ....*....|
gi 1582666899 561 GRVVE-EGNH 569
Cdd:PRK10636  222 QSLFEyTGNY 231

PRK10762

D-ribose transporter ATP binding protein; Provisional

367-572

2.14e-06

D-ribose transporter ATP binding protein; Provisional

Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.39 E-value: 2.14e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 367 LSG-----VSFTAEGGATTALVGPSGAGKSTVISLIprfYD--PRE-GEILIDGQDI-AHITKKSLRQQLAYVSQQP--- 434
Cdd:PRK10762  263 LSGpgvndVSFTLRKGEILGVSGLMGAGRTELMKVL---YGalPRTsGYVTLDGHEVvTRSPQDGLANGIVYISEDRkrd 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 435 -YLFEGTIRDN-----IRY-----GRPEAtDAEVEEAArlayahDFISA---QPQGYETPVGEngvtLSGGQRQRLSIAR 500
Cdd:PRK10762  340 gLVLGMSVKENmsltaLRYfsragGSLKH-ADEQQAVS------DFIRLfniKTPSMEQAIGL----LSGGNQQKVAIAR 408

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 501 ALVRNAPILLLDEATSALDT----ESEAAVQKALDEAMSgrtVVVIAHRLSTVV-RADKIVVMQQGRV-----VEEGNHE 570
Cdd:PRK10762  409 GLMTRPKVLILDEPTRGVDVgakkEIYQLINQFKAEGLS---IILVSSEMPEVLgMSDRILVMHEGRIsgeftREQATQE 485


                  ..
gi 1582666899 571 TL 572
Cdd:PRK10762  486 KL 487

ABC_6TM_ATM1_ABCB7

cd18582

Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ...

38-236

2.14e-06

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: 49.80 E-value: 2.14e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  38 AIACLIVVALSTAFTAWIMRAIIDeAFANRRADVVWIICLSIFIAFVLRGFAS---YGQAVALSKVGNDIVARYQRRLYA 114
Cdd:cd18582     1 ALLLLVLAKLLNVAVPFLLKYAVD-ALSAPASALLAVPLLLLLAYGLARILSSlfnELRDALFARVSQRAVRRLALRVFR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 115 HLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVM-ILQDPLLSLAVFIMAppLLYAL--R 191
Cdd:cd18582    80 HLHSLSLRFHLSRKTGALSRAIERGTRGIEFLLRFLLFNILPTILELLLVCGILwYLYGWSYALITLVTV--ALYVAftI 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1582666899 192 YVSKRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEE-ELER 236
Cdd:cd18582   158 KVTEWRTKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEyEAER 203

PRK13541

cytochrome c biogenesis protein CcmA; Provisional

352-552

4.03e-06

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 47.94 E-value: 4.03e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYgNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIAHITKKslrqQLAYVS 431
Cdd:PRK13541    2 LSLHQLQFNI-EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKP----YCTYIG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 QQPYL-FEGTIRDNIRYGrpeatdAEVEEAARLAYA-------HDFISaqpqgyetpvgENGVTLSGGQRQRLSIARALV 503
Cdd:PRK13541   77 HNLGLkLEMTVFENLKFW------SEIYNSAETLYAaihyfklHDLLD-----------EKCYSLSSGMQKIVAIARLIA 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1582666899 504 RNAPILLLDEATSALDTESEAAVQKALD-EAMSGRTVVVIAHRLSTVVRA 552
Cdd:PRK13541  140 CQSDLWLLDEVETNLSKENRDLLNNLIVmKANSGGIVLLSSHLESSIKSA 189

PLN03073

ABC transporter F family; Provisional

352-595

5.58e-06

ABC transporter F family; Provisional

Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.47 E-value: 5.58e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTV--------ISLIPRFYDPREGEILIDGQDI-------- 415
Cdd:PLN03073  178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFlrymamhaIDGIPKNCQILHVEQEVVGDDTtalqcvln 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 416 AHITKKSLRQQLAYVSQQPYLFE--------------GTIRDNIR------YGRPEATDAEVEEA-ARLAYAHDFISAQP 474
Cdd:PLN03073  258 TDIERTQLLEEEAQLVAQQRELEfetetgkgkgankdGVDKDAVSqrleeiYKRLELIDAYTAEArAASILAGLSFTPEM 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 475 QGYETPvgengvTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEAmsGRTVVVIAHR---LSTVVr 551
Cdd:PLN03073  338 QVKATK------TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKW--PKTFIVVSHArefLNTVV- 408

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1582666899 552 ADKIVVMQQGRVVEEGNHETLAKVSDglyARLNNLQRpsASDSN 595
Cdd:PLN03073  409 TDILHLHGQKLVTYKGDYDTFERTRE---EQLKNQQK--AFESN 447

PRK11147

ABC transporter ATPase component; Reviewed

352-571

1.24e-05

ABC transporter ATPase component; Reviewed

Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.41 E-value: 1.24e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 352 IEFRNVSFAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIPRFYDPREGEILIDgQDIAhitkkslrqqlayVS 431
Cdd:PRK11147    4 ISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLI-------------VA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 432 --QQ--PYLFEGTIRDNIRYGRPE---------------ATDAEVEEAARLAYAHDFISAQpQGY--------------- 477
Cdd:PRK11147   70 rlQQdpPRNVEGTVYDFVAEGIEEqaeylkryhdishlvETDPSEKNLNELAKLQEQLDHH-NLWqlenrinevlaqlgl 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 478 --ETPVGEngvtLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDEaMSGrTVVVIAHRLSTVVR-ADK 554
Cdd:PRK11147  149 dpDAALSS----LSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT-FQG-SIIFISHDRSFIRNmATR 222

                         250
                  ....*....|....*...
gi 1582666899 555 IVVMQQGRVVE-EGNHET 571
Cdd:PRK11147  223 IVDLDRGKLVSyPGNYDQ 240

rim_protein

TIGR01257

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...

377-546

1.46e-05

Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 48.47 E-value: 1.46e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  377 GATTALVGPSGAGKSTVISLIPRFYDPREGEILIDGQDIahITKKS-LRQQLAYVSQqpylFEG-----TIRDNIR-YGR 449
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTNISdVHQNMGYCPQ----FDAiddllTGREHLYlYAR 2038

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  450 PEATDA-EVEEAARLayahdfiSAQPQGYETPVGENGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQK 528
Cdd:TIGR01257 2039 LRGVPAeEIEKVANW-------SIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWN 2111

                          170
                   ....*....|....*....
gi 1582666899  529 ALDEAM-SGRTVVVIAHRL 546
Cdd:TIGR01257 2112 TIVSIIrEGRAVVLTSHSM 2130

uvrA

PRK00349

excinuclease ABC subunit UvrA;

457-577

1.66e-05

excinuclease ABC subunit UvrA;

Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 48.15 E-value: 1.66e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 457 VEEAArlayahDFISAQPQ-------------GYETpVGENGVTLSGGQRQRLSIARALVRNA---PILLLDEATSALDT 520
Cdd:PRK00349  794 VEEAL------EFFEAIPKiarklqtlvdvglGYIK-LGQPATTLSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHF 866

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1582666899 521 ESeaaVQKALD------EAmsGRTVVVIAHRLSTVVRADKIVVM------QQGRVVEEGNHETLAKVSD 577
Cdd:PRK00349  867 ED---IRKLLEvlhrlvDK--GNTVVVIEHNLDVIKTADWIIDLgpeggdGGGEIVATGTPEEVAKVEA 930

ABC_6TM_TAP2

cd18590

Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ...

101-243

3.03e-05

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: 46.18 E-value: 3.03e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 101 GNDIVARYQRRLYAHLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLAVF 180
Cdd:cd18590    64 LSRLNLRLRHQLFSSLVQQDIGFFEKTKTGDLTSRLSTDTTLMSRSVALNANVLLRSLVKTLGMLGFMLSLSWQLTLLTL 143

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 181 IMAPPLLYALRYVSKRLRSATREAVHLNSHVLGAMQETIQGIAIVKAFTMEEELERKVNKLIK 243
Cdd:cd18590   144 IEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALE 206

PRK10982

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

476-563

3.22e-05

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 3.22e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 476 GYETPVGengvTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAV-QKALDEAMSGRTVVVIAHRLSTVVR-AD 553
Cdd:PRK10982  384 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIyQLIAELAKKDKGIIIISSEMPELLGiTD 459

                          90
                  ....*....|
gi 1582666899 554 KIVVMQQGRV 563
Cdd:PRK10982  460 RILVMSNGLV 469

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

370-519

4.52e-05

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 46.66 E-value: 4.52e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 370 VSFTAEGGATTALVGPSGAGKSTVIS----LIPrfydPREGEIL-----IDGQDIAhitkksLRQQLAYVSQQPYLF-EG 439
Cdd:NF033858  285 VSFRIRRGEIFGFLGSNGCGKSTTMKmltgLLP----ASEGEAWlfgqpVDAGDIA------TRRRVGYMSQAFSLYgEL 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 440 TIRDNIR-----YGRPEATDAE-VEEAAR---LAyahDFISAQPQGyetpvgengvtLSGGQRQRLSIARALVRNAPILL 510
Cdd:NF033858  355 TVRQNLElharlFHLPAAEIAArVAEMLErfdLA---DVADALPDS-----------LPLGIRQRLSLAVAVIHKPELLI 420


                  ....*....
gi 1582666899 511 LDEATSALD 519
Cdd:NF033858  421 LDEPTSGVD 429

ABC_Rad50

cd03240

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...

380-556

7.76e-05

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.

Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 44.14 E-value: 7.76e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 380 TALVGPSGAGKSTVISLI--------PRFYDpregeiliDGQDIAHITKKSLRqqLAYVSQQPYLFEG---TIRDNIRYg 448
Cdd:cd03240    25 TLIVGQNGAGKTTIIEALkyaltgelPPNSK--------GGAHDPKLIREGEV--RAQVKLAFENANGkkyTITRSLAI- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 449 rpeatdaeVEEAArlayahdFIsaqPQG-YETPVGENGVTLSGGQRQ------RLSIARALVRNAPILLLDEATSALDTE 521
Cdd:cd03240    94 --------LENVI-------FC---HQGeSNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEE 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1582666899 522 SeaaVQKALDEAM------SGRTVVVIAHRLSTVVRADKIV 556
Cdd:cd03240   156 N---IEESLAEIIeerksqKNFQLIVITHDEELVDAADHIY 193

PRK15093

peptide ABC transporter ATP-binding protein SapD;

339-572

9.75e-05

peptide ABC transporter ATP-binding protein SapD;

Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 44.79 E-value: 9.75e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 339 LPDARPLTvtqarIEFRNvsfAYGNESVLSGVSFTAEGGATTALVGPSGAGKSTVISLIP--------------RFYD-- 402
Cdd:PRK15093    3 LLDIRNLT-----IEFKT---SDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICgvtkdnwrvtadrmRFDDid 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 403 -----PREGEILIdGQDIAHITK---------KSLRQQLayVSQQP-YLFEGTIRDNIRYGRPEAtdaeVEEAARLAYA- 466
Cdd:PRK15093   75 llrlsPRERRKLV-GHNVSMIFQepqscldpsERVGRQL--MQNIPgWTYKGRWWQRFGWRKRRA----IELLHRVGIKd 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 467 -HDFISAQPqgYEtpvgengvtLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVQKALDE--AMSGRTVVVIA 543
Cdd:PRK15093  148 hKDAMRSFP--YE---------LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRlnQNNNTTILLIS 216

                         250       260       270
                  ....*....|....*....|....*....|
gi 1582666899 544 HRLSTVVR-ADKIVVMQQGRVVEEGNHETL 572
Cdd:PRK15093  217 HDLQMLSQwADKINVLYCGQTVETAPSKEL 246

40850658_otr

NF000106

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

482-572

1.84e-04

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

Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 43.96 E-value: 1.84e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 482 GENGVTLSGGQRQRLSIARALVRNAPILLLDEATSALDTESEAAVqkaLDEAMS----GRTVVVIAHRLSTVVR-ADKIV 556
Cdd:NF000106  139 GRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEV---WDEVRSmvrdGATVLLTTQYMEEAEQlAHELT 215

                          90
                  ....*....|....*.
gi 1582666899 557 VMQQGRVVEEGNHETL 572
Cdd:NF000106  216 VIDRGRVIADGKVDEL 231

PRK00635

excinuclease ABC subunit A; Provisional

480-556

2.30e-04

excinuclease ABC subunit A; Provisional

Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 2.30e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  480 PVGENGVTLSGGQRQRLSIARAL---VRNAPILLLDEATSALDTES-EAAVQKALDEAMSGRTVVVIAHRLSTVVRADKI 555
Cdd:PRK00635   802 PLGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYV 881


                   .
gi 1582666899  556 V 556
Cdd:PRK00635   882 L 882

ABC_6TM_PrtD_like

cd18586

Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ...

74-291

2.41e-04

Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS metalloprotease secretion system, and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS) such as PrtD, which is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). 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. The Aquifex aeolicus PrtDEF of T1SS is composed of an inner-membrane ABC transporter (PrtD), a periplasmic membrane-fusion protein (PrtE), and an outer-membrane porin (PrtF). These three components assemble into complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides

Pssm-ID: 350030 [Multi-domain] Cd Length: 291 Bit Score: 43.36 E-value: 2.41e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  74 IICLSIFIA-FVLRGFASYgqavALSKVGNDIVARYQRRLYAHLMTLSVgffsEARSAHIAAQvsqnvsGIRDVLNL--T 150
Cdd:cd18586    46 LGMVVLLAFdGLLRQVRSR----ILQRVGLRLDVELGRRVFRAVLELPL----ESRPSGYWQQ------LLRDLDTLrnF 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 151 ITS----TVRDLLTFVSLLAVMILQDPLLSLaVFIMAPPLLYALRYVSKRL-RSATREAVHLNSHVLGAMQETIQGIAIV 225
Cdd:cd18586   112 LTGpslfAFFDLPWAPLFLAVIFLIHPPLGW-VALVGAPVLVGLAWLNHRAtRKPLGEANEAQAARDALAAETLRNAETI 190

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 226 KAFTMEEELER----KVNKLIKGAESRANRIARLSERTSPLTEsfagFAVASVLAYAAYRSIYFNVPPGA 291
Cdd:cd18586   191 KALGMLGNLRRrweaRHAETLELQIRASDLAGAISAIGKTLRM----ALQSLILGVGAYLVIDGELTIGA 256

UvrA

COG0178

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

457-577

3.32e-04

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

Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.86 E-value: 3.32e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 457 VEEAArlayahDFISAQPQ-------------GYETpVGENGVTLSGGQRQRLSIARALVRNAP---ILLLDEATSAL-- 518
Cdd:COG0178   790 VEEAL------EFFENIPKiarklqtlqdvglGYIK-LGQPATTLSGGEAQRVKLASELSKRSTgktLYILDEPTTGLhf 862

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1582666899 519 -DteseaaVQKALD------EAmsGRTVVVIAHRLStVVR-ADKIVVM------QQGRVVEEGNHETLAKVSD 577
Cdd:COG0178   863 hD------IRKLLEvlhrlvDK--GNTVVVIEHNLD-VIKtADWIIDLgpeggdGGGEIVAEGTPEEVAKVKA 926

guanyl_kin

TIGR03263

guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP ...

382-414

3.96e-04

guanylate kinase; Members of this family are the enzyme guanylate kinase, also called GMP kinase. This enzyme transfers a phosphate from ATP to GMP, yielding ADP and GDP. [Purines, pyrimidines, nucleosides, and nucleotides, Nucleotide and nucleoside interconversions]

Pssm-ID: 213788 Cd Length: 179 Bit Score: 41.71 E-value: 3.96e-04

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1582666899 382 LVGPSGAGKSTVISLI----PRFY--------DPREGEilIDGQD 414
Cdd:TIGR03263   5 ISGPSGAGKSTLVKALleedPNLKfsisattrKPRPGE--VDGVD 47

ABC_sbcCD

cd03279

ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...

351-544

4.04e-04

ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.

Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 41.87 E-value: 4.04e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 351 RIEFRNVSFAYGNESVlsgvSFTA-EGGATTALVGPSGAGKSTVISLIP-RFYdpreGEILIDGQDIAHITKKSLRQQLA 428
Cdd:cd03279     5 KLELKNFGPFREEQVI----DFTGlDNNGLFLICGPTGAGKSTILDAITyALY----GKTPRYGRQENLRSVFAPGEDTA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 429 YVSqqpylFEGTIRdNIRYgrpeatdaEVEEAARLAYaHDFISAQ--PQG-----YETPVGengvTLSGGQRQRLSIARA 501
Cdd:cd03279    77 EVS-----FTFQLG-GKKY--------RVERSRGLDY-DQFTRIVllPQGefdrfLARPVS----TLSGGETFLASLSLA 137

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1582666899 502 L--------VRNAPI--LLLDEATSALDTESEAAVQKALDE-AMSGRTVVVIAH 544
Cdd:cd03279   138 LalsevlqnRGGARLeaLFIDEGFGTLDPEALEAVATALELiRTENRMVGVISH 191

GMPK

cd00071

Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ...

382-420

5.18e-04

Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.

Pssm-ID: 238026 Cd Length: 137 Bit Score: 40.59 E-value: 5.18e-04

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1582666899 382 LVGPSGAGKSTVIS-LIPRFYD------------PREGEilIDGQDIAHITK 420
Cdd:cd00071     4 LSGPSGVGKSTLLKrLLEEFDPnfgfsvshttrkPRPGE--VDGVDYHFVSK 53

ABC_6TM_TAP1

cd18589

Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ...

104-296

7.40e-04

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: 41.69 E-value: 7.40e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 104 IVARYQRRLYAHLMTLSVGFFSEARSAHIAAQVSQNVSGIRDVLNLTITSTVRDLLTFVSLLAVMILQDPLLSLaVFIMA 183
Cdd:cd18589    67 IHSRLQGLVFAAVLRQEIAFFDSNQTGDIVSRVTTDTEDMSESLSENLSLLMWYLARGLFLFIFMLWLSPKLAL-LTALG 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 184 PPLLYALRYVSKRLRSATreAVHLNSHVLGAMQ---ETIQGIAIVKAFTMEE-ELERKVNKLIKgaESRANRIARLSERT 259
Cdd:cd18589   146 LPLLLLVPKFVGKFQQSL--AVQVQKSLARANQvavETFSAMKTVRSFANEEgEAQRYRQRLQK--TYRLNKKEAAAYAV 221

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1582666899 260 SPLTESFAGFAV-ASVLAYAAYRSIYFNVPPGAFFSFV 296
Cdd:cd18589   222 SMWTSSFSGLALkVGILYYGGQLVTAGTVSSGDLVTFV 259

ABC_6TM_YOR1_D2_like

cd18606

Six-transmembrane helical domain 2 (TMD2) of the yeast Yor1p and similar proteins; ABCC ...

145-242

8.17e-04

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: 41.69 E-value: 8.17e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 145 DVLNLTITSTVRDLL-TFVSLLAVMIL---QDPLLSLAVfimaPPLLYALRYVSKRLRSATREAVHLN----SHVLGAMQ 216
Cdd:cd18606   103 DVLDNELPDSLRMFLyTLSSIIGTFILiiiYLPWFAIAL----PPLLVLYYFIANYYRASSRELKRLEsilrSFVYANFS 178

                          90       100
                  ....*....|....*....|....*.
gi 1582666899 217 ETIQGIAIVKAFTMEEELERKVNKLI 242
Cdd:cd18606   179 ESLSGLSTIRAYGAQDRFIKKNEKLI 204

PRK00635

excinuclease ABC subunit A; Provisional

476-561

8.59e-04

excinuclease ABC subunit A; Provisional

Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 8.59e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  476 GYeTPVGENGVTLSGGQRQRLSIARALV---RNAPILLLDEATSALDTESEAAVQKALDEAMS-GRTVVVIAHRLSTVVR 551
Cdd:PRK00635  1689 GY-LPLGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSlGHSVIYIDHDPALLKQ 1767

                           90
                   ....*....|
gi 1582666899  552 ADKIVVMQQG 561
Cdd:PRK00635  1768 ADYLIEMGPG 1777

SMC_N

pfam02463

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...

470-563

9.37e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.

Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 42.27 E-value: 9.37e-04

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899  470 ISAQPQGYETPVGENgvtLSGGQRQRLSIA--RAL--VRNAPILLLDEATSALDTESEAAVQKALDEAMSGRTVVVIAHR 545
Cdd:pfam02463 1063 ISARPPGKGVKNLDL---LSGGEKTLVALAliFAIqkYKPAPFYLLDEIDAALDDQNVSRVANLLKELSKNAQFIVISLR 1139

                           90       100
                   ....*....|....*....|
gi 1582666899  546 LSTVVRADKI--VVMQQGRV 563
Cdd:pfam02463 1140 EEMLEKADKLvgVTMVENGV 1159

GguA

NF040905

sugar ABC transporter ATP-binding protein;

366-566

2.43e-03

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.54 E-value: 2.43e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 366 VLSGVSFTAEGGATTALVGPSGAGKS-TVISLIPRFYDPR-EGEILIDGQDIAHIT-KKSLRQQLAYVS----QQPYLFE 438
Cdd:NF040905  275 VVDDVSLNVRRGEIVGIAGLMGAGRTeLAMSVFGRSYGRNiSGTVFKDGKEVDVSTvSDAIDAGLAYVTedrkGYGLNLI 354

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 439 GTIRDNI---------RYGRpeatdaeVEEAARLAYAHDFISAQpqGYETP-VGENGVTLSGGQRQRLSIARALVRNAPI 508
Cdd:NF040905  355 DDIKRNItlanlgkvsRRGV-------IDENEEIKVAEEYRKKM--NIKTPsVFQKVGNLSGGNQQKVVLSKWLFTDPDV 425

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 509 LLLDEATSALDTESEAAVQKALDE-AMSGRTVVVIAHRLSTVV-RADKIVVMQQGRVVEE 566
Cdd:NF040905  426 LILDEPTRGIDVGAKYEIYTIINElAAEGKGVIVISSELPELLgMCDRIYVMNEGRITGE 485

Gmk

COG0194

Guanylate kinase [Nucleotide transport and metabolism];

382-414

2.64e-03

Guanylate kinase [Nucleotide transport and metabolism];

Pssm-ID: 439964 Cd Length: 190 Bit Score: 39.28 E-value: 2.64e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1582666899 382 LVGPSGAGKSTVIS-LIPRFYD-----------PREGEilIDGQD 414
Cdd:COG0194     7 LSGPSGAGKTTLVKaLLERDPDlrfsvsattrpPRPGE--VDGVD 49

ABC_SMC_barmotin

cd03278

ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...

380-560

3.83e-03

ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).

Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 38.99 E-value: 3.83e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 380 TALVGPSGAGKSTVISLIpRFydpregeILidGQDIAhitkKSLRQqlayvsqqpylfeGTIRDNIRYG---RPEATDAE 456
Cdd:cd03278    25 TAIVGPNGSGKSNIIDAI-RW-------VL--GEQSA----KSLRG-------------EKMSDVIFAGsetRKPANFAE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 457 VE---EAARLAYAhdFISaqpQG-----YETPvGENGVT---LSGGQRQRLSIAR--AL--VRNAPILLLDEATSALDte 521
Cdd:cd03278    78 VTltfDNSDGRYS--IIS---QGdvseiIEAP-GKKVQRlslLSGGEKALTALALlfAIfrVRPSPFCVLDEVDAALD-- 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1582666899 522 sEAAVQK--ALDEAMSGRT-VVVIAHRLSTVVRADKI--VVMQQ 560
Cdd:cd03278   150 -DANVERfaRLLKEFSKETqFIVITHRKGTMEAADRLygVTMQE 192

gmk

PRK00300

guanylate kinase; Provisional

382-414

4.51e-03

guanylate kinase; Provisional

Pssm-ID: 234719 Cd Length: 205 Bit Score: 38.92 E-value: 4.51e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1582666899 382 LVGPSGAGKSTVISLI----PRFY--------DPREGEilIDGQD 414
Cdd:PRK00300   10 LSGPSGAGKSTLVKALlerdPNLQlsvsattrAPRPGE--VDGVD 52

ABC_UvrA_I

cd03270

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...

487-567

7.69e-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: 38.39 E-value: 7.69e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1582666899 487 TLSGGQRQRLSIARALVRN--APILLLDEATSAL---DTESEAAVQKALDEAmsGRTVVVIAHRLSTVVRADKIVVM--- 558
Cdd:cd03270   137 TLSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLhprDNDRLIETLKRLRDL--GNTVLVVEHDEDTIRAADHVIDIgpg 214

                          90
                  ....*....|..
gi 1582666899 559 ---QQGRVVEEG 567
Cdd:cd03270   215 agvHGGEIVAQG 226

Blast search parameters

Data Source:	Precalculated data, version = cdd.v.3.21
Preset Options:	Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01