NCBI Conserved Domain Search

Conserved domains on [gi|755511082|ref|XP_011248092|]

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mitochondrial potassium channel ATP-binding subunit isoform X2 [Mus musculus]

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];

1-426

1.50e-179

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

Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 513.94 E-value: 1.50e-179

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   1 MLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKA 80
Cdd:COG1132  158 VIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRAN 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  81 EELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARVFEY 160
Cdd:COG1132  238 LRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFEL 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 161 MALSPVIPLTGGYcIPNKDIRGSITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEA 240
Cdd:COG1132  318 LDEPPEIPDPPGA-VPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTS 394

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 241 GSVTLDGHDLRTLNPSWLRGQvIGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGER 320
Cdd:COG1132  395 GRILIDGVDIRDLTLESLRRQ-IGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGER 473

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 321 GTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVC 400
Cdd:COG1132  474 GVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIV 553

                        410       420
                 ....*....|....*....|....*.
gi 755511082 401 EAGTHEELLKKGGLYSELIRRQTLDA 426
Cdd:COG1132  554 EQGTHEELLARGGLYARLYRLQFGEE 579

Name

Accession

Description

Interval

E-value

MdlB

COG1132

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

1-426

1.50e-179

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

Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 513.94 E-value: 1.50e-179

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   1 MLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKA 80
Cdd:COG1132  158 VIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRAN 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  81 EELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARVFEY 160
Cdd:COG1132  238 LRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFEL 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 161 MALSPVIPLTGGYcIPNKDIRGSITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEA 240
Cdd:COG1132  318 LDEPPEIPDPPGA-VPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTS 394

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 241 GSVTLDGHDLRTLNPSWLRGQvIGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGER 320
Cdd:COG1132  395 GRILIDGVDIRDLTLESLRRQ-IGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGER 473

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 321 GTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVC 400
Cdd:COG1132  474 GVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIV 553

                        410       420
                 ....*....|....*....|....*.
gi 755511082 401 EAGTHEELLKKGGLYSELIRRQTLDA 426
Cdd:COG1132  554 EQGTHEELLARGGLYARLYRLQFGEE 579

ABC_MTABC3_MDL1_MDL2

cd03249

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

184-422

1.50e-147

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: 419.64 E-value: 1.50e-147

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQvI 263
Cdd:cd03249    1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ-I 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPT 343
Cdd:cd03249   80 GLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755511082 344 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELIRRQ 422
Cdd:cd03249  160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238

3a01208

TIGR00958

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

2-419

3.52e-137

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

Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 410.27 E-value: 3.52e-137

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082    2 LSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESC--CCK 79
Cdd:TIGR00958 299 LSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETlqLNK 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   80 AEELGRgiALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARVFE 159
Cdd:TIGR00958 379 RKALAY--AGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFE 456

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  160 YMALSPVIPLTGGYCIPNkdIRGSITFQNVTFSYPCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPE 239
Cdd:TIGR00958 457 YLDRKPNIPLTGTLAPLN--LEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPT 534

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  240 AGSVTLDGHDLRTLNPSWLRGQViGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGE 319
Cdd:TIGR00958 535 GGQVLLDGVPLVQYDHHYLHRQV-ALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGE 613

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  320 RGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEalDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQV 399
Cdd:TIGR00958 614 KGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSV 691

                         410       420
                  ....*....|....*....|
gi 755511082  400 CEAGTHEELLKKGGLYSELI 419
Cdd:TIGR00958 692 VEMGTHKQLMEDQGCYKHLV 711

PRK13657

glucan ABC transporter ATP-binding protein/ permease;

5-435

7.29e-97

glucan ABC transporter ATP-binding protein/ permease;

Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 302.65 E-value: 7.29e-97

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   5 RLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAmekreeeRYQAELESCCCKAEELG 84
Cdd:PRK13657 157 RLSLVLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYN-------RIEAETQALRDIADNLL 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  85 RG-------IALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFL-VASQTVQRsmasLSVLFGQVVRGLSAGAR 156
Cdd:PRK13657 230 AAqmpvlswWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVgFATLLIGR----LDQVVAFINQVFMAAPK 305

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 157 VFEYMALSPVIPLTG--GYCIPNKDIRGSITFQNVTFSYP-CRPGfnvLKDFTLKLPSGKIVALVGQSGGGKTTVASLLE 233
Cdd:PRK13657 306 LEEFFEVEDAVPDVRdpPGAIDLGRVKGAVEFDDVSFSYDnSRQG---VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQ 382

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 234 RFYDPEAGSVTLDGHDLRTLNPSWLRgQVIGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGY 313
Cdd:PRK13657 383 RVFDPQSGRILIDGTDIRTVTRASLR-RNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGY 461

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 314 STVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIV 393
Cdd:PRK13657 462 DTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILV 541

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 755511082 394 MANGQVCEAGTHEELLKKGGLYSELIRRQ--TLDASLTSTPPAE 435
Cdd:PRK13657 542 FDNGRVVESGSFDELVARGGRFAALLRAQgmLQEDERRKQPAAE 585

ABC_tran

pfam00005

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

202-352

4.88e-43

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: 148.56 E-value: 4.88e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  202 LKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQvIGFISQEPVLF-ATTIMEN 280
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKE-IGYVFQDPQLFpRLTVREN 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755511082  281 IRFGkldASDEEVYTAAREANAHEFISSF--PDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATS 352
Cdd:pfam00005  80 LRLG---LLLKGLSKREKDARAEEALEKLglGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150

AztA

NF040873

zinc ABC transporter ATP-binding protein AztA;

192-394

8.56e-21

zinc ABC transporter ATP-binding protein AztA;

Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.60 E-value: 8.56e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 192 SYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSwlrgqvigfISQEPV 271
Cdd:NF040873   1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ---------RSEVPD 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 272 LFATTIMENIRFG---------KLDASDEEVYTAAREANahefissfpdGYSTVVGERGTTLSGGQKQRLAIARALIKQP 342
Cdd:NF040873  69 SLPLTVRDLVAMGrwarrglwrRLTRDDRAAVDDALERV----------GLADLAGRQLGELSGGQRQRALLAQGLAQEA 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755511082 343 TVLILDEATSALDAESERVVQEALDRASA-GRTVLVIAHRLSTVRAAHSIIVM 394
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCVLL 191

GguA

NF040905

sugar ABC transporter ATP-binding protein;

197-401

6.63e-13

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 70.20 E-value: 6.63e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 197 PGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYdPEA---GSVTLDGH--DLRTLNPSWLRGQVIgfISQE-- 269
Cdd:NF040905  12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEvcRFKDIRDSEALGIVI--IHQEla 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 270 --PVLfatTIMENI-------RFGKLDAsdEEVYTAAREANAHEFISSFPDgysTVVGERGTtlsgGQKQRLAIARALIK 340
Cdd:NF040905  89 liPYL---SIAENIflgneraKRGVIDW--NETNRRARELLAKVGLDESPD---TLVTDIGV----GKQQLVEIAKALSK 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755511082 341 QPTVLILDEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCE 401
Cdd:NF040905 157 DVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219

AAA

smart00382

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

211-392

6.28e-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: 57.38 E-value: 6.28e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   211 SGKIVALVGQSGGGKTTVASLLERFYDPEAGSVtldghdlRTLNPSWLRGQVIGFISQEPVlfattimenirfgkldasd 290
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV-------IYIDGEDILEEVLDQLLLIIV------------------- 54

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   291 eevytaareanahefissfpdgystvvGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALD--- 367
Cdd:smart00382  55 ---------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107

                          170       180
                   ....*....|....*....|....*....
gi 755511082   368 ----RASAGRTVLVIAHRLSTVRAAHSII 392
Cdd:smart00382 108 llllKSEKNLTVILTTNDEKDLGPALLRR 136

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

202-441

7.68e-10

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.29 E-value: 7.68e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 202 LKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRtlNPSWlRGQV---IGFISQ------EPVL 272
Cdd:NF033858  17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DARH-RRAVcprIAYMPQglgknlYPTL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 273 fatTIMENIRF-GKL---DAsdeevytAAREANAHEF-----ISSFPD---GystvvgergtTLSGGQKQRLAIARALIK 340
Cdd:NF033858  94 ---SVFENLDFfGRLfgqDA-------AERRRRIDELlratgLAPFADrpaG----------KLSGGMKQKLGLCCALIH 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 341 QPTVLILDEATSALDAESERVVQEALDRASAGR---TVLViahrlSTV------RAAHsIIVMANGQVCEAGTHEELLKK 411
Cdd:NF033858 154 DPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpgmSVLV-----ATAymeeaeRFDW-LVAMDAGRVLATGTPAELLAR 227

                        250       260       270
                 ....*....|....*....|....*....|
gi 755511082 412 GGlyselirRQTLDASLTSTPPAEKPEDPK 441
Cdd:NF033858 228 TG-------ADTLEAAFIALLPEEKRRGHQ 250

40850658_otr

NF000106

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

300-420

1.23e-07

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

Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.20 E-value: 1.23e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 300 ANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVV-QEALDRASAGRTVLVI 378
Cdd:NF000106 123 ARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMVRDGATVLLT 200

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 755511082 379 AHRLSTV-RAAHSIIVMANGQVCEAGTHEELLKKGGLYSELIR 420
Cdd:NF000106 201 TQYMEEAeQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIR 243

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

204-355

4.82e-06

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.97 E-value: 4.82e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 204 DFT------LKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTL-----DGHDLRTlnpswlRGQViGFISQEPVL 272
Cdd:NF033858 278 DFTavdhvsFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDAGDIAT------RRRV-GYMSQAFSL 350

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 273 FAT-TIMENIrfgKLDASDEEVYTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEAT 351
Cdd:NF033858 351 YGElTVRQNL---ELHARLFHLPAAEIAARVAEMLERF--DLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425


                 ....
gi 755511082 352 SALD 355
Cdd:NF033858 426 SGVD 429

GguA

NF040905

sugar ABC transporter ATP-binding protein;

194-378

3.59e-05

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 3.59e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 194 PCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVA-SLLERFYDP-EAGSVTLDGHDLRTLNPSWLRGQVIGFISQEP- 270
Cdd:NF040905 268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAmSVFGRSYGRnISGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRk 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 271 ----VLfATTIMENIRFGKLDA-SDEEVYTAAREAN-AHEFISSF----PDGYSTVVgergtTLSGGQKQRLAIARALIK 340
Cdd:NF040905 348 gyglNL-IDDIKRNITLANLGKvSRRGVIDENEEIKvAEEYRKKMniktPSVFQKVG-----NLSGGNQQKVVLSKWLFT 421

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 755511082 341 QPTVLILDEATSALD--AESE--RVVQEAldrASAGRTVLVI 378
Cdd:NF040905 422 DPDVLILDEPTRGIDvgAKYEiyTIINEL---AAEGKGVIVI 460

Name

Accession

Description

Interval

E-value

MdlB

COG1132

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

1-426

1.50e-179

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

Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 513.94 E-value: 1.50e-179

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   1 MLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKA 80
Cdd:COG1132  158 VIDWRLALIVLLVLPLLLLVLRLFGRRLRKLFRRVQEALAELNGRLQESLSGIRVVKAFGREERELERFREANEELRRAN 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  81 EELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARVFEY 160
Cdd:COG1132  238 LRAARLSALFFPLMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILYLLRLFGPLRQLANVLNQLQRALASAERIFEL 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 161 MALSPVIPLTGGYcIPNKDIRGSITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEA 240
Cdd:COG1132  318 LDEPPEIPDPPGA-VPLPPVRGEIEFENVSFSYP--GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTS 394

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 241 GSVTLDGHDLRTLNPSWLRGQvIGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGER 320
Cdd:COG1132  395 GRILIDGVDIRDLTLESLRRQ-IGVVPQDTFLFSGTIRENIRYGRPDATDEEVEEAAKAAQAHEFIEALPDGYDTVVGER 473

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 321 GTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVC 400
Cdd:COG1132  474 GVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRNADRILVLDDGRIV 553

                        410       420
                 ....*....|....*....|....*.
gi 755511082 401 EAGTHEELLKKGGLYSELIRRQTLDA 426
Cdd:COG1132  554 EQGTHEELLARGGLYARLYRLQFGEE 579

ABC_MTABC3_MDL1_MDL2

cd03249

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

184-422

1.50e-147

Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 419.64 E-value: 1.50e-147

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQvI 263
Cdd:cd03249    1 IEFKNVSFRYPSRPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQ-I 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPT 343
Cdd:cd03249   80 GLVSQEPVLFDGTIAENIRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYDTLVGERGSQLSGGQKQRIAIARALLRNPK 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755511082 344 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELIRRQ 422
Cdd:cd03249  160 ILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGTHDELMAQKGVYAKLVKAQ 238

SunT

COG2274

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

1-423

1.12e-139

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: 416.54 E-value: 1.12e-139

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   1 MLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCcKA 80
Cdd:COG2274  292 FYSPPLALVVLLLIPLYVLLGLLFQPRLRRLSREESEASAKRQSLLVETLRGIETIKALGAESRFRRRWENLLAKYL-NA 370

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  81 EELGRGIALFQGLSNIAFNCMV-LGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARVFE 159
Cdd:COG2274  371 RFKLRRLSNLLSTLSGLLQQLAtVALLWLGAYLVIDGQLTLGQLIAFNILSGRFLAPVAQLIGLLQRFQDAKIALERLDD 450

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 160 YMALsPVIPLTGGYCIPNKDIRGSITFQNVTFSYPcRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPE 239
Cdd:COG2274  451 ILDL-PPEREEGRSKLSLPRLKGDIELENVSFRYP-GDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT 528

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 240 AGSVTLDGHDLRTLNPSWLRGQvIGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGE 319
Cdd:COG2274  529 SGRILIDGIDLRQIDPASLRRQ-IGVVLQDVFLFSGTIRENITLGDPDATDEEIIEAARLAGLHDFIEALPMGYDTVVGE 607

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 320 RGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQV 399
Cdd:COG2274  608 GGSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRI 687

                        410       420
                 ....*....|....*....|....
gi 755511082 400 CEAGTHEELLKKGGLYSELIRRQT 423
Cdd:COG2274  688 VEDGTHEELLARKGLYAELVQQQL 711

3a01208

TIGR00958

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

2-419

3.52e-137

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

Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 410.27 E-value: 3.52e-137

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082    2 LSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESC--CCK 79
Cdd:TIGR00958 299 LSPRLTMVTLINLPLVFLAEKVFGKRYQLLSEELQEAVAKANQVAEEALSGMRTVRSFAAEEGEASRFKEALEETlqLNK 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   80 AEELGRgiALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARVFE 159
Cdd:TIGR00958 379 RKALAY--AGYLWTTSVLGMLIQVLVLYYGGQLVLTGKVSSGNLVSFLLYQEQLGEAVRVLSYVYSGMMQAVGASEKVFE 456

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  160 YMALSPVIPLTGGYCIPNkdIRGSITFQNVTFSYPCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPE 239
Cdd:TIGR00958 457 YLDRKPNIPLTGTLAPLN--LEGLIEFQDVSFSYPNRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPT 534

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  240 AGSVTLDGHDLRTLNPSWLRGQViGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGE 319
Cdd:TIGR00958 535 GGQVLLDGVPLVQYDHHYLHRQV-ALVGQEPVLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGE 613

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  320 RGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEalDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQV 399
Cdd:TIGR00958 614 KGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAECEQLLQE--SRSRASRTVLLIAHRLSTVERADQILVLKKGSV 691

                         410       420
                  ....*....|....*....|
gi 755511082  400 CEAGTHEELLKKGGLYSELI 419
Cdd:TIGR00958 692 VEMGTHKQLMEDQGCYKHLV 711

MsbA_rel

TIGR02204

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

3-422

1.09e-133

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: 396.76 E-value: 1.09e-133

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082    3 SPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELEscccKAEE 82
Cdd:TIGR02204 157 SPKLTSLVLLAVPLVLLPILLFGRRVRKLSRESQDRIADAGSYAGETLGAIRTVQAFGHEDAERSRFGGAVE----KAYE 232

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   83 LGRG-----IALFQGLSNIAFNCMVlGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 157
Cdd:TIGR02204 233 AARQrirtrALLTAIVIVLVFGAIV-GVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEVWGELQRAAGAAERL 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  158 FEYMALSPVIPLTGGYCIPNKDIRGSITFQNVTFSYPCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYD 237
Cdd:TIGR02204 312 IELLQAEPDIKAPAHPKTLPVPLRGEIEFEQVNFAYPARPDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYD 391

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  238 PEAGSVTLDGHDLRTLNPSWLRgQVIGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVV 317
Cdd:TIGR02204 392 PQSGRILLDGVDLRQLDPAELR-ARMALVPQDPVLFAASVMENIRYGRPDATDEEVEAAARAAHAHEFISALPEGYDTYL 470

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  318 GERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANG 397
Cdd:TIGR02204 471 GERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDAESEQLVQQALETLMKGRTTLIIAHRLATVLKADRIVVMDQG 550

                         410       420
                  ....*....|....*....|....*
gi 755511082  398 QVCEAGTHEELLKKGGLYSELIRRQ 422
Cdd:TIGR02204 551 RIVAQGTHAELIAKGGLYARLARLQ 575

ABCC_MsbA

cd03251

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

184-418

7.96e-124

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: 359.24 E-value: 7.96e-124

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPGfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQvI 263
Cdd:cd03251    1 VEFKNVTFRYPGDGP-PVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ-I 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPT 343
Cdd:cd03251   79 GLVSQDVFLFNDTVAENIAYGRPGATREEVEEAARAANAHEFIMELPEGYDTVIGERGVKLSGGQRQRIAIARALLKDPP 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755511082 344 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSEL 418
Cdd:cd03251  159 ILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGTHEELLAQGGVYAKL 233

ATM1

COG5265

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

30-422

4.48e-119

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: 360.29 E-value: 4.48e-119

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  30 KLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAEELGRGIALFQGLSNIAFNCMVLGTLFIG 109
Cdd:COG5265  205 KFRREMNEADSEANTRAVDSLLNYETVKYFGNEAREARRYDEALARYERAAVKSQTSLALLNFGQALIIALGLTAMMLMA 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 110 GSLVAGQQLKGGDLMsfLVASQTVQRSMA--SLSVLFGQVVRGLSAGARVFEYMALSPVI-------PLTGGycipnkdi 180
Cdd:COG5265  285 AQGVVAGTMTVGDFV--LVNAYLIQLYIPlnFLGFVYREIRQALADMERMFDLLDQPPEVadapdapPLVVG-------- 354

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 181 RGSITFQNVTFSY-PCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLR 259
Cdd:COG5265  355 GGEVRFENVSFGYdPERP---ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLR 431

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 260 gQVIGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALI 339
Cdd:COG5265  432 -AAIGIVPQDTVLFNDTIAYNIAYGRPDASEEEVEAAARAAQIHDFIESLPDGYDTRVGERGLKLSGGEKQRVAIARTLL 510

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 340 KQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELI 419
Cdd:COG5265  511 KNPPILIFDEATSALDSRTERAIQAALREVARGRTTLVIAHRLSTIVDADEILVLEAGRIVERGTHAELLAQGGLYAQMW 590


                 ...
gi 755511082 420 RRQ 422
Cdd:COG5265  591 ARQ 593

ABCC_ATM1_transporter

cd03253

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

184-422

3.35e-118

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: 344.98 E-value: 3.35e-118

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgQVI 263
Cdd:cd03253    1 IEFENVTFAYD--PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLR-RAI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPT 343
Cdd:cd03253   78 GVVPQDTVLFNDTIGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLKLSGGEKQRVAIARAILKNPP 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755511082 344 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELIRRQ 422
Cdd:cd03253  158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGLYAEMWKAQ 236

MsbA_lipidA

TIGR02203

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

2-422

3.40e-115

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: 349.40 E-value: 3.40e-115

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082    2 LSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAE 81
Cdd:TIGR02203 152 YSWQLTLIVVVMLPVLSILMRRVSKRLRRISKEIQNSMGQVTTVAEETLQGYRVVKLFGGQAYETRRFDAVSNRNRRLAM 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   82 ELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARVFEYM 161
Cdd:TIGR02203 232 KMTSAGSISSPITQLIASLALAVVLFIALFQAQAGSLTAGDFTAFITAMIALIRPLKSLTNVNAPMQRGLAAAESLFTLL 311

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  162 AlSPVIPLTGGYCIPNkdIRGSITFQNVTFSYPCRpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAG 241
Cdd:TIGR02203 312 D-SPPEKDTGTRAIER--ARGDVEFRNVTFRYPGR-DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSG 387

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  242 SVTLDGHDLRTLNPSWLRGQvIGFISQEPVLFATTIMENIRFGKL-DASDEEVYTAAREANAHEFISSFPDGYSTVVGER 320
Cdd:TIGR02203 388 QILLDGHDLADYTLASLRRQ-VALVSQDVVLFNDTIANNIAYGRTeQADRAEIERALAAAYAQDFVDKLPLGLDTPIGEN 466

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  321 GTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVC 400
Cdd:TIGR02203 467 GVLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIAHRLSTIEKADRIVVMDDGRIV 546

                         410       420
                  ....*....|....*....|..
gi 755511082  401 EAGTHEELLKKGGLYSELIRRQ 422
Cdd:TIGR02203 547 ERGTHNELLARNGLYAQLHNMQ 568

CydD

COG4988

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

150-413

5.62e-107

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: 327.87 E-value: 5.62e-107

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 150 GLSAGARVFEYMALSPVIPLTGGYCIPNKDIrGSITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVA 229
Cdd:COG4988  304 GIAAAEKIFALLDAPEPAAPAGTAPLPAAGP-PSIELEDVSFSYP--GGRPALDGLSLTIPPGERVALVGPSGAGKSTLL 380

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 230 SLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQvIGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSF 309
Cdd:COG4988  381 NLLLGFLPPYSGSILINGVDLSDLDPASWRRQ-IAWVPQNPYLFAGTIRENLRLGRPDASDEELEAALEAAGLDEFVAAL 459

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 310 PDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAH 389
Cdd:COG4988  460 PDGLDTPLGEGGRGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALLAQAD 539

                        250       260
                 ....*....|....*....|....
gi 755511082 390 SIIVMANGQVCEAGTHEELLKKGG 413
Cdd:COG4988  540 RILVLDDGRIVEQGTHEELLAKNG 563

ABCC_Glucan_exporter_like

cd03254

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

182-413

1.10e-103

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: 307.61 E-value: 1.10e-103

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 182 GSITFQNVTFSYpcRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQ 261
Cdd:cd03254    1 GEIEFENVNFSY--DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 262 vIGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQ 341
Cdd:cd03254   79 -IGVVLQDTFLFSGTIMENIRLGRPNATDEEVIEAAKEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRD 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755511082 342 PTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGG 413
Cdd:cd03254  158 PKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAKKG 229

CydC

COG4987

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

2-421

2.86e-103

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: 318.25 E-value: 2.86e-103

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   2 LSPRLTLMLAVvtpALMGVGTLMGSGLRKLSRQCQEQIARATG----VADEALGNVRTVRAFAMEKREEERYQAeLESCC 77
Cdd:COG4987  153 FSPALALVLAL---GLLLAGLLLPLLAARLGRRAGRRLAAARAalraRLTDLLQGAAELAAYGALDRALARLDA-AEARL 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  78 CKAEE-LGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGAR 156
Cdd:COG4987  229 AAAQRrLARLSALAQALLQLAAGLAVVAVLWLAAPLVAAGALSGPLLALLVLAALALFEALAPLPAAAQHLGRVRAAARR 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 157 VFEYMALSPVIPLTGGYCIPNKDirGSITFQNVTFSYPCRPGfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFY 236
Cdd:COG4987  309 LNELLDAPPAVTEPAEPAPAPGG--PSLELEDVSFRYPGAGR-PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFL 385

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 237 DPEAGSVTLDGHDLRTLNPSWLRgQVIGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTV 316
Cdd:COG4987  386 DPQSGSITLGGVDLRDLDEDDLR-RRIAVVPQRPHLFDTTLRENLRLARPDATDEELWAALERVGLGDWLAALPDGLDTW 464

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 317 VGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMAN 396
Cdd:COG4987  465 LGEGGRRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERMDRILVLED 544

                        410       420
                 ....*....|....*....|....*
gi 755511082 397 GQVCEAGTHEELLKKGGLYSELIRR 421
Cdd:COG4987  545 GRIVEQGTHEELLAQNGRYRQLYQR 569

PRK13657

glucan ABC transporter ATP-binding protein/ permease;

5-435

7.29e-97

glucan ABC transporter ATP-binding protein/ permease;

Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 302.65 E-value: 7.29e-97

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   5 RLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAmekreeeRYQAELESCCCKAEELG 84
Cdd:PRK13657 157 RLSLVLVVLGIVYTLITTLVMRKTKDGQAAVEEHYHDLFAHVSDAIGNVSVVQSYN-------RIEAETQALRDIADNLL 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  85 RG-------IALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFL-VASQTVQRsmasLSVLFGQVVRGLSAGAR 156
Cdd:PRK13657 230 AAqmpvlswWALASVLNRAASTITMLAILVLGAALVQKGQLRVGEVVAFVgFATLLIGR----LDQVVAFINQVFMAAPK 305

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 157 VFEYMALSPVIPLTG--GYCIPNKDIRGSITFQNVTFSYP-CRPGfnvLKDFTLKLPSGKIVALVGQSGGGKTTVASLLE 233
Cdd:PRK13657 306 LEEFFEVEDAVPDVRdpPGAIDLGRVKGAVEFDDVSFSYDnSRQG---VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQ 382

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 234 RFYDPEAGSVTLDGHDLRTLNPSWLRgQVIGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGY 313
Cdd:PRK13657 383 RVFDPQSGRILIDGTDIRTVTRASLR-RNIAVVFQDAGLFNRSIEDNIRVGRPDATDEEMRAAAERAQAHDFIERKPDGY 461

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 314 STVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIV 393
Cdd:PRK13657 462 DTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNADRILV 541

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....
gi 755511082 394 MANGQVCEAGTHEELLKKGGLYSELIRRQ--TLDASLTSTPPAE 435
Cdd:PRK13657 542 FDNGRVVESGSFDELVARGGRFAALLRAQgmLQEDERRKQPAAE 585

ABCC_Hemolysin

cd03252

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

184-422

2.84e-95

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: 286.69 E-value: 2.84e-95

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYpcRP-GFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQV 262
Cdd:cd03252    1 ITFEHVRFRY--KPdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 263 iGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQP 342
Cdd:cd03252   79 -GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 343 TVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELIRRQ 422
Cdd:cd03252  158 RILIFDEATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENGLYAYLYQLQ 237

PRK11176

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

3-422

1.70e-94

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

Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 296.16 E-value: 1.70e-94

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   3 SPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYqaelESCCCKAEE 82
Cdd:PRK11176 164 SWQLSLILIVIAPIVSIAIRVVSKRFRNISKNMQNTMGQVTTSAEQMLKGHKEVLIFGGQEVETKRF----DKVSNRMRQ 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  83 LGRGIALFQGLSN-----IAFNCMVLgTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 157
Cdd:PRK11176 240 QGMKMVSASSISDpiiqlIASLALAF-VLYAASFPSVMDTLTAGTITVVFSSMIALMRPLKSLTNVNAQFQRGMAACQTL 318

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 158 FEYMALSPVIPlTGGYCIpnKDIRGSITFQNVTFSYPCR--PGfnvLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERF 235
Cdd:PRK11176 319 FAILDLEQEKD-EGKRVI--ERAKGDIEFRNVTFTYPGKevPA---LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRF 392

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 236 YDPEAGSVTLDGHDLRTLNPSWLRGQViGFISQEPVLFATTIMENIRFGKLDA-SDEEVYTAAREANAHEFISSFPDGYS 314
Cdd:PRK11176 393 YDIDEGEILLDGHDLRDYTLASLRNQV-ALVSQNVHLFNDTIANNIAYARTEQySREQIEEAARMAYAMDFINKMDNGLD 471

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 315 TVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVM 394
Cdd:PRK11176 472 TVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVV 551

                        410       420
                 ....*....|....*....|....*...
gi 755511082 395 ANGQVCEAGTHEELLKKGGLYSELIRRQ 422
Cdd:PRK11176 552 EDGEIVERGTHAELLAQNGVYAQLHKMQ 579

ABCC_TAP

cd03248

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

178-399

3.98e-91

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: 275.50 E-value: 3.98e-91

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 178 KDIRGSITFQNVTFSYPCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSW 257
Cdd:cd03248    6 DHLKGIVKFQNVTFAYPTRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKY 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 258 LRGQViGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARA 337
Cdd:cd03248   86 LHSKV-SLVGQEPVLFARSLQDNIAYGLQSCSFECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARA 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755511082 338 LIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQV 399
Cdd:cd03248  165 LIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226

ABC_6TM_ABCB8_like

cd18574

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette transporter subfamily B ...

1-157

8.92e-86

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: 264.41 E-value: 8.92e-86

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   1 MLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKA 80
Cdd:cd18574  139 LISPKLTLLLLVIVPVVVLVGTLYGSFLRKLSRRAQAQVAKATGVADEALGNIRTVRAFAMEDRELELYEEEVEKAAKLN 218

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755511082  81 EELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 157
Cdd:cd18574  219 EKLGLGIGIFQGLSNLALNGIVLGVLYYGGSLVSRGELTAGDLMSFLVATQTIQRSLAQLSVLFGQYVKGKSAGARV 295

ABCC_MRP_Like

cd03228

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

184-398

2.29e-83

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

Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 253.46 E-value: 2.29e-83

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPGFnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQvI 263
Cdd:cd03228    1 IEFKNVSFSYPGRPKP-VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-I 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEPVLFATTIMENIrfgkldasdeevytaareanahefissfpdgystvvgergttLSGGQKQRLAIARALIKQPT 343
Cdd:cd03228   79 AYVPQDPFLFSGTIRENI------------------------------------------LSGGQRQRIAIARALLRDPP 116

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755511082 344 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQ 398
Cdd:cd03228  117 ILILDEATSALDPETEALILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171

NHLM_micro_ABC1

TIGR03796

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

3-420

1.89e-78

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: 257.56 E-value: 1.89e-78

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082    3 SPRLTLmLAVVTPALMGVGTLMGSGLRK-LSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEER---YQAELESccc 78
Cdd:TIGR03796 292 DPVLTL-IGIAFAAINVLALQLVSRRRVdANRRLQQDAGKLTGVAISGLQSIETLKASGLESDFFSRwagYQAKLLN--- 367

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   79 KAEELGRGIALFQGLSNI--AFNCMVLgtLFIGGSLVAGQQLKGGDLmsflVASQTVqrsMASLS------VLFGQVVRG 150
Cdd:TIGR03796 368 AQQELGVLTQILGVLPTLltSLNSALI--LVVGGLRVMEGQLTIGML----VAFQSL---MSSFLepvnnlVGFGGTLQE 438

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  151 LSAGARVFEYMALSPVIPL------TGGYCIPNKDIRGSITFQNVTFSYPcRPGFNVLKDFTLKLPSGKIVALVGQSGGG 224
Cdd:TIGR03796 439 LEGDLNRLDDVLRNPVDPLleepegSAATSEPPRRLSGYVELRNITFGYS-PLEPPLIENFSLTLQPGQRVALVGGSGSG 517

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  225 KTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQViGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHE 304
Cdd:TIGR03796 518 KSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSV-AMVDQDIFLFEGTVRDNLTLWDPTIPDADLVRACKDAAIHD 596

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  305 FISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRAsaGRTVLVIAHRLST 384
Cdd:TIGR03796 597 VITSRPGGYDAELAEGGANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIIDDNLRRR--GCTCIIVAHRLST 674

                         410       420       430
                  ....*....|....*....|....*....|....*.
gi 755511082  385 VRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELIR 420
Cdd:TIGR03796 675 IRDCDEIIVLERGKVVQRGTHEELWAVGGAYARLIR 710

ArpD

COG4618

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

1-411

8.53e-73

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: 238.88 E-value: 8.53e-73

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   1 MLSPRLTLMlavvtpALMGVGTLMGSGL------RKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAEle 74
Cdd:COG4618  152 LFHPLLGLL------ALVGALVLVALALlnerltRKPLKEANEAAIRANAFAEAALRNAEVIEAMGMLPALRRRWQRA-- 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  75 scccKAEELGRGI------ALFQGLS---NIAFNCMVLGTlfiGGSLVAGQQLKGGDLM--SFLVAsqtvqRSMASLSVL 143
Cdd:COG4618  224 ----NARALALQArasdraGGFSALSkflRLLLQSAVLGL---GAYLVIQGEITPGAMIaaSILMG-----RALAPIEQA 291

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 144 FG---QVVRGLSAGARVFEYMALSPVIPLTggycIPNKDIRGSITFQNVTFSYPC--RPgfnVLKDFTLKLPSGKIVALV 218
Cdd:COG4618  292 IGgwkQFVSARQAYRRLNELLAAVPAEPER----MPLPRPKGRLSVENLTVVPPGskRP---ILRGVSFSLEPGEVLGVI 364

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 219 GQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLrGQVIGFISQEPVLFATTIMENI-RFGklDASDEEVYTAA 297
Cdd:COG4618  365 GPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL-GRHIGYLPQDVELFDGTIAENIaRFG--DADPEKVVAAA 441

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 298 REANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRA-SAGRTVL 376
Cdd:COG4618  442 KLAGVHEMILRLPDGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVV 521

                        410       420       430
                 ....*....|....*....|....*....|....*
gi 755511082 377 VIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKK 411
Cdd:COG4618  522 VITHRPSLLAAVDKLLVLRDGRVQAFGPRDEVLAR 556

NHLM_micro_ABC2

TIGR03797

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

3-422

1.96e-71

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: 238.32 E-value: 1.96e-71

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082    3 SPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERY------QAELESc 76
Cdd:TIGR03797 274 SWKLALVAVALALVAIAVTLVLGLLQVRKERRLLELSGKISGLTVQLINGISKLRVAGAENRAFARWaklfsrQRKLEL- 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   77 ccKAEELGRGIALFqglsNIAFNCMVLGTLF-IGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVrglsagA 155
Cdd:TIGR03797 353 --SAQRIENLLTVF----NAVLPVLTSAALFaAAISLLGGAGLSLGSFLAFNTAFGSFSGAVTQLSNTLISIL------A 420

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  156 RVFEYMALSPV---IPLTGGYCIPNKDIRGSITFQNVTFSYPCRpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLL 232
Cdd:TIGR03797 421 VIPLWERAKPIleaLPEVDEAKTDPGKLSGAIEVDRVTFRYRPD-GPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLL 499

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  233 ERFYDPEAGSVTLDGHDLRTLNPSWLRGQvIGFISQEPVLFATTIMENIrFGKLDASDEEVYTAAREANAHEFISSFPDG 312
Cdd:TIGR03797 500 LGFETPESGSVFYDGQDLAGLDVQAVRRQ-LGVVLQNGRLMSGSIFENI-AGGAPLTLDEAWEAARMAGLAEDIRAMPMG 577

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  313 YSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRtvLVIAHRLSTVRAAHSII 392
Cdd:TIGR03797 578 MHTVISEGGGTLSGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKVTR--IVIAHRLSTIRNADRIY 655

                         410       420       430
                  ....*....|....*....|....*....|
gi 755511082  393 VMANGQVCEAGTHEELLKKGGLYSELIRRQ 422
Cdd:TIGR03797 656 VLDAGRVVQQGTYDELMAREGLFAQLARRQ 685

ABCC_bacteriocin_exporters

cd03245

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

182-399

2.09e-71

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: 224.78 E-value: 2.09e-71

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 182 GSITFQNVTFSYPCRPGfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgQ 261
Cdd:cd03245    1 GRIEFRNVSFSYPNQEI-PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLR-R 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 262 VIGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQ 341
Cdd:cd03245   79 NIGYVPQDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPNGLDLQIGERGRGLSGGQRQAVALARALLND 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755511082 342 PTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQV 399
Cdd:cd03245  159 PPILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLDLVDRIIVMDSGRI 216

CydD

TIGR02857

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

150-394

1.27e-68

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: 227.17 E-value: 1.27e-68

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  150 GLSAGARVFEYMALSPViPLTGGYCIPNKDIRgSITFQNVTFSYPCRPgfNVLKDFTLKLPSGKIVALVGQSGGGKTTVA 229
Cdd:TIGR02857 290 GVAAAEALFAVLDAAPR-PLAGKAPVTAAPAS-SLEFSGVSVAYPGRR--PALRPVSFTVPPGERVALVGPSGAGKSTLL 365

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  230 SLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQvIGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSF 309
Cdd:TIGR02857 366 NLLLGFVDPTEGSIAVNGVPLADADADSWRDQ-IAWVPQHPFLFAGTIAENIRLARPDASDAEIREALERAGLDEFVAAL 444

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  310 PDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAH 389
Cdd:TIGR02857 445 PQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALAALAD 524


                  ....*
gi 755511082  390 SIIVM 394
Cdd:TIGR02857 525 RIVVL 529

PRK10789

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

46-436

1.77e-68

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

Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 227.67 E-value: 1.77e-68

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  46 ADEALGNVRTVRAFAMEKREEERYQAELESCCCKAEELGRGIALFQ-------GLSNIafncmvlgtLFIGGS--LVAGQ 116
Cdd:PRK10789 179 TQESLTSIRMIKAFGLEDRQSALFAADAEDTGKKNMRVARIDARFDptiyiaiGMANL---------LAIGGGswMVVNG 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 117 QLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARVFEYMALSPVIpLTGGYCIPNKdiRGSITFQNVTFSYP-- 194
Cdd:PRK10789 250 SLTLGQLTSFVMYLGLMIWPMLALAWMFNIVERGSAAYSRIRAMLAEAPVV-KDGSEPVPEG--RGELDVNIRQFTYPqt 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 195 CRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQvIGFISQEPVLFA 274
Cdd:PRK10789 327 DHP---ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSR-LAVVSQTPFLFS 402

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 275 TTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSAL 354
Cdd:PRK10789 403 DTVANNIALGRPDATQQEIEHVARLASVHDDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAV 482

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 355 DAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELIRRQTLDASLTSTPPA 434
Cdd:PRK10789 483 DGRTEHQILHNLRQWGEGRTVIISAHRLSALTEASEILVMQHGHIAQRGNHDQLAQQSGWYRDMYRYQQLEAALDDAPEI 562


                 ..
gi 755511082 435 EK 436
Cdd:PRK10789 563 RE 564

PRK10790

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

132-435

2.83e-68

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

Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 228.06 E-value: 2.83e-68

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 132 TVQRSMASLSVLfgqvvrglsAGARVFEYMAlSP-------VIPLTGGycipnkdirgSITFQNVTFSYpcRPGFNVLKD 204
Cdd:PRK10790 302 TTQQSMLQQAVV---------AGERVFELMD-GPrqqygndDRPLQSG----------RIDIDNVSFAY--RDDNLVLQN 359

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 205 FTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgQVIGFISQEPVLFATTIMENIRFG 284
Cdd:PRK10790 360 INLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLR-QGVAMVQQDPVVLADTFLANVTLG 438

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 285 KlDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQE 364
Cdd:PRK10790 439 R-DISEEQVWQALETVQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATANIDSGTEQAIQQ 517

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755511082 365 ALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELIRRQTLDASLTSTPPAE 435
Cdd:PRK10790 518 ALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAAQGRYWQMYQLQLAGEELAASVREE 588

ABCC_MRP_domain2

cd03244

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

182-404

3.65e-68

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.

Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 216.21 E-value: 3.65e-68

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 182 GSITFQNVTFSYpcRPGFN-VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRG 260
Cdd:cd03244    1 GDIEFKNVSLRY--RPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 261 QvIGFISQEPVLFATTIMENIR-FGKldASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALI 339
Cdd:cd03244   79 R-ISIIPQDPVLFSGTIRSNLDpFGE--YSDEELWQALERVGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALL 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755511082 340 KQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGT 404
Cdd:cd03244  156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVVEFDS 220

type_I_sec_PrtD

TIGR01842

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

1-411

8.04e-66

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: 220.30 E-value: 8.04e-66

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082    1 MLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKA 80
Cdd:TIGR01842 138 LLHPWIGILALGGAVVLVGLALLNNRATKKPLKEATEASIRANNLADSALRNAEVIEAMGMMGNLTKRWGRFHSKYLSAQ 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   81 EELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGdlmSFLVASQTVQRSMASLSVLFG---QVVRGLSAGARV 157
Cdd:TIGR01842 218 SAASDRAGMLSNLSKYFRIVLQSLVLGLGAYLAIDGEITPG---MMIAGSILVGRALAPIDGAIGgwkQFSGARQAYKRL 294

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  158 FEYMALSP----VIPLtggyciPNKdiRGSITFQNVTFSYPcRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLE 233
Cdd:TIGR01842 295 NELLANYPsrdpAMPL------PEP--EGHLSVENVTIVPP-GGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIV 365

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  234 RFYDPEAGSVTLDGHDLRTLNPSWLrGQVIGFISQEPVLFATTIMENI-RFGKlDASDEEVYTAAREANAHEFISSFPDG 312
Cdd:TIGR01842 366 GIWPPTSGSVRLDGADLKQWDRETF-GKHIGYLPQDVELFPGTVAENIaRFGE-NADPEKIIEAAKLAGVHELILRLPDG 443

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  313 YSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA-GRTVLVIAHRLSTVRAAHSI 391
Cdd:TIGR01842 444 YDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKArGITVVVITHRPSLLGCVDKI 523

                         410       420
                  ....*....|....*....|
gi 755511082  392 IVMANGQVCEAGTHEELLKK 411
Cdd:TIGR01842 524 LVLQDGRIARFGERDEVLAK 543

PRK11174

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

204-425

2.53e-64

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

Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 217.41 E-value: 2.53e-64

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 204 DFTLklPSGKIVALVGQSGGGKTTVASLLERFYdPEAGSVTLDGHDLRTLNPSWLRGQvIGFISQEPVLFATTIMENIRF 283
Cdd:PRK11174 370 NFTL--PAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKH-LSWVGQNPQLPHGTLRDNVLL 445

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 284 GKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQ 363
Cdd:PRK11174 446 GNPDASDEQLQQALENAWVSEFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVM 525

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755511082 364 EALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELIRRQTLD 425
Cdd:PRK11174 526 QALNAASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGGLFATLLAHRQEE 587

CydC

TIGR02868

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

84-382

7.90e-61

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: 206.83 E-value: 7.90e-61

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   84 GRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARVFEYMAL 163
Cdd:TIGR02868 234 AAATALGAALTLLAAGLAVLGALWAGGPAVADGRLAPVTLAVLVLLPLAAFEAFAALPAAAQQLTRVRAAAERIVEVLDA 313

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  164 SP-----VIPLTGGYciPNKDIRgsITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDP 238
Cdd:TIGR02868 314 AGpvaegSAPAAGAV--GLGKPT--LELRDLSAGYP--GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDP 387

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  239 EAGSVTLDGHDLRTLNPSWLRgQVIGFISQEPVLFATTIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVG 318
Cdd:TIGR02868 388 LQGEVTLDGVPVSSLDQDEVR-RRVSVCAQDAHLFDTTVRENLRLARPDATDEELWAALERVGLADWLRALPDGLDTVLG 466

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755511082  319 ERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRL 382
Cdd:TIGR02868 467 EGGARLSGGERQRLALARALLADAPILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530

PRK11160

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

66-422

5.60e-60

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

Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 205.44 E-value: 5.60e-60

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  66 EERYQAELEscccKAEEL----GRGIALFQGLSN---IAFNCM-VLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSM 137
Cdd:PRK11160 219 EDRYRQQLE----QTEQQwlaaQRRQANLTGLSQalmILANGLtVVLMLWLAAGGVGGNAQPGALIALFVFAALAAFEAL 294

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 138 ASLSVLF---GQVVrglSAGARVFEYMALSPVIPLTGGYCIPNKdiRGSITFQNVTFSYPCRPgFNVLKDFTLKLPSGKI 214
Cdd:PRK11160 295 MPVAGAFqhlGQVI---ASARRINEITEQKPEVTFPTTSTAAAD--QVSLTLNNVSFTYPDQP-QPVLKGLSLQIKAGEK 368

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 215 VALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgQVIGFISQEPVLFATTIMENIRFGKLDASDEEVY 294
Cdd:PRK11160 369 VALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR-QAISVVSQRVHLFSATLRDNLLLAAPNASDEALI 447

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 295 TAAREANAHEFISSfPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRT 374
Cdd:PRK11160 448 EVLQQVGLEKLLED-DKGLNAWLGEGGRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKT 526

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 755511082 375 VLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELIRRQ 422
Cdd:PRK11160 527 VLMITHRLTGLEQFDRICVMDNGQIIEQGTHQELLAQQGRYYQLKQRL 574

bacteriocin_ABC

TIGR01193

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

182-419

7.65e-60

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: 207.67 E-value: 7.65e-60

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  182 GSITFQNVTFSYpcrpGF--NVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLR 259
Cdd:TIGR01193 472 GDIVINDVSYSY----GYgsNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLR 547

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  260 gQVIGFISQEPVLFATTIMENIRFG-KLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARAL 338
Cdd:TIGR01193 548 -QFINYLPQEPYIFSGSILENLLLGaKENVSQDEIWAACEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARAL 626

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  339 IKQPTVLILDEATSALDAESERVVQEALDRASAgRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSEL 418
Cdd:TIGR01193 627 LTDSKVLILDESTSNLDTITEKKIVNNLLNLQD-KTIIFVAHRLSVAKQSDKIIVLDHGKIIEQGSHDELLDRNGFYASL 705


                  .
gi 755511082  419 I 419
Cdd:TIGR01193 706 I 706

PTZ00265

multidrug resistance protein (mdr1); Provisional

5-446

4.02e-57

multidrug resistance protein (mdr1); Provisional

Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 203.72 E-value: 4.02e-57

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082    5 RLTLMLAVVTPALMGVGTLMGSGLrKLSRQCQEQIARAT-GVADEALGNVRTVRAFAMEKREEERYQAElESCCCK---- 79
Cdd:PTZ00265  198 RLTLCITCVFPLIYICGVICNKKV-KINKKTSLLYNNNTmSIIEEALVGIRTVVSYCGEKTILKKFNLS-EKLYSKyilk 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   80 ---AEELGrgIALFQG--LSNIAFNcMVLGTLFIGGSLVAGQ---QLKGGDLMSFLVAsqtVQRSMASLSVLFGQV---V 148
Cdd:PTZ00265  276 anfMESLH--IGMINGfiLASYAFG-FWYGTRIIISDLSNQQpnnDFHGGSVISILLG---VLISMFMLTIILPNIteyM 349

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  149 RGLSAGARVFEYMALSPVIPLTG-GYCIPnkDIRgSITFQNVTFSYPCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTT 227
Cdd:PTZ00265  350 KSLEATNSLYEIINRKPLVENNDdGKKLK--DIK-KIQFKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKST 426

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  228 VASLLERFYDPEAGSVTL-DGHDLRTLNPSWLRGQvIGFISQEPVLFATTIMENIRFG-----KLDA------------- 288
Cdd:PTZ00265  427 ILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSK-IGVVSQDPLLFSNSIKNNIKYSlyslkDLEAlsnyynedgndsq 505

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  289 ---------------------------------------SDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQK 329
Cdd:PTZ00265  506 enknkrnscrakcagdlndmsnttdsneliemrknyqtiKDSEVVDVSKKVLIHDFVSALPDKYETLVGSNASKLSGGQK 585

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  330 QRLAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRAAHSIIVMANGQ--------- 398
Cdd:PTZ00265  586 QRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINnlKGNENRITIIIAHRLSTIRYANTIFVLSNRErgstvdvdi 665

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  399 --------------------------------------VCEAGTHEELLK-KGGLYSELIRRQTLDASLTSTPPAEKPED 439
Cdd:PTZ00265  666 igedptkdnkennnknnkddnnnnnnnnnnkinnagsyIIEQGTHDALMKnKNGIYYTMINNQKVSSKKSSNNDNDKDSD 745


                  ....*..
gi 755511082  440 PKSCQSK 446
Cdd:PTZ00265  746 MKSSAYK 752

PTZ00265

multidrug resistance protein (mdr1); Provisional

171-420

3.64e-56

multidrug resistance protein (mdr1); Provisional

Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 201.03 E-value: 3.64e-56

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  171 GGYCIPNK-DIRGSITFQNVTFSYPCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYD------------ 237
Cdd:PTZ00265 1152 GGIRIKNKnDIKGKIEIMDVNFRYISRPNVPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDlkndhhivfkne 1231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  238 ------------------------------------------PEAGSVTLDGHDLRTLNPSWLRgQVIGFISQEPVLFAT 275
Cdd:PTZ00265 1232 htndmtneqdyqgdeeqnvgmknvnefsltkeggsgedstvfKNSGKILLDGVDICDYNLKDLR-NLFSIVSQEPMLFNM 1310

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  276 TIMENIRFGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD 355
Cdd:PTZ00265 1311 SIYENIKFGKEDATREDVKRACKFAAIDEFIESLPNKYDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLD 1390

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755511082  356 AESERVVQEAL--DRASAGRTVLVIAHRLSTVRAAHSIIVMAN----GQVCEA-GTHEELLK-KGGLYSELIR 420
Cdd:PTZ00265 1391 SNSEKLIEKTIvdIKDKADKTIITIAHRIASIKRSDKIVVFNNpdrtGSFVQAhGTHEELLSvQDGVYKKYVK 1463

EcfA2

COG1122

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

184-411

1.01e-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: 168.66 E-value: 1.01e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVi 263
Cdd:COG1122    1 IELENLSFSYP--GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKV- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEPV--LFATTIMENIRFG--KLDASDEEVYTAAREA----NAHEFISSFPDgystvvgergtTLSGGQKQRLAIA 335
Cdd:COG1122   78 GLVFQNPDdqLFAPTVEEDVAFGpeNLGLPREEIRERVEEAlelvGLEHLADRPPH-----------ELSGGQKQRVAIA 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755511082 336 RALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEELLKK 411
Cdd:COG1122  147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPREVFSD 224

ABC_PstB_phosphate_transporter

cd03260

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

184-408

6.02e-47

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: 161.58 E-value: 6.02e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYD-----PEAGSVTLDGHDLRTL--NPS 256
Cdd:cd03260    1 IELRDLNVYYG---DKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLDGKDIYDLdvDVL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 257 WLRGQViGFISQEPVLFATTIMENIRFG-KL------DASDEEVYTAAREANAHEFISSFPDGYStvvgergttLSGGQK 329
Cdd:cd03260   78 ELRRRV-GMVFQKPNPFPGSIYDNVAYGlRLhgiklkEELDERVEEALRKAALWDEVKDRLHALG---------LSGGQQ 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 330 QRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEEL 408
Cdd:cd03260  148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAaRVADRTAFLLNGRLVEFGPTEQI 227

CcmA

COG1131

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

184-411

1.52e-46

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

Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 160.61 E-value: 1.52e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgqVI 263
Cdd:COG1131    1 IEVRGLTKRYG---DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRR--RI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEPVLFAT-TIMENIRF-GKL-DASDEEvytaaREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIK 340
Cdd:COG1131   76 GYVPQEPALYPDlTVRENLRFfARLyGLPRKE-----ARERIDELLELF--GLTDAADRKVGTLSGGMKQRLGLALALLH 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755511082 341 QPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEELLKK 411
Cdd:COG1131  149 DPELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDELKAR 221

FetA

COG4619

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

184-399

1.70e-46

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

Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 159.60 E-value: 1.70e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVi 263
Cdd:COG4619    1 LELEGLSFRVGGKP---ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQV- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEPVLFATTIMENIRFGKLDASDEevytaAREANAHEFISSFpdGYSTVVGERGTT-LSGGQKQRLAIARALIKQP 342
Cdd:COG4619   77 AYVPQEPALWGGTVRDNLPFPFQLRERK-----FDRERALELLERL--GLPPDILDKPVErLSGGERQRLALIRALLLQP 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755511082 343 TVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAH--RLSTvRAAHSIIVMANGQV 399
Cdd:COG4619  150 DVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHdpEQIE-RVADRVLTLEAGRL 209

ABCC_Protease_Secretion

cd03246

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

184-399

2.12e-45

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: 155.45 E-value: 2.12e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYP--CRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQ 261
Cdd:cd03246    1 LEVENVSFRYPgaEPP---VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 262 vIGFISQEPVLFATTIMENIrfgkldasdeevytaareanahefissfpdgystvvgergttLSGGQKQRLAIARALIKQ 341
Cdd:cd03246   78 -VGYLPQDDELFSGSIAENI------------------------------------------LSGGQRQRLGLARALYGN 114

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755511082 342 PTVLILDEATSALDAESERVVQEALDRAS-AGRTVLVIAHRLSTVRAAHSIIVMANGQV 399
Cdd:cd03246  115 PRILVLDEPNSHLDVEGERALNQAIAALKaAGATRIVIAHRPETLASADRILVLEDGRV 173

GsiA

COG1123

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

184-409

6.41e-45

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: 163.54 E-value: 6.41e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPG--FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLR-- 259
Cdd:COG1123  261 LEVRNLSKRYPVRGKggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRel 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 260 GQVIGFISQEPV--LF-----ATTIMENIR-FGKLDASD--EEVYTAAREAN-AHEFISSFPDgystvvgergtTLSGGQ 328
Cdd:COG1123  341 RRRVQMVFQDPYssLNprmtvGDIIAEPLRlHGLLSRAErrERVAELLERVGlPPDLADRYPH-----------ELSGGQ 409

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 329 KQRLAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTH 405
Cdd:COG1123  410 RQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRdlQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPT 489


                 ....
gi 755511082 406 EELL 409
Cdd:COG1123  490 EEVF 493

ABCC_cytochrome_bd

cd03247

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

184-403

8.91e-45

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: 154.01 E-value: 8.91e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSwlRGQVI 263
Cdd:cd03247    1 LSINNVSFSYP-EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA--LSSLI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEPVLFATTIMENIrfgkldasdeevytaareanahefissfpdgystvvgerGTTLSGGQKQRLAIARALIKQPT 343
Cdd:cd03247   78 SVLNQRPYLFDTTLRNNL---------------------------------------GRRFSGGERQRLALARILLQDAP 118

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 344 VLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAG 403
Cdd:cd03247  119 IVLLDEPTVGLDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHMDKILFLENGKIIMQG 178

ABCC_NFT1

cd03369

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

182-404

2.47e-44

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: 153.72 E-value: 2.47e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 182 GSITFQNVTFSY-PCRPgfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRG 260
Cdd:cd03369    5 GEIEVENLSVRYaPDLP--PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 261 QvIGFISQEPVLFATTIMENI-RFGKLdaSDEEVYTAAReanahefissfpdgystvVGERGTTLSGGQKQRLAIARALI 339
Cdd:cd03369   83 S-LTIIPQDPTLFSGTIRSNLdPFDEY--SDEEIYGALR------------------VSEGGLNLSQGQRQLLCLARALL 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755511082 340 KQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGT 404
Cdd:cd03369  142 KRPRVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIIDYDKILVMDAGEVKEYDH 206

LolD

COG1136

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

184-399

7.40e-44

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

Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 153.28 E-value: 7.40e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPG-FNVLKDFTLKLPSGKIVALVGQSGGGKTT---VASLLERfydPEAGSVTLDGHDLRTLNP---S 256
Cdd:COG1136    5 LELRNLTKSYGTGEGeVTALRGVSLSIEAGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVLIDGQDISSLSErelA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 257 WLRGQVIGFISQEPVLFAT-TIMENI----RFGKLDAsdeevytAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQR 331
Cdd:COG1136   82 RLRRRHIGFVFQFFNLLPElTALENValplLLAGVSR-------KERRERARELLERV--GLGDRLDHRPSQLSGGQQQR 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 332 LAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRAAHSIIVMANGQV 399
Cdd:COG1136  153 VAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRElnRELGTTIVMVTHDPELAARADRVIRLRDGRI 222

ABCC_MRP_domain1

cd03250

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

184-398

1.46e-43

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: 151.85 E-value: 1.46e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPGFN--VLKDFTLKLPSGKIVALVGQSGGGKTTVASLL--ErfYDPEAGSVTLDGHdlrtlnpswlr 259
Cdd:cd03250    1 ISVEDASFTWDSGEQETsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgE--LEKLSGSVSVPGS----------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 260 gqvIGFISQEPVLFATTIMENIRFGKldASDEEVYTAAREANA-HEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARAL 338
Cdd:cd03250   68 ---IAYVSQEPWIQNGTIRENILFGK--PFDEERYEKVIKACAlEPDLEILPDGDLTEIGEKGINLSGGQKQRISLARAV 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755511082 339 IKQPTVLILDEATSALDAES-----ERVVQEALdraSAGRTVLVIAHRLSTVRAAHSIIVMANGQ 398
Cdd:cd03250  143 YSDADIYLLDDPLSAVDAHVgrhifENCILGLL---LNNKTRILVTHQLQLLPHADQIVVLDNGR 204

ABC_cobalt_CbiO_domain1

cd03225

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

186-398

2.31e-43

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: 151.47 E-value: 2.31e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 186 FQNVTFSYPcRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPsWLRGQVIGF 265
Cdd:cd03225    2 LKNLSFSYP-DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSL-KELRRKVGL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 266 ISQEP--VLFATTIMENIRFG--KLDASDEEVYTAAREANAHEFISSFPDgystvvgERGTTLSGGQKQRLAIARALIKQ 341
Cdd:cd03225   80 VFQNPddQFFGPTVEEEVAFGleNLGLPEEEIEERVEEALELVGLEGLRD-------RSPFTLSGGQKQRVAIAGVLAMD 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755511082 342 PTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQ 398
Cdd:cd03225  153 PDILLLDEPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLElADRVIVLEDGK 211

ABC_tran

pfam00005

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

202-352

4.88e-43

Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 148.56 E-value: 4.88e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  202 LKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQvIGFISQEPVLF-ATTIMEN 280
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKE-IGYVFQDPQLFpRLTVREN 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755511082  281 IRFGkldASDEEVYTAAREANAHEFISSF--PDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATS 352
Cdd:pfam00005  80 LRLG---LLLKGLSKREKDARAEEALEKLglGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150

ABC_6TM_TAP_ABCB8_10_like

cd18557

Six-transmembrane helical domain (6-TMD) of the ABC transporter TAP, ABCB8 and ABCB10; This ...

1-157

7.32e-43

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: 152.71 E-value: 7.32e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   1 MLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKA 80
Cdd:cd18557  133 ILSWKLTLVLLLVIPLLLIASKIYGRYIRKLSKEVQDALAKAGQVAEESLSNIRTVRSFSAEEKEIRRYSEALDRSYRLA 212

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755511082  81 EELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 157
Cdd:cd18557  213 RKKALANALFQGITSLLIYLSLLLVLWYGGYLVLSGQLTVGELTSFILYTIMVASSVGGLSSLLADIMKALGASERV 289

NatA

COG4555

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

184-413

1.96e-42

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

Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 150.01 E-value: 1.96e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTlNPSWLRGQvI 263
Cdd:COG4555    2 IEVENLSKKYGKVP---ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQ-I 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEPVLFAT-TIMENIR-FGKL-DASDEEVYTAAREAnAHEF-ISSFPDgystvvgERGTTLSGGQKQRLAIARALI 339
Cdd:COG4555   77 GVLPDERGLYDRlTVRENIRyFAELyGLFDEELKKRIEEL-IELLgLEEFLD-------RRVGELSTGMKKKVALARALV 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755511082 340 KQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEELLKKGG 413
Cdd:COG4555  149 HDPKVLLLDEPTNGLDVMARRLLREILRAlKKEGKTVLFSSHIMQEVeALCDRVVILHKGKVVAQGSLDELREEIG 224

GsiA

COG1123

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

184-437

3.03e-42

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: 156.22 E-value: 3.03e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPgFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEA---GSVTLDGHDLRTLNPsWLRG 260
Cdd:COG1123    5 LEVRDLSVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSE-ALRG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 261 QVIGFISQEP--VLFATTIMENIRFG--KLDASDEEVYTAAREANAHEFISSFPDGYSTvvgergtTLSGGQKQRLAIAR 336
Cdd:COG1123   83 RRIGMVFQDPmtQLNPVTVGDQIAEAleNLGLSRAEARARVLELLEAVGLERRLDRYPH-------QLSGGQRQRVAIAM 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 337 ALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEELLKKGG 413
Cdd:COG1123  156 ALALDPDLLIADEPTTALDVTTQAEILDLLRelQRERGTTVLLITHDLGVVaEIADRVVVMDDGRIVEDGPPEEILAAPQ 235

                        250       260
                 ....*....|....*....|....
gi 755511082 414 LYSELIRRQTLDASLTSTPPAEKP 437
Cdd:COG1123  236 ALAAVPRLGAARGRAAPAAAAAEP 259

ABC_NikE_OppD_transporters

cd03257

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

184-403

4.56e-41

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: 145.73 E-value: 4.56e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPGFN-VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWL--RG 260
Cdd:cd03257    2 LEVKNLSVSFPTGGGSVkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRkiRR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 261 QVIGFISQEPVL-------FATTIMENIRFGKLDASDEEVYTAAREA-----NAHEFISSFPDgystvvgergtTLSGGQ 328
Cdd:cd03257   82 KEIQMVFQDPMSslnprmtIGEQIAEPLRIHGKLSKKEARKEAVLLLlvgvgLPEEVLNRYPH-----------ELSGGQ 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755511082 329 KQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAG 403
Cdd:cd03257  151 RQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEelGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228

ABC_MetN_methionine_transporter

cd03258

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

184-411

9.91e-41

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: 145.03 E-value: 9.91e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPG-FNVLKDFTLKLPSGKIVALVGQSGGGKTTVA---SLLERfydPEAGSVTLDGHDLRTLNPSWLR 259
Cdd:cd03258    2 IELKNVSKVFGDTGGkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIrciNGLER---PTSGSVLVDGTDLTLLSGKELR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 260 G--QVIGFISQEPVLFAT-TIMENIRFG-KLDASDEevytAAREANAHEFI-----SSFPDGYSTvvgergtTLSGGQKQ 330
Cdd:cd03258   79 KarRRIGMIFQHFNLLSSrTVFENVALPlEIAGVPK----AEIEERVLELLelvglEDKADAYPA-------QLSGGQKQ 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 331 RLAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEE 407
Cdd:cd03258  148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDinRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEGTVEE 227


                 ....
gi 755511082 408 LLKK 411
Cdd:cd03258  228 VFAN 231

FepC

COG1120

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

184-421

1.63e-40

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];

Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 145.19 E-value: 1.63e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgQVI 263
Cdd:COG1120    2 LEAENLSVGYGGRP---VLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA-RRI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEPVL-FATTIMENI---------RFGKLDASDEE-VYTAAREANAHEFIssfpdgystvvgERG-TTLSGGQKQR 331
Cdd:COG1120   78 AYVPQEPPApFGLTVRELValgryphlgLFGRPSAEDREaVEEALERTGLEHLA------------DRPvDELSGGERQR 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 332 LAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLS-TVRAAHSIIVMANGQVCEAGTHEEL 408
Cdd:COG1120  146 VLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRlaRERGRTVVMVLHDLNlAARYADRLVLLKDGRIVAQGPPEEV 225

                        250
                 ....*....|...
gi 755511082 409 LKkgglySELIRR 421
Cdd:COG1120  226 LT-----PELLEE 233

ABC_MJ0796_LolCDE_FtsE

cd03255

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

184-399

2.54e-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: 143.40 E-value: 2.54e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPG-FNVLKDFTLKLPSGKIVALVGQSGGGKTT---VASLLERfydPEAGSVTLDGHDLRTLNPSWL- 258
Cdd:cd03255    1 IELKNLSKTYGGGGEkVQALKGVSLSIEKGEFVAIVGPSGSGKSTllnILGGLDR---PTSGEVRVDGTDISKLSEKELa 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 259 --RGQVIGFISQEPVLFAT-TIMENIRFGKLDASDEevyTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIA 335
Cdd:cd03255   78 afRRRHIGFVFQSFNLLPDlTALENVELPLLLAGVP---KKERRERAEELLERV--GLGDRLNHYPSELSGGQQQRVAIA 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755511082 336 RALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRAAHSIIVMANGQV 399
Cdd:cd03255  153 RALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218

MRP_assoc_pro

TIGR00957

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

181-428

4.82e-40

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]

Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 153.56 E-value: 4.82e-40

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   181 RGSITFQNVTFSYpcRPGFN-VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLR 259
Cdd:TIGR00957 1282 RGRVEFRNYCLRY--REDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLR 1359

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   260 GQvIGFISQEPVLFATTIMENIR-FGKLdaSDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARAL 338
Cdd:TIGR00957 1360 FK-ITIIPQDPVLFSGSLRMNLDpFSQY--SDEEVWWALELAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARAL 1436

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   339 IKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSEL 418
Cdd:TIGR00957 1437 LRKTKILVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQRGIFYSM 1516

                          250
                   ....*....|
gi 755511082   419 IRrqtlDASL 428
Cdd:TIGR00957 1517 AK----DAGL 1522

ABC_ATPase

cd00267

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

185-398

2.08e-39

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

Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 139.30 E-value: 2.08e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 185 TFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQvIG 264
Cdd:cd00267    1 EIENLSFRYGGRT---ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRR-IG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 265 FISQepvlfattimenirfgkldasdeevytaareanahefissfpdgystvvgergttLSGGQKQRLAIARALIKQPTV 344
Cdd:cd00267   77 YVPQ-------------------------------------------------------LSGGQRQRVALARALLLNPDL 101

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755511082 345 LILDEATSALDAESERVVQEALDRASA-GRTVLVIAHRLSTV-RAAHSIIVMANGQ 398
Cdd:cd00267  102 LLLDEPTSGLDPASRERLLELLRELAEeGRTVIIVTHDPELAeLAADRVIVLKDGK 157

DppF

COG1124

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

184-410

2.25e-39

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: 141.86 E-value: 2.25e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYP-CRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQV 262
Cdd:COG1124    2 LEVRNLSVSYGqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 263 iGFISQEPVL-------FATTIMENIRFGKLDASDEEVYTAAREAN-AHEFISSFPDgystvvgergtTLSGGQKQRLAI 334
Cdd:COG1124   82 -QMVFQDPYAslhprhtVDRILAEPLRIHGLPDREERIAELLEQVGlPPSFLDRYPH-----------QLSGGQRQRVAI 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 335 ARALIKQPTVLILDEATSALDAeserVVQ-EALD-----RASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEE 407
Cdd:COG1124  150 ARALILEPELLLLDEPTSALDV----SVQaEILNllkdlREERGLTYLFVSHDLAVVaHLCDRVAVMQNGRIVEELTVAD 225


                 ...
gi 755511082 408 LLK 410
Cdd:COG1124  226 LLA 228

ABC_DR_subfamily_A

cd03230

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

184-399

3.59e-39

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: 139.07 E-value: 3.59e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTlNPSWLRGQvI 263
Cdd:cd03230    1 IEVRNLSKRYG---KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRR-I 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEPVLFAT-TIMENIRfgkldasdeevytaareanahefissfpdgystvvgergttLSGGQKQRLAIARALIKQP 342
Cdd:cd03230   76 GYLPEEPSLYENlTVRENLK-----------------------------------------LSGGMKQRLALAQALLHDP 114

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755511082 343 TVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV-RAAHSIIVMANGQV 399
Cdd:cd03230  115 ELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAeRLCDRVAILNNGRI 173

ECF_ATPase_1

TIGR04520

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...

184-425

7.24e-39

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]

Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 141.41 E-value: 7.24e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  184 ITFQNVTFSYPcrPGF-NVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDlrTLNPS--WLRG 260
Cdd:TIGR04520   1 IEVENVSFSYP--ESEkPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD--TLDEEnlWEIR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  261 QVIGFISQEP--VLFATTIMENIRFG--KLDASDEE----VYTAAREANAHEFISSFPdgystvvgergTTLSGGQKQRL 332
Cdd:TIGR04520  77 KKVGMVFQNPdnQFVGATVEDDVAFGleNLGVPREEmrkrVDEALKLVGMEDFRDREP-----------HLLSGGQKQRV 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  333 AIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLK 410
Cdd:TIGR04520 146 AIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRklNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPREIFS 225

                         250
                  ....*....|....*
gi 755511082  411 KGglysELIRRQTLD 425
Cdd:TIGR04520 226 QV----ELLKEIGLD 236

AbcC

COG1135

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

184-409

8.02e-39

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

Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 142.91 E-value: 8.02e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPG-FNVLKDFTLKLPSGKIVALVGQSGGGKTTVA---SLLERfydPEAGSVTLDGHDLRTLNPSWLR 259
Cdd:COG1135    2 IELENLSKTFPTKGGpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIrciNLLER---PTSGSVLVDGVDLTALSERELR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 260 G--QVIGFISQEPVLFAT-TIMENIRF----GKLDAsdeevytAAREANAHEFISsfpdgystVVG--ERGTT----LSG 326
Cdd:COG1135   79 AarRKIGMIFQHFNLLSSrTVAENVALpleiAGVPK-------AEIRKRVAELLE--------LVGlsDKADAypsqLSG 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 327 GQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAG 403
Cdd:COG1135  144 GQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQG 223


                 ....*.
gi 755511082 404 THEELL 409
Cdd:COG1135  224 PVLDVF 229

ABC_NrtD_SsuB_transporters

cd03293

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

184-396

8.83e-39

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: 139.53 E-value: 8.83e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYP-CRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSwlrgqv 262
Cdd:cd03293    1 LEVRNVSKTYGgGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD------ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 263 IGFISQEPVLFA-TTIMENIRFGkLDASDeeVYTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQ 341
Cdd:cd03293   75 RGYVFQQDALLPwLTVLDNVALG-LELQG--VPKAEARERAEELLELV--GLSGFENAYPHQLSGGMRQRVALARALAVD 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755511082 342 PTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLS-TVRAAHSIIVMAN 396
Cdd:cd03293  150 PDVLLLDEPFSALDALTREQLQEELLDiwRETGKTVLLVTHDIDeAVFLADRVVVLSA 207

TauB

COG1116

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

184-397

1.84e-37

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

Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 137.14 E-value: 1.84e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPG-FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSwlrgqv 262
Cdd:COG1116    8 LELRGVSKRFPTGGGgVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD------ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 263 IGFISQEPVLFA-TTIMENIRFGkLDASDeeVYTAAREANAHEFIS---------SFPDgystvvgergtTLSGGQKQRL 332
Cdd:COG1116   82 RGVVFQEPALLPwLTVLDNVALG-LELRG--VPKAERRERARELLElvglagfedAYPH-----------QLSGGMRQRV 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755511082 333 AIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAH------RLSTvRaahsIIVMANG 397
Cdd:COG1116  148 AIARALANDPEVLLMDEPFGALDALTRERLQDELLRlwQETGKTVLFVTHdvdeavFLAD-R----VVVLSAR 215

ABC_Class3

cd03229

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

184-398

3.97e-37

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: 133.85 E-value: 3.97e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWL-RGQV 262
Cdd:cd03229    1 LELKNVSKRYG---QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPpLRRR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 263 IGFISQEPVLFAT-TIMENIRFGkldasdeevytaareanahefissfpdgystvvgergttLSGGQKQRLAIARALIKQ 341
Cdd:cd03229   78 IGMVFQDFALFPHlTVLENIALG---------------------------------------LSGGQQQRVALARALAMD 118

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 342 PTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTV-RAAHSIIVMANGQ 398
Cdd:cd03229  119 PDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAaRLADRVVVLRDGK 178

DppD

COG0444

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

187-410

1.08e-36

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];

Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 136.72 E-value: 1.08e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 187 QNVTFSYPCRPG-FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEA---GSVTLDGHDLRTLNPS---WLR 259
Cdd:COG0444    5 RNLKVYFPTRRGvVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKelrKIR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 260 GQVIGFISQEPvlFA---------TTIMENIRFGKlDASDEEVYTAAREA-------NAHEFISSFPdgystvvGErgtt 323
Cdd:COG0444   85 GREIQMIFQDP--MTslnpvmtvgDQIAEPLRIHG-GLSKAEARERAIELlervglpDPERRLDRYP-------HE---- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 324 LSGGQKQRLAIARALIKQPTVLILDEATSALDAeserVVQ-EALD-----RASAGRTVLVIAHRLSTVRA-AHSIIVMAN 396
Cdd:COG0444  151 LSGGMRQRVMIARALALEPKLLIADEPTTALDV----TIQaQILNllkdlQRELGLAILFITHDLGVVAEiADRVAVMYA 226

                        250
                 ....*....|....
gi 755511082 397 GQVCEAGTHEELLK 410
Cdd:COG0444  227 GRIVEEGPVEELFE 240

PLN03232

ABC transporter C family member; Provisional

7-419

8.42e-36

ABC transporter C family member; Provisional

Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 140.88 E-value: 8.42e-36

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082    7 TLMLAVVTPalmgVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAelesccCKAEELgrg 86
Cdd:PLN03232  447 SLILFLLIP----LQTLIVRKMRKLTKEGLQWTDKRVGIINEILASMDTVKCYAWEKSFESRIQG------IRNEEL--- 513

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   87 iALF---QGLSniAFNCMVLGTLFIGGSLVAGQQ--LKGGDL-----MSFLVASQTVQRSMASLSVLFGQVVRGLSAGAR 156
Cdd:PLN03232  514 -SWFrkaQLLS--AFNSFILNSIPVVVTLVSFGVfvLLGGDLtparaFTSLSLFAVLRSPLNMLPNLLSQVVNANVSLQR 590

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  157 VFEYM-----ALSPVIPLTGGycIPnkdirgSITFQNVTFSYPCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTT-VAS 230
Cdd:PLN03232  591 IEELLlseerILAQNPPLQPG--AP------AISIKNGYFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSlISA 662

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  231 LLERFYDPEAGSVTLdghdlrtlnpswlRGQViGFISQEPVLFATTIMENIRFGKldASDEEVYTAAREANA--HEfISS 308
Cdd:PLN03232  663 MLGELSHAETSSVVI-------------RGSV-AYVPQVSWIFNATVRENILFGS--DFESERYWRAIDVTAlqHD-LDL 725

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  309 FPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAE-SERVVQEALDRASAGRTVLVIAHRLSTVRA 387
Cdd:PLN03232  726 LPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGKTRVLVTNQLHFLPL 805

                         410       420       430
                  ....*....|....*....|....*....|..
gi 755511082  388 AHSIIVMANGQVCEAGTHEELLKKGGLYSELI 419
Cdd:PLN03232  806 MDRIILVSEGMIKEEGTFAELSKSGSLFKKLM 837

PLN03232

ABC transporter C family member; Provisional

181-413

1.10e-35

ABC transporter C family member; Provisional

Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 140.88 E-value: 1.10e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  181 RGSITFQNVTFSYpcRPGFN-VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLR 259
Cdd:PLN03232 1232 RGSIKFEDVHLRY--RPGLPpVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLR 1309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  260 gQVIGFISQEPVLFATTIMENIR-FGklDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARAL 338
Cdd:PLN03232 1310 -RVLSIIPQSPVLFSGTVRFNIDpFS--EHNDADLWEALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARAL 1386

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755511082  339 IKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGG 413
Cdd:PLN03232 1387 LRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDT 1461

PLN03130

ABC transporter C family member; Provisional

182-420

1.16e-35

ABC transporter C family member; Provisional

Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 140.64 E-value: 1.16e-35

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  182 GSITFQNVTFSYpcRPGFN-VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRg 260
Cdd:PLN03130 1236 GSIKFEDVVLRY--RPELPpVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLR- 1312

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  261 QVIGFISQEPVLFATTImeniRFgKLDA----SDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIAR 336
Cdd:PLN03130 1313 KVLGIIPQAPVLFSGTV----RF-NLDPfnehNDADLWESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLAR 1387

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  337 ALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELL-KKGGLY 415
Cdd:PLN03130 1388 ALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLLsNEGSAF 1467


                  ....*
gi 755511082  416 SELIR 420
Cdd:PLN03130 1468 SKMVQ 1472

ABC_PhnC_transporter

cd03256

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

184-408

2.00e-35

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: 131.15 E-value: 2.00e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQV- 262
Cdd:cd03256    1 IEVENLSKTYP--NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLRr 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 263 -IGFISQEPVLFA-TTIMENIRFGKLdasdeevytaareaNAHEFISSFPDGYS-----------TVVG------ERGTT 323
Cdd:cd03256   79 qIGMIFQQFNLIErLSVLENVLSGRL--------------GRRSTWRSLFGLFPkeekqralaalERVGlldkayQRADQ 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 324 LSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRA-AHSIIVMANGQVC 400
Cdd:cd03256  145 LSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAREyADRIVGLKDGRIV 224


                 ....*...
gi 755511082 401 EAGTHEEL 408
Cdd:cd03256  225 FDGPPAEL 232

ABC_Carb_Solutes_like

cd03259

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

184-403

2.12e-35

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: 130.33 E-value: 2.12e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLnPSWLRGqvI 263
Cdd:cd03259    1 LELKGLSKTYG---SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV-PPERRN--I 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEPVLFAT-TIMENIRFG------KLDASDEEVYTAAREANAHEFISSFPDgystvvgergtTLSGGQKQRLAIAR 336
Cdd:cd03259   75 GMVFQDYALFPHlTVAENIAFGlklrgvPKAEIRARVRELLELVGLEGLLNRYPH-----------ELSGGQQQRVALAR 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 337 ALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLS-TVRAAHSIIVMANGQVCEAG 403
Cdd:cd03259  144 ALAREPSLLLLDEPLSALDAKLREELREELKElqRELGITTIYVTHDQEeALALADRIAVMNEGRIVQVG 213

ABC_cobalt_CbiO_domain2

cd03226

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

188-399

3.06e-35

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

Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 129.68 E-value: 3.06e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 188 NVTFSYpcRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLrtlnPSWLRGQVIGFIS 267
Cdd:cd03226    4 NISFSY--KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI----KAKERRKSIGYVM 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 268 QEP--VLFATTIMENIRFGK--LDASDEEVYTAAREANAHEFISSFPdgystvvgergTTLSGGQKQRLAIARALIKQPT 343
Cdd:cd03226   78 QDVdyQLFTDSVREELLLGLkeLDAGNEQAETVLKDLDLYALKERHP-----------LSLSGGQKQRLAIAAALLSGKD 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755511082 344 VLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV-RAAHSIIVMANGQV 399
Cdd:cd03226  147 LLIFDEPTSGLDYKNMERVGELIRElAAQGKAVIVITHDYEFLaKVCDRVLLLANGAI 204

ZnuC

COG1121

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

184-409

4.23e-35

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

Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 130.59 E-value: 4.23e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTT-VASLLeRFYDPEAGSVTLDGHDLRtlnpswLRGQV 262
Cdd:COG1121    7 IELENLTVSYGGRP---VLEDVSLTIPPGEFVAIVGPNGAGKSTlLKAIL-GLLPPTSGTVRLFGKPPR------RARRR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 263 IGFISQEPVL---FATTIMENIR---------FGKLDASDEEvytAAREA----NAHEFISsfpdgysTVVGErgttLSG 326
Cdd:COG1121   77 IGYVPQRAEVdwdFPITVRDVVLmgrygrrglFRRPSRADRE---AVDEAlervGLEDLAD-------RPIGE----LSG 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 327 GQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEaGT 404
Cdd:COG1121  143 GQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREyFDRVLLLNRGLVAH-GP 221


                 ....*
gi 755511082 405 HEELL 409
Cdd:COG1121  222 PEEVL 226

cbiO

PRK13635

energy-coupling factor ABC transporter ATP-binding protein;

184-420

4.82e-35

energy-coupling factor ABC transporter ATP-binding protein;

Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 131.29 E-value: 4.82e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYP--CRPGfnvLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGhdlRTLNPS--W-L 258
Cdd:PRK13635   6 IRVEHISFRYPdaATYA---LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEEtvWdV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 259 RGQViGFISQEP--VLFATTIMENIRFG------KLDASDEEVYTAAREANAHEFISSFPdgystvvgergTTLSGGQKQ 330
Cdd:PRK13635  80 RRQV-GMVFQNPdnQFVGATVQDDVAFGlenigvPREEMVERVDQALRQVGMEDFLNREP-----------HRLSGGQKQ 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 331 RLAIARALIKQPTVLILDEATSALDAESErvvQEALD-----RASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTH 405
Cdd:PRK13635 148 RVAIAGVLALQPDIIILDEATSMLDPRGR---REVLEtvrqlKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTP 224

                        250
                 ....*....|....*
gi 755511082 406 EELLKKGglySELIR 420
Cdd:PRK13635 225 EEIFKSG---HMLQE 236

FtsE

COG2884

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

184-403

4.82e-35

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

Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 129.79 E-value: 4.82e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPS---WLRg 260
Cdd:COG2884    2 IRFENVSKRYP--GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRReipYLR- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 261 QVIGFISQE-PVLFATTIMENIRF-----GKldaSDEEVYTAAREA----NAHEFISSFPDgystvvgergtTLSGGQKQ 330
Cdd:COG2884   79 RRIGVVFQDfRLLPDRTVYENVALplrvtGK---SRKEIRRRVREVldlvGLSDKAKALPH-----------ELSGGEQQ 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755511082 331 RLAIARALIKQPTVLILDEATSALDAE-SERVVqEALDRASA-GRTVLVIAHRLSTVRAA-HSIIVMANGQVCEAG 403
Cdd:COG2884  145 RVAIARALVNRPELLLADEPTGNLDPEtSWEIM-ELLEEINRrGTTVLIATHDLELVDRMpKRVLELEDGRLVRDE 219

ABC_Iron-Siderophores_B12_Hemin

cd03214

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

187-403

5.25e-35

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.

Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 128.32 E-value: 5.25e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 187 QNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgQVIGFI 266
Cdd:cd03214    3 ENLSVGYGGRT---VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA-RKIAYV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 267 SQepvlfattIMEniRFGKLDASDEEVytaareanahefissfpdgystvvgergTTLSGGQKQRLAIARALIKQPTVLI 346
Cdd:cd03214   79 PQ--------ALE--LLGLAHLADRPF----------------------------NELSGGERQRVLLARALAQEPPILL 120

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 347 LDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLS-TVRAAHSIIVMANGQVCEAG 403
Cdd:cd03214  121 LDEPTSHLDIAHQIELLELLRRlaRERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180

ABC_OpuCA_Osmoprotection

cd03295

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

184-409

5.42e-35

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: 130.11 E-value: 5.42e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgQVI 263
Cdd:cd03295    1 IEFENVTKRYG--GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELR-RKI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEPVLFA-TTIMENIrfgKLDASDEEVYTAAREANAHEFIS-------SFPDGYSTvvgergtTLSGGQKQRLAIA 335
Cdd:cd03295   78 GYVIQQIGLFPhMTVEENI---ALVPKLLKWPKEKIRERADELLAlvgldpaEFADRYPH-------ELSGGQQQRVGVA 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755511082 336 RALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRL-STVRAAHSIIVMANGQVCEAGTHEELL 409
Cdd:cd03295  148 RALAADPPLLLMDEPFGALDPITRDQLQEEFKRlqQELGKTIVFVTHDIdEAFRLADRIAIMKNGEIVQVGTPDEIL 224

PotA

COG3842

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

183-408

8.31e-35

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

Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 132.53 E-value: 8.31e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 183 SITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLnPSWLRGqv 262
Cdd:COG3842    5 ALELENVSKRYG---DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL-PPEKRN-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 263 IGFISQEPVLFA-TTIMENIRFG----KLDAsdeevytAAREANAHE---------FISSFPDgystvvgergtTLSGGQ 328
Cdd:COG3842   79 VGMVFQDYALFPhLTVAENVAFGlrmrGVPK-------AEIRARVAEllelvglegLADRYPH-----------QLSGGQ 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 329 KQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLS---TVraAHSIIVMANGQVCEAG 403
Cdd:COG3842  141 QQRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRlqRELGITFIYVTHDQEealAL--ADRIAVMNDGRIEQVG 218


                 ....*
gi 755511082 404 THEEL 408
Cdd:COG3842  219 TPEEI 223

PhnC

COG3638

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

184-399

8.35e-35

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

Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 129.79 E-value: 8.35e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRG--Q 261
Cdd:COG3638    3 LELRNLSKRYP--GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRlrR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 262 VIGFISQEPVLFA-TTIMENIRFGKLDA-----------SDEEVytaareANAHEFISSfpdgystvVG------ERGTT 323
Cdd:COG3638   81 RIGMIFQQFNLVPrLSVLTNVLAGRLGRtstwrsllglfPPEDR------ERALEALER--------VGladkayQRADQ 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755511082 324 LSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRA-AHSIIVMANGQV 399
Cdd:COG3638  147 LSGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIARedGITVVVNLHQVDLARRyADRIIGLRDGRV 225

ABC_Org_Solvent_Resistant

cd03261

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

184-410

1.15e-34

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: 129.16 E-value: 1.15e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRG--Q 261
Cdd:cd03261    1 IELRGLTKSFGGRT---VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRlrR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 262 VIGFISQEPVLF-ATTIMENIRFG---KLDASDEEVYTAARE----ANAHEFISSFPdgystvvGErgttLSGGQKQRLA 333
Cdd:cd03261   78 RMGMLFQSGALFdSLTVFENVAFPlreHTRLSEEEIREIVLEkleaVGLRGAEDLYP-------AE----LSGGMKKRVA 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 334 IARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEELLK 410
Cdd:cd03261  147 LARALALDPELLLYDEPTAGLDPIASGVIDDLIRSlkKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEGTPEELRA 226

cbiO

PRK13632

cobalt transporter ATP-binding subunit; Provisional

175-410

3.34e-34

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 128.96 E-value: 3.34e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 175 IPNKDIrgSITFQNVTFSYPcrPGF-NVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTL 253
Cdd:PRK13632   1 IKNKSV--MIKVENVSFSYP--NSEnNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 254 NPSWLRGQvIGFISQEP--VLFATTIMENIRFG----KLDASD--EEVYTAAREANAHEFISSFPDgystvvgergtTLS 325
Cdd:PRK13632  77 NLKEIRKK-IGIIFQNPdnQFIGATVEDDIAFGlenkKVPPKKmkDIIDDLAKKVGMEDYLDKEPQ-----------NLS 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 326 GGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAG 403
Cdd:PRK13632 145 GGQKQRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVdlRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQG 224


                 ....*..
gi 755511082 404 THEELLK 410
Cdd:PRK13632 225 KPKEILN 231

MlaF

COG1127

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

184-410

5.68e-34

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: 127.40 E-value: 5.68e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPS---WLRG 260
Cdd:COG1127    6 IEVRNLTKSFG---DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyELRR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 261 QvIGFISQEPVLF-ATTIMENIRFG---KLDASDEEVYTAAREA----NAHEFISSFPdgystvvGErgttLSGGQKQRL 332
Cdd:COG1127   83 R-IGMLFQGGALFdSLTVFENVAFPlreHTDLSEAEIRELVLEKlelvGLPGAADKMP-------SE----LSGGMRKRV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 333 AIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEELL 409
Cdd:COG1127  151 ALARALALDPEILLYDEPTAGLDPITSAVIDELIRelRDELGLTSVVVTHDLDSAFAiADRVAVLADGKIIAEGTPEELL 230


                 .
gi 755511082 410 K 410
Cdd:COG1127  231 A 231

ABCC_SUR2

cd03288

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

182-420

5.83e-34

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: 127.72 E-value: 5.83e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 182 GSITFQNVTFSYP--CRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLR 259
Cdd:cd03288   18 GEIKIHDLCVRYEnnLKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 260 GQvIGFISQEPVLFATTIMENIRfGKLDASDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALI 339
Cdd:cd03288   95 SR-LSIILQDPILFSGSIRFNLD-PECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFV 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 340 KQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELL-KKGGLYSEL 418
Cdd:cd03288  173 RKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIAHRVSTILDADLVLVLSRGILVECDTPENLLaQEDGVFASL 252


                 ..
gi 755511082 419 IR 420
Cdd:cd03288  253 VR 254

ABC_6TM_ABCB10_like

cd18573

Six-transmembrane helical domain (6-TMD) of the mitochondrial transporter ABCB10 (subfamily B, ...

2-157

6.82e-34

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: 128.79 E-value: 6.82e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   2 LSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAE 81
Cdd:cd18573  139 ISPKLTLVMLLVVPPIAVGAVFYGRYVRKLSKQVQDALADATKVAEERLSNIRTVRAFAAERKEVERYAKKVDEVFDLAK 218

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755511082  82 ELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 157
Cdd:cd18573  219 KEALASGLFFGSTGFSGNLSLLSVLYYGGSLVASGELTVGDLTSFLMYAVYVGSSVSGLSSFYSELMKGLGASSRL 294

GlnQ

COG1126

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

184-409

8.83e-34

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

Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 126.65 E-value: 8.83e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTV---ASLLERfydPEAGSVTLDGHDL----RTLNPs 256
Cdd:COG1126    2 IEIENLHKSFG---DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDLtdskKDINK- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 257 wLRGQvIGFISQEPVLFA-TTIMENIRFG-----KLdaSDEEVYTAAREANAH----EFISSFPDgystvvgergtTLSG 326
Cdd:COG1126   75 -LRRK-VGMVFQQFNLFPhLTVLENVTLApikvkKM--SKAEAEERAMELLERvglaDKADAYPA-----------QLSG 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 327 GQKQRLAIARALIKQPTVLILDEATSALDAEserVVQEALD--R--ASAGRTVLVIAHRLSTVR-AAHSIIVMANGQVCE 401
Cdd:COG1126  140 GQQQRVAIARALAMEPKVMLFDEPTSALDPE---LVGEVLDvmRdlAKEGMTMVVVTHEMGFAReVADRVVFMDGGRIVE 216


                 ....*...
gi 755511082 402 AGTHEELL 409
Cdd:COG1126  217 EGPPEEFF 224

ABC_ModC_like

cd03299

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

201-411

2.87e-33

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: 125.14 E-value: 2.87e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 201 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSwLRGqvIGFISQEPVLFA-TTIME 279
Cdd:cd03299   14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-KRD--ISYVPQNYALFPhMTVYK 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 280 NIRFG--KLDASDEEVYTAAREanahefISSFPdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAE 357
Cdd:cd03299   91 NIAYGlkKRKVDKKEIERKVLE------IAEML-GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVR 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755511082 358 SERVVQEALDRA--SAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEELLKK 411
Cdd:cd03299  164 TKEKLREELKKIrkEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKK 220

CysA

COG1118

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

183-410

2.18e-32

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

Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 125.64 E-value: 2.18e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 183 SITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASL---LERfydPEAGSVTLDGHDLRTLNPSWLR 259
Cdd:COG1118    2 SIEVRNISKRFG---SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIiagLET---PDSGRIVLNGRDLFTNLPPRER 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 260 GqvIGFISQEPVLFA-TTIMENIRFG--KLDASDEEvytaaREANAHEFISSFP-DGYstvvGER-GTTLSGGQKQRLAI 334
Cdd:COG1118   76 R--VGFVFQHYALFPhMTVAENIAFGlrVRPPSKAE-----IRARVEELLELVQlEGL----ADRyPSQLSGGQRQRVAL 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 335 ARALIKQPTVLILDEATSALDA----ESERVVQEALDRasAGRTVLVIAH-RLSTVRAAHSIIVMANGQVCEAGTHEELL 409
Cdd:COG1118  145 ARALAVEPEVLLLDEPFGALDAkvrkELRRWLRRLHDE--LGGTTVFVTHdQEEALELADRVVVMNQGRIEQVGTPDEVY 222


                 .
gi 755511082 410 K 410
Cdd:COG1118  223 D 223

ABC_Mj1267_LivG_branched

cd03219

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

198-410

2.36e-32

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: 122.93 E-value: 2.36e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 198 GFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVIG--FisQEPVLFAT 275
Cdd:cd03219   12 GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGrtF--QIPRLFPE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 276 -TIMENIR--------FGKLDASDEEVYTAAREAnAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLI 346
Cdd:cd03219   90 lTVLENVMvaaqartgSGLLLARARREEREARER-AEELLERV--GLADLADRPAGELSYGQQRRLEIARALATDPKLLL 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755511082 347 LDEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEELLK 410
Cdd:cd03219  167 LDEPAAGLnPEETEELAELIRELRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTPDEVRN 232

ThiQ

COG3840

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

184-409

2.99e-32

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

Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 122.56 E-value: 2.99e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcrpgfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSwLRGqvI 263
Cdd:COG3840    2 LRLDDLTYRYG-----DFPLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA-ERP--V 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEPVLFA-TTIMENIRFG-----KLDASD-EEVYTAAREANAHEFISSFPDgystvvgergtTLSGGQKQRLAIAR 336
Cdd:COG3840   74 SMLFQENNLFPhLTVAQNIGLGlrpglKLTAEQrAQVEQALERVGLAGLLDRLPG-----------QLSGGQRQRVALAR 142

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755511082 337 ALIKQPTVLILDEATSALD----AESERVVQEAldRASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEELL 409
Cdd:COG3840  143 CLVRKRPILLLDEPFSALDpalrQEMLDLVDEL--CRERGLTVLMVTHDPEDAaRIADRVLLVADGRIAADGPTAALL 218

ABC_Metallic_Cations

cd03235

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

186-403

4.13e-32

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.

Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 121.49 E-value: 4.13e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 186 FQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGhdlrtlNPSWLRGQVIGF 265
Cdd:cd03235    2 VEDLTVSYG---GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG------KPLEKERKRIGY 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 266 ISQEPVL---FATTIMENIR---------FGKLDASDEEvytAAREAnaHEF--ISSFPDgystvvgERGTTLSGGQKQR 331
Cdd:cd03235   73 VPQRRSIdrdFPISVRDVVLmglyghkglFRRLSKADKA---KVDEA--LERvgLSELAD-------RQIGELSGGQQQR 140

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755511082 332 LAIARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAG 403
Cdd:cd03235  141 VLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYFDRVLLLNRTVVASG 213

PstB

COG1117

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

184-408

5.50e-32

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

Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 122.45 E-value: 5.50e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYD--PEA---GSVTLDGHDL--RTLNPS 256
Cdd:COG1117   12 IEVRNLNVYYG---DKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDliPGArveGEILLDGEDIydPDVDVV 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 257 WLRGQViGFISQEPVLFATTIMENIRFG-----KLDAS--DEEVYTAAREANA-HEfissfpdgystvVGER----GTTL 324
Cdd:COG1117   89 ELRRRV-GMVFQKPNPFPKSIYDNVAYGlrlhgIKSKSelDEIVEESLRKAALwDE------------VKDRlkksALGL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 325 SGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLS-TVRAAHSIIVMANGQVCEAG 403
Cdd:COG1117  156 SGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTIVIVTHNMQqAARVSDYTAFFYLGELVEFG 235


                 ....*
gi 755511082 404 THEEL 408
Cdd:COG1117  236 PTEQI 240

ABC_HisP_GlnQ

cd03262

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

184-399

3.81e-31

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: 118.79 E-value: 3.81e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDL--RTLNPSWLRGQ 261
Cdd:cd03262    1 IEIKNLHKSFG---DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtdDKKNINELRQK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 262 ViGFISQEPVLFA-TTIMENIRFGK---LDASDEEVYTAAREANAH----EFISSFPDgystvvgergtTLSGGQKQRLA 333
Cdd:cd03262   78 V-GMVFQQFNLFPhLTVLENITLAPikvKGMSKAEAEERALELLEKvglaDKADAYPA-----------QLSGGQQQRVA 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755511082 334 IARALIKQPTVLILDEATSALDAEserVVQEALD----RASAGRTVLVIAHRLSTVR-AAHSIIVMANGQV 399
Cdd:cd03262  146 IARALAMNPKVMLFDEPTSALDPE---LVGEVLDvmkdLAEEGMTMVVVTHEMGFAReVADRVIFMDDGRI 213

YejF

COG4172

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...

187-409

7.57e-31

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];

Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 124.41 E-value: 7.57e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 187 QNVTFSYPCRPG--------FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFyDPEAGSVTLDGHDLRTLNPSWL 258
Cdd:COG4172  279 RDLKVWFPIKRGlfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRAL 357

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 259 RG-----QVIgFisQEPvlFAT---------TIMENIRFGKLDASDEEVYTAAREANA-------------HEFissfpd 311
Cdd:COG4172  358 RPlrrrmQVV-F--QDP--FGSlsprmtvgqIIAEGLRVHGPGLSAAERRARVAEALEevgldpaarhrypHEF------ 426

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 312 gystvvgergttlSGGQKQRLAIARALIKQPTVLILDEATSALDaeseRVVQ-EALD-----RASAGRTVLVIAHRLSTV 385
Cdd:COG4172  427 -------------SGGQRQRIAIARALILEPKLLVLDEPTSALD----VSVQaQILDllrdlQREHGLAYLFISHDLAVV 489

                        250       260
                 ....*....|....*....|....*
gi 755511082 386 RA-AHSIIVMANGQVCEAGTHEELL 409
Cdd:COG4172  490 RAlAHRVMVMKDGKVVEQGPTEQVF 514

ABC_TM1139_LivF_branched

cd03224

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

198-409

3.63e-30

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: 116.38 E-value: 3.63e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 198 GFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWL--RGqvIGFISQEPVLFAT 275
Cdd:cd03224   12 KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERarAG--IGYVPEGRRIFPE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 276 -TIMENIRFG-------KLDASDEEVYTAareanahefissFPdgystVVGER----GTTLSGGQKQRLAIARALIKQPT 343
Cdd:cd03224   90 lTVEENLLLGayarrraKRKARLERVYEL------------FP-----RLKERrkqlAGTLSGGEQQMLAIARALMSRPK 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755511082 344 VLILDEATSALdaeSERVVQEALDR----ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEELL 409
Cdd:cd03224  153 LLLLDEPSEGL---APKIVEEIFEAirelRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAAELL 220

ABC_CysA_sulfate_importer

cd03296

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...

183-408

5.64e-30

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 116.28 E-value: 5.64e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 183 SITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPswlRGQV 262
Cdd:cd03296    2 SIEVRNVSKRFG---DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPV---QERN 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 263 IGFISQEPVLFA-TTIMENIRFG-KLDASDEEVYTAAREANAHEFI-----SSFPDGYSTvvgergtTLSGGQKQRLAIA 335
Cdd:cd03296   76 VGFVFQHYALFRhMTVFDNVAFGlRVKPRSERPPEAEIRAKVHELLklvqlDWLADRYPA-------QLSGGQRQRVALA 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755511082 336 RALIKQPTVLILDEATSALDA----ESERVVQEALDRASAgRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEEL 408
Cdd:cd03296  149 RALAVEPKVLLLDEPFGALDAkvrkELRRWLRRLHDELHV-TTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224

ABC_6TM_TAP

cd18572

Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen ...

1-157

6.15e-30

Six-transmembrane helical domain (6-TMD) of the ABC transporter associated with antigen processing; This group represents the 6-TM subunit of the ABC transporter associated with antigen processing (TAP), which is essential to cellular immunity against viral infection. TAP is involved in the transport of antigens from the cytoplasm to the endoplasmic reticulum(ER) for association with MHC class I molecules, which play a central role in the adaptive immune response to viruses and cancers by presenting antigenic peptides to CD8+ cytotoxic T lymphocytes (CTLs). It also acts as a molecular scaffold for the assembly of the MHC I peptide-loading complex in the ER membrane. Newly synthesized MHC class I molecules associate with TAP via tapasin, which is one component of the peptide-loading complex. TAP is a heterodimer formed by two distinct subunits, TAP1 (ABCB2) and TAP2 (ABCB3), each half-transporter comprises one transmembrane domain (TMD) and one nucleotide domain (NBD). Two 6-helical core TMDs contain the peptide-binding pocket and translocation channel, while the NBDs bind and hydrolyze ATP to power peptide translocation.

Pssm-ID: 350016 [Multi-domain] Cd Length: 289 Bit Score: 117.64 E-value: 6.15e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   1 MLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKA 80
Cdd:cd18572  133 SLSWRLTLLAFITVPVIALITKVYGRYYRKLSKEIQDALAEANQVAEEALSNIRTVRSFATEEREARRYERALDKALKLS 212

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755511082  81 EELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 157
Cdd:cd18572  213 VRQALAYAGYVAVNTLLQNGTQVLVLFYGGHLVLSGRMSAGQLVTFMLYQQQLGEAFQSLGDVFSSLMQAVGAAEKV 289

ABC_6TM_bac_exporter_ABCB8_10_like

cd18576

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

2-157

1.22e-29

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: 116.81 E-value: 1.22e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   2 LSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAE 81
Cdd:cd18576  134 ISWKLTLLMLATVPVVVLVAVLFGRRIRKLSKKVQDELAEANTIVEETLQGIRVVKAFTREDYEIERYRKALERVVKLAL 213

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755511082  82 ELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 157
Cdd:cd18576  214 KRARIRALFSSFIIFLLFGAIVAVLWYGGRLVLAGELTAGDLVAFLLYTLFIAGSIGSLADLYGQLQKALGASERV 289

MRP_assoc_pro

TIGR00957

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

183-420

1.68e-29

Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 122.36 E-value: 1.68e-29

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   183 SITFQNVTFSYpCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHdlrtlnpswlrgqv 262
Cdd:TIGR00957  636 SITVHNATFTW-ARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------- 700

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   263 IGFISQEPVLFATTIMENIRFGKldASDEEVYTAAREANAH-EFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQ 341
Cdd:TIGR00957  701 VAYVPQQAWIQNDSLRENILFGK--ALNEKYYQQVLEACALlPDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSN 778

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   342 PTVLILDEATSALDAESERVVQEAL---DRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSEL 418
Cdd:TIGR00957  779 ADIYLFDDPLSAVDAHVGKHIFEHVigpEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKISEMGSYQELLQRDGAFAEF 858


                   ..
gi 755511082   419 IR 420
Cdd:TIGR00957  859 LR 860

ABC_subfamily_A

cd03263

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...

184-408

2.20e-29

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: 114.14 E-value: 2.20e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPgFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTlNPSWLRgQVI 263
Cdd:cd03263    1 LQIRNLTKTYKKGT-KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAAR-QSL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEPVLFAT-TIMENIRF-GKLDAsdeeVYTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQ 341
Cdd:cd03263   78 GYCPQFDALFDElTVREHLRFyARLKG----LPKSEIKEEVELLLRVL--GLTDKANKRARTLSGGMKRKLSLAIALIGG 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755511082 342 PTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEEL 408
Cdd:cd03263  152 PSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQEL 219

MglA

COG1129

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

184-399

5.04e-29

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

Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 118.97 E-value: 5.04e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNP--SWLRGq 261
Cdd:COG1129    5 LEMRGISKSFG---GVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrdAQAAG- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 262 vIGFISQEPVLFAT-TIMENI-------RFGKLDasDEEVYTAAREAnahefISSF-----PDgysTVVGErgttLSGGQ 328
Cdd:COG1129   81 -IAIIHQELNLVPNlSVAENIflgreprRGGLID--WRAMRRRAREL-----LARLgldidPD---TPVGD----LSVAQ 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755511082 329 KQRLAIARALIKQPTVLILDEATSAL-DAESER---VVQEaLdrASAGRTVLVIAHRLSTVRA-AHSIIVMANGQV 399
Cdd:COG1129  146 QQLVEIARALSRDARVLILDEPTASLtEREVERlfrIIRR-L--KAQGVAIIYISHRLDEVFEiADRVTVLRDGRL 218

ABC_Pro_Gly_Betaine

cd03294

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

202-409

6.51e-29

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: 114.28 E-value: 6.51e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 202 LKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWL---RGQVIGFISQEPVLFA-TTI 277
Cdd:cd03294   40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELrelRRKKISMVFQSFALLPhRTV 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 278 MENIRFGkLD---ASDEEVYTAAREA----NAHEFISSFPDgystvvgergtTLSGGQKQRLAIARALIKQPTVLILDEA 350
Cdd:cd03294  120 LENVAFG-LEvqgVPRAEREERAAEAlelvGLEGWEHKYPD-----------ELSGGMQQRVGLARALAVDPDILLMDEA 187

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755511082 351 TSALDAESERVVQEALDR--ASAGRTVLVIAHRLS-TVRAAHSIIVMANGQVCEAGTHEELL 409
Cdd:cd03294  188 FSALDPLIRREMQDELLRlqAELQKTIVFITHDLDeALRLGDRIAIMKDGRLVQVGTPEEIL 249

ABC_Carb_Monos_I

cd03216

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

184-399

1.06e-28

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: 110.60 E-value: 1.06e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVI 263
Cdd:cd03216    1 LELRGITKRFG---GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQepvlfattimenirfgkldasdeevytaareanahefissfpdgystvvgergttLSGGQKQRLAIARALIKQPT 343
Cdd:cd03216   78 AMVYQ-------------------------------------------------------LSVGERQMVEIARALARNAR 102

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755511082 344 VLILDEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQV 399
Cdd:cd03216  103 LLILDEPTAALtPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVTVLRDGRV 160

PLN03130

ABC transporter C family member; Provisional

7-419

1.31e-28

ABC transporter C family member; Provisional

Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 119.46 E-value: 1.31e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082    7 TLMLAVVTPAlmgvGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKReeerYQAELESCccKAEELG-- 84
Cdd:PLN03130  447 SLMLVLMFPI----QTFIISKMQKLTKEGLQRTDKRIGLMNEVLAAMDTVKCYAWENS----FQSKVQTV--RDDELSwf 516

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   85 RGIALfqgLSniAFNCMVLGTLFIGGSLVA--GQQLKGGDLmsflvasqTVQRSMASLSV-------------LFGQVVR 149
Cdd:PLN03130  517 RKAQL---LS--AFNSFILNSIPVLVTVVSfgVFTLLGGDL--------TPARAFTSLSLfavlrfplfmlpnLITQAVN 583

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  150 GLSAGARVFEYM-----ALSPVIPLTGGycIPnkdirgSITFQNVTFSYPCRPGFNVLKDFTLKLPSGKIVALVGQSGGG 224
Cdd:PLN03130  584 ANVSLKRLEELLlaeerVLLPNPPLEPG--LP------AISIKNGYFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEG 655

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  225 KTTVAS-LLERFYDPEAGSVTLdghdlrtlnpswlRGQViGFISQEPVLFATTIMENIRFGKldASDEEVYTAAREANA- 302
Cdd:PLN03130  656 KTSLISaMLGELPPRSDASVVI-------------RGTV-AYVPQVSWIFNATVRDNILFGS--PFDPERYERAIDVTAl 719

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  303 HEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESER-VVQEALDRASAGRT-VLVI-- 378
Cdd:PLN03130  720 QHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRqVFDKCIKDELRGKTrVLVTnq 799

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 755511082  379 AHRLSTVraaHSIIVMANGQVCEAGTHEELLKKGGLYSELI 419
Cdd:PLN03130  800 LHFLSQV---DRIILVHEGMIKEEGTYEELSNNGPLFQKLM 837

metN

PRK11153

DL-methionine transporter ATP-binding subunit; Provisional

184-404

1.76e-28

DL-methionine transporter ATP-binding subunit; Provisional

Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 114.90 E-value: 1.76e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPC-RPGFNVLKDFTLKLPSGKIVALVGQSGGGKTT---VASLLERfydPEAGSVTLDGHDLRTLNPSWLR 259
Cdd:PRK11153   2 IELKNISKVFPQgGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 260 G--QVIGFISQEPVLFAT-TIMENIRFG-KLDASDEevytAAREANAHEF-----ISSFPDGYSTvvgergtTLSGGQKQ 330
Cdd:PRK11153  79 KarRQIGMIFQHFNLLSSrTVFDNVALPlELAGTPK----AEIKARVTELlelvgLSDKADRYPA-------QLSGGQKQ 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755511082 331 RLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGT 404
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRiCDRVAVIDAGRLVEQGT 224

ABC_PotA_N

cd03300

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

184-408

1.98e-28

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: 111.95 E-value: 1.98e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLnPSWLRGqvI 263
Cdd:cd03300    1 IELENVSKFYG---GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL-PPHKRP--V 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEPVLFA-TTIMENIRFG----KLDASD--EEVYTAAREANAHEFISSFPDgystvvgergtTLSGGQKQRLAIAR 336
Cdd:cd03300   75 NTVFQNYALFPhLTVFENIAFGlrlkKLPKAEikERVAEALDLVQLEGYANRKPS-----------QLSGGQQQRVAIAR 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755511082 337 ALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEEL 408
Cdd:cd03300  144 ALVNEPKVLLLDEPLGALDLKLRKDMQLELKRlqKELGITFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEI 218

AppF

COG4608

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

187-408

2.62e-28

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

Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 114.06 E-value: 2.62e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 187 QNVTFSYPCRPGF-----NVLK---DFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWL 258
Cdd:COG4608   11 RDLKKHFPVRGGLfgrtvGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGREL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 259 RG-----QVIgFisQEPvlFA---------TTIMENIRFGKLdASDEEVYTAAREA-------------NAHEFissfpd 311
Cdd:COG4608   91 RPlrrrmQMV-F--QDP--YAslnprmtvgDIIAEPLRIHGL-ASKAERRERVAELlelvglrpehadrYPHEF------ 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 312 gystvvgergttlSGGQKQRLAIARALIKQPTVLILDEATSALD----AEserVV------QEALdrasaGRTVLVIAHR 381
Cdd:COG4608  159 -------------SGGQRQRIGIARALALNPKLIVCDEPVSALDvsiqAQ---VLnlledlQDEL-----GLTYLFISHD 217

                        250       260
                 ....*....|....*....|....*...
gi 755511082 382 LSTVR-AAHSIIVMANGQVCEAGTHEEL 408
Cdd:COG4608  218 LSVVRhISDRVAVMYLGKIVEIAPRDEL 245

PTZ00243

ABC transporter; Provisional

134-408

3.41e-28

ABC transporter; Provisional

Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 118.34 E-value: 3.41e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  134 QRSMASLSVLFGQVVRGLSAGARVFEYMALSPVIPLTGGyciPNKDIRGSITFQNVTFSYpcRPGFN-VLKDFTLKLPSG 212
Cdd:PTZ00243 1262 HEDMPELDEEVDALERRTGMAADVTGTVVIEPASPTSAA---PHPVQAGSLVFEGVQMRY--REGLPlVLRGVSFRIAPR 1336

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  213 KIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQvIGFISQEPVLFATTIMENIR-FgkLDASDE 291
Cdd:PTZ00243 1337 EKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQ-FSMIPQDPVLFDGTVRQNVDpF--LEASSA 1413

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  292 EVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLIL-DEATSALDAESERVVQEALDRAS 370
Cdd:PTZ00243 1414 EVWAALELVGLRERVASESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSGFILmDEATANIDPALDRQIQATVMSAF 1493

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 755511082  371 AGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEEL 408
Cdd:PTZ00243 1494 SAYTVITIAHRLHTVAQYDKIIVMDHGAVAEMGSPREL 1531

CcmA

COG4133

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

184-391

5.31e-28

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: 109.88 E-value: 5.31e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTT----VASLLErfydPEAGSVTLDGHDLRTLNPSWLR 259
Cdd:COG4133    3 LEAENLSCRRGERL---LFSGLSFTLAAGEALALTGPNGSGKTTllriLAGLLP----PSAGEVLWNGEPIRDAREDYRR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 260 gqVIGFISQEPVLFAT-TIMENIRF----GKLDASDEEVYTAAREAN----AHEFISsfpdgystvvgergtTLSGGQKQ 330
Cdd:COG4133   76 --RLAYLGHADGLKPElTVRENLRFwaalYGLRADREAIDEALEAVGlaglADLPVR---------------QLSAGQKR 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755511082 331 RLAIARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRAAHSI 391
Cdd:COG4133  139 RVALARLLLSPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTHQPLELAAARVL 200

ABCG_EPDR

cd03213

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

183-399

5.51e-28

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.

Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 109.56 E-value: 5.51e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 183 SITFQNVTFSYPCRPG---FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLL--ERFYDPEAGSVTLDGHDLRtlnPSW 257
Cdd:cd03213    3 TLSFRNLTVTVKSSPSksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagRRTGLGVSGEVLINGRPLD---KRS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 258 LRGQvIGFISQEPVLFAT-TIMENIRFgkldasdeevytAAREanahefissfpdgystvvgeRGttLSGGQKQRLAIAR 336
Cdd:cd03213   80 FRKI-IGYVPQDDILHPTlTVRETLMF------------AAKL--------------------RG--LSGGERKRVSIAL 124

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755511082 337 ALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLST--VRAAHSIIVMANGQV 399
Cdd:cd03213  125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRlADTGRTIICSIHQPSSeiFELFDKLLLLSQGRV 190

LivF

COG0410

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

187-409

7.08e-28

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

Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 110.46 E-value: 7.08e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 187 QNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVIGFI 266
Cdd:COG0410    7 ENLHAGYG---GIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 267 SQEPVLFAT-TIMENIRFG--------KLDASDEEVYTAareanahefissFPdgystVVGER----GTTLSGGQKQRLA 333
Cdd:COG0410   84 PEGRRIFPSlTVEENLLLGayarrdraEVRADLERVYEL------------FP-----RLKERrrqrAGTLSGGEQQMLA 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 334 IARALIKQPTVLILDEATSALdaeSERVVQE---ALDR-ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEEL 408
Cdd:COG0410  147 IGRALMSRPKLLLLDEPSLGL---APLIVEEifeIIRRlNREGVTILLVEQNARFALEiADRAYVLERGRIVLEGTAAEL 223


                 .
gi 755511082 409 L 409
Cdd:COG0410  224 L 224

LivG

COG0411

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

198-407

7.36e-28

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: 110.90 E-value: 7.36e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 198 GFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWL--RGQVIGFisQEPVLFAT 275
Cdd:COG0411   16 GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIarLGIARTF--QNPRLFPE 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 276 -TIMENI-----------------RFGKLDASDEEVYTAAREAnAHEFissfpdGYSTVVGERGTTLSGGQKQRLAIARA 337
Cdd:COG0411   94 lTVLENVlvaaharlgrgllaallRLPRARREEREARERAEEL-LERV------GLADRADEPAGNLSYGQQRRLEIARA 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755511082 338 LIKQPTVLILDEATSAL-DAESERVVQ--EALdRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEE 407
Cdd:COG0411  167 LATEPKLLLLDEPAAGLnPEETEELAEliRRL-RDERGITILLIEHDMDLVMGlADRIVVLDFGRVIAEGTPAE 239

cbiO

PRK13648

cobalt transporter ATP-binding subunit; Provisional

184-412

1.30e-27

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 110.61 E-value: 1.30e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPGFnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgQVI 263
Cdd:PRK13648   8 IVFKNVSFQYQSDASF-TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLR-KHI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEP--VLFATTIMENIRFG------KLDASDEEVYTAAREANAHEFISSFPDgystvvgergtTLSGGQKQRLAIA 335
Cdd:PRK13648  86 GIVFQNPdnQFVGSIVKYDVAFGlenhavPYDEMHRRVSEALKQVDMLERADYEPN-----------ALSGGQKQRVAIA 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755511082 336 RALIKQPTVLILDEATSALDAESERVVQEALDRASAGR--TVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKG 412
Cdd:PRK13648 155 GVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHA 233

ABC_6TM_AtABCB27_like

cd18780

Six-transmembrane helical domain (6-TMD) of the Arabidopsis ABC transporter B family member 27 ...

1-157

1.33e-27

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: 111.19 E-value: 1.33e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   1 MLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKA 80
Cdd:cd18780  139 TTSWKLTLVMLSVVPPLSIGAVIYGKYVRKLSKKFQDALAAASTVAEESISNIRTVRSFAKETKEVSRYSEKINESYLLG 218

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755511082  81 EELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 157
Cdd:cd18780  219 KKLARASGGFNGFMGAAAQLAIVLVLWYGGRLVIDGELTTGLLTSFLLYTLTVAMSFAFLSSLYGDFMQAVGASVRV 295

cbiO

PRK13650

energy-coupling factor transporter ATPase;

184-413

1.36e-27

energy-coupling factor transporter ATPase;

Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 110.98 E-value: 1.36e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLrTLNPSWLRGQVI 263
Cdd:PRK13650   5 IEVKNLTFKYKEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLL-TEENVWDIRHKI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEP--VLFATTIMENIRFGKLDASDEEVYTAAREANAHEFIssfpdGYSTVVGERGTTLSGGQKQRLAIARALIKQ 341
Cdd:PRK13650  84 GMVFQNPdnQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELV-----GMQDFKEREPARLSGGQKQRVAIAGAVAMR 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755511082 342 PTVLILDEATSALDAESE----RVVQEAldRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGG 413
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRleliKTIKGI--RDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPRELFSRGN 232

ABC_drug_resistance_like

cd03264

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

184-399

1.95e-27

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: 108.82 E-value: 1.95e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRpgfNVLKDFTLKLPSGkIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTlNPSWLRgQVI 263
Cdd:cd03264    1 LQLENLTKRYGKK---RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLR-RRI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEPVLFAT-TIMENIRF----GKLDASDEEvytaAREANAHEFIssfpdGYSTVVGERGTTLSGGQKQRLAIARAL 338
Cdd:cd03264   75 GYLPQEFGVYPNfTVREFLDYiawlKGIPSKEVK----ARVDEVLELV-----NLGDRAKKKIGSLSGGMRRRVGIAQAL 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755511082 339 IKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQV 399
Cdd:cd03264  146 VGDPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESlCNQVAVLNKGKL 207

urea_trans_UrtE

TIGR03410

urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...

201-408

2.39e-27

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: 108.77 E-value: 2.39e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  201 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVIGFISQEPVLFAT-TIME 279
Cdd:TIGR03410  15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYVPQGREIFPRlTVEE 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  280 NIRFGkLDAsdeevyTAAREANAHEFISS-FPdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD--- 355
Cdd:TIGR03410  95 NLLTG-LAA------LPRRSRKIPDEIYElFP-VLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQpsi 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755511082  356 -AESERVVQEAldRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEEL 408
Cdd:TIGR03410 167 iKDIGRVIRRL--RAEGGMAILLVEQYLDFARElADRYYVMERGRVVASGAGDEL 219

ABC_ThiQ_thiamine_transporter

cd03298

ATP-binding cassette domain of the thiamine transport system; Part of the ...

184-403

3.61e-27

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

Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 107.96 E-value: 3.61e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPgfnvlKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSwlrGQVI 263
Cdd:cd03298    1 VRLDKIRFSYGEQP-----MHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA---DRPV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEPVLFA-TTIMENIRFG-----KLDASDEE-VYTAAREANAHEFISSFPDgystvvgergtTLSGGQKQRLAIAR 336
Cdd:cd03298   73 SMLFQENNLFAhLTVEQNVGLGlspglKLTAEDRQaIEVALARVGLAGLEKRLPG-----------ELSGGERQRVALAR 141

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 337 ALIKQPTVLILDEATSALD-AESERVVQEALD-RASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAG 403
Cdd:cd03298  142 VLVRDKPVLLLDEPFAALDpALRAEMLDLVLDlHAETKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQG 211

cbiO

PRK13647

cobalt transporter ATP-binding subunit; Provisional

184-411

7.08e-27

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 109.05 E-value: 7.08e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYpcRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVi 263
Cdd:PRK13647   5 IEVEDLHFRY--KDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKV- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEP--VLFATTIMENIRFGKL------DASDEEVYTAAREANAHEFISSFPdgystvvgergTTLSGGQKQRLAIA 335
Cdd:PRK13647  82 GLVFQDPddQVFSSTVWDDVAFGPVnmgldkDEVERRVEEALKAVRMWDFRDKPP-----------YHLSYGQKKRVAIA 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755511082 336 RALIKQPTVLILDEATSALDAESERVVQEALDRAS-AGRTVLVIAHRLS-TVRAAHSIIVMANGQVCEAGTHEELLKK 411
Cdd:PRK13647 151 GVLAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHnQGKTVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTDE 228

fecE

PRK11231

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

183-437

1.16e-25

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

Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 105.10 E-value: 1.16e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 183 SITFQNVTFSYPCRpgfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLrGQV 262
Cdd:PRK11231   2 TLRTENLTVGYGTK---RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQL-ARR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 263 IGFISQEPVlfattIMENIR---------------FGKLDASDEEVYTAAREANAhefISSFPDgystvvgERGTTLSGG 327
Cdd:PRK11231  78 LALLPQHHL-----TPEGITvrelvaygrspwlslWGRLSAEDNARVNQAMEQTR---INHLAD-------RRLTDLSGG 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 328 QKQRLAIARALIKQPTVLILDEATSALD----AESERVVQEaldRASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEA 402
Cdd:PRK11231 143 QRQRAFLAMVLAQDTPVVLLDEPTTYLDinhqVELMRLMRE---LNTQGKTVVTVLHDLNQAsRYCDHLVVLANGHVMAQ 219

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 755511082 403 GTHEELLKKgglysELIRRQ-TLDASLTSTPPAEKP 437
Cdd:PRK11231 220 GTPEEVMTP-----GLLRTVfDVEAEIHPEPVSGTP 250

ABC_6TM_Pgp_ABCB1_D1_like

cd18577

Six-transmembrane helical domain 1 (TMD1) of P-glycoprotein 1 (Pgp) and related proteins; ...

3-157

1.39e-25

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: 105.63 E-value: 1.39e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   3 SPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELEscccKAEE 82
Cdd:cd18577  146 SWKLTLVLLATLPLIAIVGGIMGKLLSKYTKKEQEAYAKAGSIAEEALSSIRTVKAFGGEEKEIKRYSKALE----KARK 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  83 LGRGIALFQGLSNIAFNCMVLGT----LFIGGSLVAGQQLKGGD----LMSFLVASQTVQRSMASLSVLfgqvVRGLSAG 154
Cdd:cd18577  222 AGIKKGLVSGLGLGLLFFIIFAMyalaFWYGSRLVRDGEISPGDvltvFFAVLIGAFSLGQIAPNLQAF----AKARAAA 297


                 ...
gi 755511082 155 ARV 157
Cdd:cd18577  298 AKI 300

hmuV

PRK13548

hemin importer ATP-binding subunit; Provisional

187-421

1.53e-25

hemin importer ATP-binding subunit; Provisional

Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 104.85 E-value: 1.53e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 187 QNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPsWLRGQVIGFI 266
Cdd:PRK13548   6 RNLSVRLGGRT---LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSP-AELARRRAVL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 267 SQEPVL-FATTIMENIRFGKL------DASDEEVYTAAREANAHEFISSFpdgYstvvgergTTLSGGQKQRLAIARALI 339
Cdd:PRK13548  82 PQHSSLsFPFTVEEVVAMGRAphglsrAEDDALVAAALAQVDLAHLAGRD---Y--------PQLSGGEQQRVQLARVLA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 340 ------KQPTVLILDEATSALD-AESERVVQEALDRA-SAGRTVLVIAHRLS-TVRAAHSIIVMANGQVCEAGTHEELLK 410
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPTSALDlAHQHHVLRLARQLAhERGLAVIVVLHDLNlAARYADRIVLLHQGRLVADGTPAEVLT 230

                        250
                 ....*....|.
gi 755511082 411 KgglysELIRR 421
Cdd:PRK13548 231 P-----ETLRR 236

YddA

COG4178

ABC-type uncharacterized transport system, permease and ATPase components [General function ...

121-393

1.68e-25

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

Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 109.13 E-value: 1.68e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 121 GDLMsflvasQTVQrsmaslsvLFGQVVRGLS-------------AGA-RVFEYM-ALSPVIPLTGGYCIPNKDIRGSIT 185
Cdd:COG4178  299 GGLM------QAAS--------AFGQVQGALSwfvdnyqslaewrATVdRLAGFEeALEAADALPEAASRIETSEDGALA 364

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 186 FQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTT----VASLlerfYDPEAGSVTLDGHDlRTLnpswlrgq 261
Cdd:COG4178  365 LEDLTLRTP--DGRPLLEDLSLSLKPGERLLITGPSGSGKSTllraIAGL----WPYGSGRIARPAGA-RVL-------- 429

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 262 vigFISQEPVLFATTIMENIRF--GKLDASDEEVYTAAREANAHEFISSFpdgysTVVGERGTTLSGGQKQRLAIARALI 339
Cdd:COG4178  430 ---FLPQRPYLPLGTLREALLYpaTAEAFSDAELREALEAVGLGHLAERL-----DEEADWDQVLSLGEQQRLAFARLLL 501

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755511082 340 KQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRlSTVRAAHSIIV 393
Cdd:COG4178  502 HKPDWLFLDEATSALDEENEAALYQLLREELPGTTVISVGHR-STLAAFHDRVL 554

modC_ABC

TIGR02142

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...

202-414

2.04e-25

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: 106.35 E-value: 2.04e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  202 LKDFTLK----LPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGhdlRTLNPSWLRGQV------IGFISQEPV 271
Cdd:TIGR02142   9 LGDFSLDadftLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG---RTLFDSRKGIFLppekrrIGYVFQEAR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  272 LFA-TTIMENIRFGKLDASDEevYTAAREANAHEFIssfpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEA 350
Cdd:TIGR02142  86 LFPhLSVRGNLRYGMKRARPS--ERRISFERVIELL-----GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEP 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755511082  351 TSALDAESERVVQEALDRASA--GRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEELLKKGGL 414
Cdd:TIGR02142 159 LAALDDPRKYEILPYLERLHAefGIPILYVSHSLQEVlRLADRVVVLEDGRVAAAGPIAEVWASPDL 225

ABC_FtsE

cd03292

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...

184-399

2.71e-25

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: 102.87 E-value: 2.71e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPS---WLRg 260
Cdd:cd03292    1 IEFINVTKTYP--NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipYLR- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 261 QVIGFISQEPVLFAT-TIMENIRFgkldaSDEEVYTAAREANahEFISSFPD--GYSTVVGERGTTLSGGQKQRLAIARA 337
Cdd:cd03292   78 RKIGVVFQDFRLLPDrNVYENVAF-----ALEVTGVPPREIR--KRVPAALElvGLSHKHRALPAELSGGEQQRVAIARA 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755511082 338 LIKQPTVLILDEATSALDAESERVVQEALDRAS-AGRTVLVIAHRLSTV-RAAHSIIVMANGQV 399
Cdd:cd03292  151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKINkAGTTVVVATHAKELVdTTRHRVIALERGKL 214

cbiO

PRK13634

cobalt transporter ATP-binding subunit; Provisional

184-412

4.05e-25

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 104.33 E-value: 4.05e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPGFN--VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDL------RTLNP 255
Cdd:PRK13634   3 ITFQKVEHRYQYKTPFErrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkknKKLKP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 256 swLRGQV-IGFISQEPVLFATTIMENIRFGKLD--ASDEEVYTAAREANA-----HEFISSFPdgystvvgergTTLSGG 327
Cdd:PRK13634  83 --LRKKVgIVFQFPEHQLFEETVEKDICFGPMNfgVSEEDAKQKAREMIElvglpEELLARSP-----------FELSGG 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 328 QKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGT 404
Cdd:PRK13634 150 QMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKlhKEKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQGT 229


                 ....*...
gi 755511082 405 HEELLKKG 412
Cdd:PRK13634 230 PREIFADP 237

MalK

COG3839

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

182-408

6.19e-25

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

Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 105.16 E-value: 6.19e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 182 GSITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTvasLLeR----FYDPEAGSVTLDGHDLRTLNPSw 257
Cdd:COG3839    2 ASLELENVSKSYG---GVEALKDIDLDIEDGEFLVLLGPSGCGKST---LL-RmiagLEDPTSGEILIGGRDVTDLPPK- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 258 LRGqvIGFISQEPVLF-ATTIMENIRFG----KLDAS--DEEVYTAAREANAHEFISSFPDgystvvgergtTLSGGQKQ 330
Cdd:COG3839   74 DRN--IAMVFQSYALYpHMTVYENIAFPlklrKVPKAeiDRRVREAAELLGLEDLLDRKPK-----------QLSGGQRQ 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 331 RLAIARALIKQPTVLILDEATSALDAESeRV--------VQEALdrasaGRTVLVIAHRLstVRA---AHSIIVMANGQV 399
Cdd:COG3839  141 RVALGRALVREPKVFLLDEPLSNLDAKL-RVemraeikrLHRRL-----GTTTIYVTHDQ--VEAmtlADRIAVMNDGRI 212


                 ....*....
gi 755511082 400 CEAGTHEEL 408
Cdd:COG3839  213 QQVGTPEEL 221

cbiO

PRK13637

energy-coupling factor transporter ATPase;

183-410

7.42e-25

energy-coupling factor transporter ATPase;

Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 103.59 E-value: 7.42e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 183 SITFQNVTFSYPCRPGFN--VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDL--RTLNPSWL 258
Cdd:PRK13637   2 SIKIENLTHIYMEGTPFEkkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdKKVKLSDI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 259 RGQViGFISQEP--VLFATTIMENIRFG--KLDASDEEVYTAAREANAHEFISsfpdgYSTVVGERGTTLSGGQKQRLAI 334
Cdd:PRK13637  82 RKKV-GLVFQYPeyQLFEETIEKDIAFGpiNLGLSEEEIENRVKRAMNIVGLD-----YEDYKDKSPFELSGGQKRRVAI 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 335 ARALIKQPTVLILDEATSALDAESErvvQEALDRASA-----GRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEEL 408
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGR---DEILNKIKElhkeyNMTIILVSHSMEDVaKLADRIIVMNKGKCELQGTPREV 232


                 ..
gi 755511082 409 LK 410
Cdd:PRK13637 233 FK 234

ABCC_SUR1_N

cd03290

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...

197-397

8.07e-25

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

Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 101.64 E-value: 8.07e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 197 PGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSV----TLDGHDLRTLNPSWLRGQViGFISQEPVL 272
Cdd:cd03290   12 SGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVhwsnKNESEPSFEATRSRNRYSV-AYAAQKPWL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 273 FATTIMENIRFGKldASDEEVYTAAREA-NAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEAT 351
Cdd:cd03290   91 LNATVEENITFGS--PFNKQRYKAVTDAcSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 755511082 352 SALDAE-SERVVQEALDR--ASAGRTVLVIAHRLSTVRAAHSIIVMANG 397
Cdd:cd03290  169 SALDIHlSDHLMQEGILKflQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217

ABC_ModC_molybdenum_transporter

cd03297

ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...

202-403

8.14e-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: 101.60 E-value: 8.14e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 202 LKDFTLKLP---SGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGhdlRTLN--------PSWLRGqvIGFISQEP 270
Cdd:cd03297   10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG---TVLFdsrkkinlPPQQRK--IGLVFQQY 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 271 VLFA-TTIMENIRFGKLDASDEEvytaaREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDE 349
Cdd:cd03297   85 ALFPhLNVRENLAFGLKRKRNRE-----DRISVDELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDE 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755511082 350 ATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAG 403
Cdd:cd03297  158 PFSALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214

glnQ

PRK09493

glutamine ABC transporter ATP-binding protein GlnQ;

184-409

8.90e-25

glutamine ABC transporter ATP-binding protein GlnQ;

Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 102.09 E-value: 8.90e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLR--TLNPSWLRgQ 261
Cdd:PRK09493   2 IEFKNVSKHFGPTQ---VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNdpKVDERLIR-Q 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 262 VIGFISQEPVLFA-TTIMENIRFGKLD---ASDEEVYTAAREANAHEFISSFPDGYSTvvgergtTLSGGQKQRLAIARA 337
Cdd:PRK09493  78 EAGMVFQQFYLFPhLTALENVMFGPLRvrgASKEEAEKQARELLAKVGLAERAHHYPS-------ELSGGQQQRVAIARA 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755511082 338 LIKQPTVLILDEATSALDAE-SERVVQEALDRASAGRTVLVIAHRLSTVRAAHS-IIVMANGQVCEAGTHEELL 409
Cdd:PRK09493 151 LAVKPKLMLFDEPTSALDPElRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASrLIFIDKGRIAEDGDPQVLI 224

cbiO

PRK13640

energy-coupling factor transporter ATPase;

184-429

1.04e-24

energy-coupling factor transporter ATPase;

Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 102.96 E-value: 1.04e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPGfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGS---VTLDGHDLrTLNPSWLRG 260
Cdd:PRK13640   6 VEFKHVSFTYPDSKK-PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITL-TAKTVWDIR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 261 QVIGFISQEP--VLFATTIMENIRFG--KLDASDEEVYTAAREANAH----EFISSFPdgystvvgergTTLSGGQKQRL 332
Cdd:PRK13640  84 EKVGIVFQNPdnQFVGATVGDDVAFGleNRAVPRPEMIKIVRDVLADvgmlDYIDSEP-----------ANLSGGQKQRV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 333 AIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLK 410
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRklKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEIFS 232

                        250
                 ....*....|....*....
gi 755511082 411 KgglySELIRRQTLDASLT 429
Cdd:PRK13640 233 K----VEMLKEIGLDIPFV 247

ArtP

COG4161

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

183-406

1.12e-24

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

Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 102.01 E-value: 1.12e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 183 SITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTT---VASLLERfydPEAGSVTLDGHDL---RTLNPS 256
Cdd:COG4161    2 SIQLKNINCFYG---SHQALFDINLECPSGETLVLLGPSGAGKSSllrVLNLLET---PDSGQLNIAGHQFdfsQKPSEK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 257 ---WLRGQViGFISQE----PVLfatTIMENI--------RFGKLDASDEEVYTAAReANAHEFISSFPdgystvvgerg 321
Cdd:COG4161   76 airLLRQKV-GMVFQQynlwPHL---TVMENLieapckvlGLSKEQAREKAMKLLAR-LRLTDKADRFP----------- 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 322 TTLSGGQKQRLAIARALIKQPTVLILDEATSALDAE-SERVVQEALDRASAGRTVLVIAHRLSTVR-AAHSIIVMANGQV 399
Cdd:COG4161  140 LHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQVVEIIRELSQTGITQVIVTHEVEFARkVASQVVYMEKGRI 219


                 ....*..
gi 755511082 400 CEAGTHE 406
Cdd:COG4161  220 IEQGDAS 226

cbiO

PRK13644

energy-coupling factor transporter ATPase;

184-409

1.29e-24

energy-coupling factor transporter ATPase;

Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 102.76 E-value: 1.29e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDlrTLNPSWLRG--Q 261
Cdd:PRK13644   2 IRLENVSYSYP--DGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID--TGDFSKLQGirK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 262 VIGFISQEP--VLFATTIMENIRFGKLDAS------DEEVYTAAREANAHEFISSFPdgystvvgergTTLSGGQKQRLA 333
Cdd:PRK13644  78 LVGIVFQNPetQFVGRTVEEDLAFGPENLClppieiRKRVDRALAEIGLEKYRHRSP-----------KTLSGGQGQCVA 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755511082 334 IARALIKQPTVLILDEATSALDAESERVVQEALDRA-SAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELL 409
Cdd:PRK13644 147 LAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEELHDADRIIVMDRGKIVLEGEPENVL 223

ABC_MalK_N

cd03301

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

184-403

1.33e-24

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: 100.79 E-value: 1.33e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSwLRGqvI 263
Cdd:cd03301    1 VELENVTKRFG---NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK-DRD--I 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEPVLFA-TTIMENIRFG-KL-----DASDEEVYTAAREANAHEFISSFPdgystvvgergTTLSGGQKQRLAIAR 336
Cdd:cd03301   75 AMVFQNYALYPhMTVYDNIAFGlKLrkvpkDEIDERVREVAELLQIEHLLDRKP-----------KQLSGGQRQRVALGR 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755511082 337 ALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHrlSTVRA---AHSIIVMANGQVCEAG 403
Cdd:cd03301  144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKRlqQRLGTTTIYVTH--DQVEAmtmADRIAVMNDGQIQQIG 213

SufC

COG0396

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...

201-412

2.78e-24

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

Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 100.91 E-value: 2.78e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 201 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLL---ERfYDPEAGSVTLDGHDLRTLNPS--WLRGQVIGFisQEPV---- 271
Cdd:COG0396   15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmghPK-YEVTSGSILLDGEDILELSPDerARAGIFLAF--QYPVeipg 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 272 ----LFATTIMENIRFGKLDASD--EEVYTAAREAN-AHEFISSFpdgystvVGErgtTLSGGQKQRLAIARALIKQPTV 344
Cdd:COG0396   92 vsvsNFLRTALNARRGEELSAREflKLLKEKMKELGlDEDFLDRY-------VNE---GFSGGEKKRNEILQMLLLEPKL 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755511082 345 LILDEATSALDAESERVVQEALDR-ASAGRTVLVIAH--RLSTVRAAHSIIVMANGQVCEAGTHE---ELLKKG 412
Cdd:COG0396  162 AILDETDSGLDIDALRIVAEGVNKlRSPDRGILIITHyqRILDYIKPDFVHVLVDGRIVKSGGKElalELEEEG 235

cbiO

PRK13639

cobalt transporter ATP-binding subunit; Provisional

188-424

3.25e-24

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 101.31 E-value: 3.25e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 188 NVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRG-QVIGFI 266
Cdd:PRK13639   6 DLKYSYP--DGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVrKTVGIV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 267 SQEP--VLFATTIMENIRFGKLDA--SDEEVYTAAREANAHEFISSFPDgystvvgERGTTLSGGQKQRLAIARALIKQP 342
Cdd:PRK13639  84 FQNPddQLFAPTVEEDVAFGPLNLglSKEEVEKRVKEALKAVGMEGFEN-------KPPHHLSGGQKKRVAIAGILAMKP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 343 TVLILDEATSALDAESERVVQEAL-DRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEELLKKgglySELIR 420
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLyDLNKEGITIIISTHDVDLVPVyADKVYVMSDGKIIKEGTPKEVFSD----IETIR 232


                 ....
gi 755511082 421 RQTL 424
Cdd:PRK13639 233 KANL 236

PRK11264

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

198-409

3.77e-24

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

Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 100.59 E-value: 3.77e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 198 GFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSV-----TLDGHdlRTLNPSW-----LRGQViGFIS 267
Cdd:PRK11264  15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTA--RSLSQQKglirqLRQHV-GFVF 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 268 QEPVLFA-TTIMENIRFGKL---DASDEEVYTAAREANAHEFISSFPDGYSTvvgergtTLSGGQKQRLAIARALIKQPT 343
Cdd:PRK11264  92 QNFNLFPhRTVLENIIEGPVivkGEPKEEATARARELLAKVGLAGKETSYPR-------RLSGGQQQRVAIARALAMRPE 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755511082 344 VLILDEATSALDAEserVVQEALDR----ASAGRTVLVIAHRLSTVR-AAHSIIVMANGQVCEAGTHEELL 409
Cdd:PRK11264 165 VILFDEPTSALDPE---LVGEVLNTirqlAQEKRTMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAKALF 232

PRK14243

phosphate transporter ATP-binding protein; Provisional

202-382

4.40e-24

phosphate transporter ATP-binding protein; Provisional

Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 101.01 E-value: 4.40e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 202 LKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYD--PEA---GSVTLDGHDL--RTLNPSWLRGQvIGFISQEPVLFA 274
Cdd:PRK14243  26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLyaPDVDPVEVRRR-IGMVFQKPNPFP 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 275 TTIMENIRFG------KLDAsDEEVYTAAREAnahefisSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILD 348
Cdd:PRK14243 105 KSIYDNIAYGaringyKGDM-DELVERSLRQA-------ALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176

                        170       180       190
                 ....*....|....*....|....*....|....
gi 755511082 349 EATSALDAESERVVQEALDRASAGRTVLVIAHRL 382
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQYTIIIVTHNM 210

YejF

COG4172

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...

199-409

5.85e-24

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: 104.38 E-value: 5.85e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 199 FNVLKDFTLKLPSGKIVALVGQSGGGKT----TVASLLERFYDPEAGSVTLDGHDLRTLNPSWL---RGQVIGFISQEPV 271
Cdd:COG4172   23 VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERELrriRGNRIAMIFQEPM 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 272 -----LFatTI----MENIRFgKLDASDEEVYTAAREA-------NAHEFISSFPdgystvvgergTTLSGGQKQRLAIA 335
Cdd:COG4172  103 tslnpLH--TIgkqiAEVLRL-HRGLSGAAARARALELlervgipDPERRLDAYP-----------HQLSGGQRQRVMIA 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 336 RALIKQPTVLILDEATSALDAeserVVQ-EALD-----RASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEEL 408
Cdd:COG4172  169 MALANEPDLLIADEPTTALDV----TVQaQILDllkdlQRELGMALLLITHDLGVVRRfADRVAVMRQGEIVEQGPTAEL 244


                 .
gi 755511082 409 L 409
Cdd:COG4172  245 F 245

TauB

COG4525

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

184-380

6.06e-24

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

Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 100.32 E-value: 6.06e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYP-CRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTlnPSWLRGQV 262
Cdd:COG4525    4 LTVRHVSVRYPgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG--PGADRGVV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 263 IgfisQEPVLFA-TTIMENIRFG-KLDAsdeeVYTAAREANAHEFISsfpdgystVVGERGT------TLSGGQKQRLAI 334
Cdd:COG4525   82 F----QKDALLPwLNVLDNVAFGlRLRG----VPKAERRARAEELLA--------LVGLADFarrriwQLSGGMRQRVGI 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 755511082 335 ARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAH 380
Cdd:COG4525  146 ARALAADPRFLLMDEPFGALDALTREQMQELLLDvwQRTGKGVFLITH 193

cbiO

PRK13641

energy-coupling factor transporter ATPase;

183-430

9.41e-24

energy-coupling factor transporter ATPase;

Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 100.29 E-value: 9.41e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 183 SITFQNVTFSYPcrPGFNV----LKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLrTLNPS-- 256
Cdd:PRK13641   2 SIKFENVDYIYS--PGTPMekkgLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHI-TPETGnk 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 257 ---WLRGQViGFISQ--EPVLFATTIMENIRFGKLD--ASDEEvytaAREAnAHEFISSFpdGYSTVVGERGT-TLSGGQ 328
Cdd:PRK13641  79 nlkKLRKKV-SLVFQfpEAQLFENTVLKDVEFGPKNfgFSEDE----AKEK-ALKWLKKV--GLSEDLISKSPfELSGGQ 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 329 KQRLAIARALIKQPTVLILDEATSALDAES-ERVVQEALDRASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHE 406
Cdd:PRK13641 151 MRRVAIAGVMAYEPEILCLDEPAAGLDPEGrKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKHASPK 230

                        250       260
                 ....*....|....*....|....
gi 755511082 407 ELLKKgglySELIRRQTLDASLTS 430
Cdd:PRK13641 231 EIFSD----KEWLKKHYLDEPATS 250

ABC_NatA_sodium_exporter

cd03266

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...

184-403

1.00e-23

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.

Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 98.59 E-value: 1.00e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSY-PCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTlNPSWLRgQV 262
Cdd:cd03266    2 ITADALTKRFrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEAR-RR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 263 IGFISQEPVLFA-TTIMENIR-FGKLDASDEEVYTAAREanahEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIK 340
Cdd:cd03266   80 LGFVSDSTGLYDrLTARENLEyFAGLYGLKGDELTARLE----ELADRL--GMEELLDRRVGGFSTGMRQKVAIARALVH 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755511082 341 QPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAG 403
Cdd:cd03266  154 DPPVLLLDEPTTGLDVMATRALREFIRQlRALGKCILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218

ABCC_CFTR1

cd03291

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...

188-408

1.06e-23

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: 100.32 E-value: 1.06e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 188 NVTFSYPCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHdlrtlnpswlrgqvIGFIS 267
Cdd:cd03291   39 NLFFSNLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------------ISFSS 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 268 QEPVLFATTIMENIRFGKldASDEEVYTAAREA-NAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLI 346
Cdd:cd03291  105 QFSWIMPGTIKENIIFGV--SYDEYRYKSVVKAcQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL 182

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755511082 347 LDEATSALDAESERVVQEA-LDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEEL 408
Cdd:cd03291  183 LDSPFGYLDVFTEKEIFEScVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSEL 245

ABCC_CFTR2

cd03289

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...

182-419

1.11e-23

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

Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 99.93 E-value: 1.11e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 182 GSITFQNVTFSYpCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEaGSVTLDGHDLRTLNPSWLRgQ 261
Cdd:cd03289    1 GQMTVKDLTAKY-TEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWR-K 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 262 VIGFISQEPVLFATTIMENIR-FGKLdaSDEEVYTAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIK 340
Cdd:cd03289   78 AFGVIPQKVFIFSGTFRKNLDpYGKW--SDEEIWKVAEEVGLKSVIEQFPGQLDFVLVDGGCVLSHGHKQLMCLARSVLS 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755511082 341 QPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELI 419
Cdd:cd03289  156 KAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLNEKSHFKQAI 234

Uup

COG0488

ATPase components of ABC transporters with duplicated ATPase domains [General function ...

184-399

1.12e-23

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

Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.22 E-value: 1.12e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLdGHDLRtlnpswlrgqvI 263
Cdd:COG0488  316 LELEGLSKSYGDKT---LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK-----------I 380

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEPVLFAT--TIMENIRfgkldasdeEVYTAAREANAHEFISSF---PDGYSTVVGergtTLSGGQKQRLAIARAL 338
Cdd:COG0488  381 GYFDQHQEELDPdkTVLDELR---------DGAPGGTEQEVRGYLGRFlfsGDDAFKPVG----VLSGGEKARLALAKLL 447

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755511082 339 IKQPTVLILDEATSALDAESERVVQEALDrASAGrTVLVIAH-R--LSTVraAHSIIVMANGQV 399
Cdd:COG0488  448 LSPPNVLLLDEPTNHLDIETLEALEEALD-DFPG-TVLLVSHdRyfLDRV--ATRILEFEDGGV 507

ModC

COG4148

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

196-409

1.39e-23

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: 101.33 E-value: 1.39e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 196 RPGFNVlkDFTLKLPSGKIVALVGQSGGGKTTVASL---LERfydPEAGSVTLDGHDL----RTLN-PSWLRGqvIGFIS 267
Cdd:COG4148   11 RGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAiagLER---PDSGRIRLGGEVLqdsaRGIFlPPHRRR--IGYVF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 268 QEPVLFAT-TIMENIRFGkldasdeevYTAAREANAHefiSSFPD-----GYSTVVGERGTTLSGGQKQRLAIARALIKQ 341
Cdd:COG4148   84 QEARLFPHlSVRGNLLYG---------RKRAPRAERR---ISFDEvvellGIGHLLDRRPATLSGGERQRVAIGRALLSS 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755511082 342 PTVLILDEATSALDAES--------ERVvqealdRASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEELL 409
Cdd:COG4148  152 PRLLLMDEPLAALDLARkaeilpylERL------RDELDIPILYVSHSLDEVaRLADHVVLLEQGRVVASGPLAEVL 222

PRK13633

energy-coupling factor transporter ATPase;

184-411

2.76e-23

energy-coupling factor transporter ATPase;

Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 99.01 E-value: 2.76e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPGFN---VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRG 260
Cdd:PRK13633   5 IKCKNVSYKYESNEESTeklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIR 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 261 QVIGFISQEP--VLFATTIMENIRFG--KLDASDEEVYTAAREA----NAHEFISSFPDgystvvgergtTLSGGQKQRL 332
Cdd:PRK13633  85 NKAGMVFQNPdnQIVATIVEEDVAFGpeNLGIPPEEIRERVDESlkkvGMYEYRRHAPH-----------LLSGGQKQRV 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 333 AIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLK 410
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKkyGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPKEIFK 233


                 .
gi 755511082 411 K 411
Cdd:PRK13633 234 E 234

artP

PRK11124

arginine transporter ATP-binding subunit; Provisional

183-406

3.08e-23

arginine transporter ATP-binding subunit; Provisional

Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 97.78 E-value: 3.08e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 183 SITFQNVTFSYpcrpGFN-VLKDFTLKLPSGKIVALVGQSGGGKTT---VASLLERfydPEAGSVTLDGH--DL-RTLNP 255
Cdd:PRK11124   2 SIQLNGINCFY----GAHqALFDITLDCPQGETLVLLGPSGAGKSSllrVLNLLEM---PRSGTLNIAGNhfDFsKTPSD 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 256 SWLRG--QVIGFISQEPVLFA-TTIMEN-----IRFGKLdaSDEEVYTAAREANAH----EFISSFPdgystvvgergTT 323
Cdd:PRK11124  75 KAIRElrRNVGMVFQQYNLWPhLTVQQNlieapCRVLGL--SKDQALARAEKLLERlrlkPYADRFP-----------LH 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 324 LSGGQKQRLAIARALIKQPTVLILDEATSALDAE-SERVVQEALDRASAGRTVLVIAHRLSTVR-AAHSIIVMANGQVCE 401
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEiTAQIVSIIRELAETGITQVIVTHEVEVARkTASRVVYMENGHIVE 221


                 ....*
gi 755511082 402 AGTHE 406
Cdd:PRK11124 222 QGDAS 226

PRK10070

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

202-409

3.46e-23

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

Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 100.88 E-value: 3.46e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 202 LKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRG---QVIGFISQEPVLFA-TTI 277
Cdd:PRK10070  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREvrrKKIAMVFQSFALMPhMTV 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 278 MENIRFG------KLDASDEEVYTAAREANAHEFISSFPDgystvvgergtTLSGGQKQRLAIARALIKQPTVLILDEAT 351
Cdd:PRK10070 124 LDNTAFGmelagiNAEERREKALDALRQVGLENYAHSYPD-----------ELSGGMRQRVGLARALAINPDILLMDEAF 192

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755511082 352 SALDAESERVVQEALDRASAG--RTVLVIAHRL-STVRAAHSIIVMANGQVCEAGTHEELL 409
Cdd:PRK10070 193 SALDPLIRTEMQDELVKLQAKhqRTIVFISHDLdEAMRIGDRIAIMQNGEVVQVGTPDEIL 253

CeuD

COG4604

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

184-409

4.23e-23

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

Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 97.85 E-value: 4.23e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLnPSWLRGQVI 263
Cdd:COG4604    2 IEIKNVSKRYGGKV---VLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATT-PSRELAKRL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEPVlFAT--TIMENIRFG-------KLDASDEEVYTAA-----REANAHEFISsfpdgystvvgergtTLSGGQK 329
Cdd:COG4604   78 AILRQENH-INSrlTVRELVAFGrfpyskgRLTAEDREIIDEAiayldLEDLADRYLD---------------ELSGGQR 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 330 QRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRAS--AGRTVLVIAHRLSTVrAAHS--IIVMANGQVCEAGTH 405
Cdd:COG4604  142 QRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLAdeLGKTVVIVLHDINFA-SCYAdhIVAMKDGRVVAQGTP 220


                 ....
gi 755511082 406 EELL 409
Cdd:COG4604  221 EEII 224

ABC_BcrA_bacitracin_resist

cd03268

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...

184-403

4.42e-23

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.

Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 96.52 E-value: 4.42e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRpgfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWlrgQVI 263
Cdd:cd03268    1 LKTNDLTKTYGKK---RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL---RRI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEPVLFAT-TIMENIRFGKLdasdeevYTAAREANAHEFISsfpdgystVVGERGT------TLSGGQKQRLAIAR 336
Cdd:cd03268   75 GALIEAPGFYPNlTARENLRLLAR-------LLGIRKKRIDEVLD--------VVGLKDSakkkvkGFSLGMKQRLGIAL 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755511082 337 ALIKQPTVLILDEATSALDAESERVVQEAL-DRASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAG 403
Cdd:cd03268  140 ALLGNPDLLILDEPTNGLDPDGIKELRELIlSLRDQGITVLISSHLLSEIqKVADRIGIINKGKLIEEG 208

thiQ

PRK10771

thiamine ABC transporter ATP-binding protein ThiQ;

184-409

5.84e-23

thiamine ABC transporter ATP-binding protein ThiQ;

Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 96.96 E-value: 5.84e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSY---PCRpgfnvlkdFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSwLRG 260
Cdd:PRK10771   2 LKLTDITWLYhhlPMR--------FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS-RRP 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 261 QVIGFisQEPVLFA-TTIMENIRFG-----KLDASD-EEVYTAAREANAHEFISSFPdgystvvgergTTLSGGQKQRLA 333
Cdd:PRK10771  73 VSMLF--QENNLFShLTVAQNIGLGlnpglKLNAAQrEKLHAIARQMGIEDLLARLP-----------GQLSGGQRQRVA 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 334 IARALIKQPTVLILDEATSALD----AESERVVQEALDRASAgrTVLVIAHRLS-TVRAAHSIIVMANGQVCEAGTHEEL 408
Cdd:PRK10771 140 LARCLVREQPILLLDEPFSALDpalrQEMLTLVSQVCQERQL--TLLMVSHSLEdAARIAPRSLVVADGRIAWDGPTDEL 217


                 .
gi 755511082 409 L 409
Cdd:PRK10771 218 L 218

ABC_6TM_exporters

cd07346

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

2-157

6.49e-23

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: 98.01 E-value: 6.49e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   2 LSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAE 81
Cdd:cd07346  137 LNWKLTLVALLLLPLYVLILRYFRRRIRKASREVRESLAELSAFLQESLSGIRVVKAFAAEEREIERFREANRDLRDANL 216

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755511082  82 ELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 157
Cdd:cd07346  217 RAARLSALFSPLIGLLTALGTALVLLYGGYLVLQGSLTIGELVAFLAYLGMLFGPIQRLANLYNQLQQALASLERI 292

PhnL

COG4778

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...

201-398

7.35e-23

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: 96.35 E-value: 7.35e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 201 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGH----DLRTLNPS---WLRGQVIGFISQepvlF 273
Cdd:COG4778   26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQASPReilALRRRTIGYVSQ----F 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 274 ATTI---------MENIRfgKLDASDEEVYTAAREANAH-----EFISSFPdgystvvgergTTLSGGQKQRLAIARALI 339
Cdd:COG4778  102 LRVIprvsaldvvAEPLL--ERGVDREEARARARELLARlnlpeRLWDLPP-----------ATFSGGEQQRVNIARGFI 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755511082 340 KQPTVLILDEATSALDAESERVVQEALDRA-SAGRTVLVIAHRLSTVRA-AHSIIVMANGQ 398
Cdd:COG4778  169 ADPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVREAvADRVVDVTPFS 229

CFTR_protein

TIGR01271

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...

155-419

8.05e-23

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: 101.91 E-value: 8.05e-23

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   155 ARVFEYMALSPVIPLTGG----------YCIPNKDIR------GSITFQNVTFSYpCRPGFNVLKDFTLKLPSGKIVALV 218
Cdd:TIGR01271 1173 SRVFKFIDLPQEEPRPSGgggkyqlstvLVIENPHAQkcwpsgGQMDVQGLTAKY-TEAGRAVLQDLSFSVEGGQRVGLL 1251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   219 GQSGGGKTTVASLLERFYDPEaGSVTLDGHDLRTLNPSWLRgQVIGFISQEPVLFATTIMENirfgkLDA----SDEEVY 294
Cdd:TIGR01271 1252 GRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWR-KAFGVIPQKVFIFSGTFRKN-----LDPyeqwSDEEIW 1324

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   295 TAAREANAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRT 374
Cdd:TIGR01271 1325 KVAEEVGLKSVIEQFPDKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCT 1404

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 755511082   375 VLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGGLYSELI 419
Cdd:TIGR01271 1405 VILSEHRVEALLECQQFLVIEGSSVKQYDSIQKLLNETSLFKQAM 1449

LptB

COG1137

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...

187-421

8.25e-23

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

Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 96.64 E-value: 8.25e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 187 QNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVasllerFY------DPEAGSVTLDGHDLRTLnPSWLRG 260
Cdd:COG1137    7 ENLVKSYGKRT---VVKDVSLEVNQGEIVGLLGPNGAGKTTT------FYmivglvKPDSGRIFLDGEDITHL-PMHKRA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 261 QV-IGFISQEPVLFAT-TIMENIR----FGKLDAsdeevytAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAI 334
Cdd:COG1137   77 RLgIGYLPQEASIFRKlTVEDNILavleLRKLSK-------KEREERLEELLEEF--GITHLRKSKAYSLSGGERRRVEI 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 335 ARALIKQPTVLILDEATSALD----AESERVVQEALDRasaGRTVLVIAHRlstVRAAHSII----VMANGQVCEAGTHE 406
Cdd:COG1137  148 ARALATNPKFILLDEPFAGVDpiavADIQKIIRHLKER---GIGVLITDHN---VRETLGICdrayIISEGKVLAEGTPE 221

                        250
                 ....*....|....*
gi 755511082 407 ELLKkgglySELIRR 421
Cdd:COG1137  222 EILN-----NPLVRK 231

CFTR_protein

TIGR01271

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...

176-419

1.21e-22

Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 101.53 E-value: 1.21e-22

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   176 PNKDirGSITFQNvtFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHdlrtlnp 255
Cdd:TIGR01271  423 PNGD--DGLFFSN--FSLYVTP---VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR------- 488

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   256 swlrgqvIGFISQEPVLFATTIMENIRFGKldASDEEVYTAAREA-NAHEFISSFPDGYSTVVGERGTTLSGGQKQRLAI 334
Cdd:TIGR01271  489 -------ISFSPQTSWIMPGTIKDNIIFGL--SYDEYRYTSVIKAcQLEEDIALFPEKDKTVLGEGGITLSGGQRARISL 559

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   335 ARALIKQPTVLILDEATSALDAESER-VVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLKKGG 413
Cdd:TIGR01271  560 ARAVYKDADLYLLDSPFTHLDVVTEKeIFESCLCKLMSNKTRILVTSKLEHLKKADKILLLHEGVCYFYGTFSELQAKRP 639


                   ....*.
gi 755511082   414 LYSELI 419
Cdd:TIGR01271  640 DFSSLL 645

PRK10247

putative ABC transporter ATP-binding protein YbbL; Provisional

201-368

1.36e-22

putative ABC transporter ATP-binding protein YbbL; Provisional

Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 95.55 E-value: 1.36e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 201 VLKDFTLKLPSGKIVALVGQSGGGKTT----VASLLErfydPEAGSVTLDGHDLRTLNPSWLRGQViGFISQEPVLFATT 276
Cdd:PRK10247  22 ILNNISFSLRAGEFKLITGPSGCGKSTllkiVASLIS----PTSGTLLFEGEDISTLKPEIYRQQV-SYCAQTPTLFGDT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 277 IMENIRFG---KLDASDEEVYTAareanaheFISSF--PDgysTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEAT 351
Cdd:PRK10247  97 VYDNLIFPwqiRNQQPDPAIFLD--------DLERFalPD---TILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165

                        170
                 ....*....|....*..
gi 755511082 352 SALDAESERVVQEALDR 368
Cdd:PRK10247 166 SALDESNKHNVNEIIHR 182

fbpC

PRK11432

ferric ABC transporter ATP-binding protein;

187-411

1.63e-22

ferric ABC transporter ATP-binding protein;

Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 98.25 E-value: 1.63e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 187 QNVTFSYpcrpGFN-VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLrtlNPSWLRGQVIGF 265
Cdd:PRK11432  10 KNITKRF----GSNtVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV---THRSIQQRDICM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 266 ISQEPVLFA-TTIMENIRFG--KLDASDEEVYTAAREANAHEFISSFPDGYstvVGErgttLSGGQKQRLAIARALIKQP 342
Cdd:PRK11432  83 VFQSYALFPhMSLGENVGYGlkMLGVPKEERKQRVKEALELVDLAGFEDRY---VDQ----ISGGQQQRVALARALILKP 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755511082 343 TVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEELLKK 411
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRelQQQFNITSLYVTHDQSEAFAvSDTVIVMNKGKIMQIGSPQELYRQ 227

YbbA

COG4181

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...

184-404

1.80e-22

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: 95.58 E-value: 1.80e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPG-FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASL---LERfydPEAGSVTLDGHDLRTLNP---S 256
Cdd:COG4181    9 IELRGLTKTVGTGAGeLTILKGISLEVEAGESVAIVGASGSGKSTLLGLlagLDR---PTSGTVRLAGQDLFALDEdarA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 257 WLRGQVIGFISQEPVLFAT-TIMENIRFGKLDASDEEVYTAAREANAhefissfpdgysTV-VGERGT----TLSGGQKQ 330
Cdd:COG4181   86 RLRARHVGFVFQSFQLLPTlTALENVMLPLELAGRRDARARARALLE------------RVgLGHRLDhypaQLSGGEQQ 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755511082 331 RLAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGT 404
Cdd:COG4181  154 RVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFelNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVEDTA 229

cbiO

PRK13642

energy-coupling factor transporter ATPase;

187-409

1.87e-22

energy-coupling factor transporter ATPase;

Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 96.70 E-value: 1.87e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 187 QNVTFSYPCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNpSWLRGQVIGFI 266
Cdd:PRK13642   8 ENLVFKYEKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEN-VWNLRRKIGMV 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 267 SQEP--VLFATTIMENIRFGKLDAS--DEEVYTAAREA----NAHEFISSFPdgystvvgergTTLSGGQKQRLAIARAL 338
Cdd:PRK13642  87 FQNPdnQFVGATVEDDVAFGMENQGipREEMIKRVDEAllavNMLDFKTREP-----------ARLSGGQKQRVAVAGII 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755511082 339 IKQPTVLILDEATSALD----AESERVVQEALDRASAgrTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELL 409
Cdd:PRK13642 156 ALRPEIIILDESTSMLDptgrQEIMRVIHEIKEKYQL--TVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELF 228

dppF

PRK11308

dipeptide transporter ATP-binding subunit; Provisional

205-408

1.99e-22

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 97.34 E-value: 1.99e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 205 FTLKlpSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHD-----------LRT------------LNPSwlrgQ 261
Cdd:PRK11308  36 FTLE--RGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDllkadpeaqklLRQkiqivfqnpygsLNPR----K 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 262 VIGFISQEPVLFATtimenirfgKLDAsdeevytAAREANAHEFISSfpdgystvVGERGT-------TLSGGQKQRLAI 334
Cdd:PRK11308 110 KVGQILEEPLLINT---------SLSA-------AERREKALAMMAK--------VGLRPEhydryphMFSGGQRQRIAI 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 335 ARALIKQPTVLILDEATSALDAESERVV-------QEALdrasaGRTVLVIAHRLSTVR-AAHSIIVMANGQVCEAGTHE 406
Cdd:PRK11308 166 ARALMLDPDVVVADEPVSALDVSVQAQVlnlmmdlQQEL-----GLSYVFISHDLSVVEhIADEVMVMYLGRCVEKGTKE 240


                 ..
gi 755511082 407 EL 408
Cdd:PRK11308 241 QI 242

cbiO

PRK13631

cobalt transporter ATP-binding subunit; Provisional

199-408

2.02e-22

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 97.23 E-value: 2.02e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 199 FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLD----GHDLRTLNPSWLRGQ-----------VI 263
Cdd:PRK13631  39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELITNPYSkkiknfkelrrRV 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEP--VLFATTIMENIRFG-------KLDASDEEVYTAAREANAHEFISSFPDGystvvgergttLSGGQKQRLAI 334
Cdd:PRK13631 119 SMVFQFPeyQLFKDTIEKDIMFGpvalgvkKSEAKKLAKFYLNKMGLDDSYLERSPFG-----------LSGGQKRRVAI 187

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755511082 335 ARALIKQPTVLILDEATSALDAESER-VVQEALDRASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEEL 408
Cdd:PRK13631 188 AGILAIQPEILIFDEPTAGLDPKGEHeMMQLILDAKANNKTVFVITHTMEHVlEVADEVIVMDKGKILKTGTPYEI 263

potA

PRK09452

spermidine/putrescine ABC transporter ATP-binding protein PotA;

184-407

2.40e-22

spermidine/putrescine ABC transporter ATP-binding protein PotA;

Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 98.10 E-value: 2.40e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSwlrgqvi 263
Cdd:PRK09452  15 VELRGISKSFD---GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE------- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 gfisQEPV--------LFA-TTIMENIRFG----KLdaSDEEVYTAAREANAHEFISSFPDgystvvgERGTTLSGGQKQ 330
Cdd:PRK09452  85 ----NRHVntvfqsyaLFPhMTVFENVAFGlrmqKT--PAAEITPRVMEALRMVQLEEFAQ-------RKPHQLSGGQQQ 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 331 RLAIARALIKQPTVLILDEATSALDAESERVVQ---EALDRaSAGRTVLVIAH----RLSTvraAHSIIVMANGQVCEAG 403
Cdd:PRK09452 152 RVAIARAVVNKPKVLLLDESLSALDYKLRKQMQnelKALQR-KLGITFVFVTHdqeeALTM---SDRIVVMRDGRIEQDG 227


                 ....
gi 755511082 404 THEE 407
Cdd:PRK09452 228 TPRE 231

YnjD

COG4136

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...

183-396

3.24e-22

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

Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 94.09 E-value: 3.24e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 183 SITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEA---GSVTLDGHDLRTLNPSwLR 259
Cdd:COG4136    1 MLSLENLTITLGGRP---LLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRLTALPAE-QR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 260 GqvIGFISQEPVLFA-TTIMENIRFG-----KLDASDEEVYTAAREANAHEFISSFPDgystvvgergtTLSGGQKQRLA 333
Cdd:COG4136   77 R--IGILFQDDLLFPhLSVGENLAFAlpptiGRAQRRARVEQALEEAGLAGFADRDPA-----------TLSGGQRARVA 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755511082 334 IARALIKQPTVLILDEATSALDAE-----SERVVQEAldRASAGRTVLViAHRLSTVRAAHSIIVMAN 396
Cdd:COG4136  144 LLRALLAEPRALLLDEPFSKLDAAlraqfREFVFEQI--RQRGIPALLV-THDEEDAPAAGRVLDLGN 208

PRK10851

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;

183-408

3.52e-22

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;

Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 97.08 E-value: 3.52e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 183 SITFQNVTFSYPCRpgfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPswlRGQV 262
Cdd:PRK10851   2 SIEIANIKKSFGRT---QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA---RDRK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 263 IGFISQEPVLFA-TTIMENIRFG-KLDASDEEVYTAAREANAHEFI-----SSFPDGYSTvvgergtTLSGGQKQRLAIA 335
Cdd:PRK10851  76 VGFVFQHYALFRhMTVFDNIAFGlTVLPRRERPNAAAIKAKVTQLLemvqlAHLADRYPA-------QLSGGQKQRVALA 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 336 RALIKQPTVLILDEATSALDAESE-------RVVQEALDRASagrtVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEEL 408
Cdd:PRK10851 149 RALAVEPQILLLDEPFGALDAQVRkelrrwlRQLHEELKFTS----VFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224

ABC_6TM_MsbA_like

cd18552

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

2-157

4.69e-22

Six-transmembrane helical domain of the bacterial ABC lipid flippase MsbA and similar proteins; The bacterial lipid flippase MsbA is found in Gram-negative bacteria and transports lipid A and lipopolysaccharide (LPS) from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. MsbA is also a polyspecific transporter capable of transporting a broad spectrum of drug molecules. Additionally, MsbA exhibits significant sequence similarity to mammalian multidrug resistance (MDR) proteins such as human MDR protein 1 (MDR1) and LmrA from Lactococcus lactis. This subgroup also contains a putative transporter Brevibacillus brevis TycD; the location of the tycD gene within the Tyc (tyrocidine) biosynthesis operon suggests that TycD may play a role in the secretion of the cyclic decapeptide antibiotic tyrocidine. This transmembrane (TM) subunit possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.

Pssm-ID: 349996 [Multi-domain] Cd Length: 292 Bit Score: 95.57 E-value: 4.69e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   2 LSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELEscccKAE 81
Cdd:cd18552  137 LDWKLTLIALVVLPLAALPIRRIGKRLRKISRRSQESMGDLTSVLQETLSGIRVVKAFGAEDYEIKRFRKANE----RLR 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  82 ELGRGIALFQGLSN-----IAFnCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGAR 156
Cdd:cd18552  213 RLSMKIARARALSSplmelLGA-IAIALVLWYGGYQVISGELTPGEFISFITALLLLYQPIKRLSNVNANLQRGLAAAER 291


                 .
gi 755511082 157 V 157
Cdd:cd18552  292 I 292

tauB

PRK11248

taurine ABC transporter ATP-binding subunit;

184-380

5.06e-22

taurine ABC transporter ATP-binding subunit;

Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 94.77 E-value: 5.06e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGhdLRTLNPSWLRGQVI 263
Cdd:PRK11248   2 LQISHLYADYGGKP---ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG--KPVEGPGAERGVVF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 gfiSQEPVLFATTIMENIRFGKLDASdeeVYTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPT 343
Cdd:PRK11248  77 ---QNEGLLPWRNVQDNVAFGLQLAG---VEKMQRLEIAHQMLKKV--GLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 755511082 344 VLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAH 380
Cdd:PRK11248 149 LLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITH 187

ModF

COG1119

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...

184-409

7.09e-22

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: 94.38 E-value: 7.09e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDP-EAGSVTLDGHDLRTLNPSWLRGQv 262
Cdd:COG1119    4 LELRNVTVRRGGKT---ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPtYGNDVRLFGERRGGEDVWELRKR- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 263 IGFISQEpvlFATTIMENIR---------FGKLDASDEevYTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLA 333
Cdd:COG1119   80 IGLVSPA---LQLRFPRDETvldvvlsgfFDSIGLYRE--PTDEQRERARELLELL--GLAHLADRPFGTLSQGEQRRVL 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 334 IARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLV-IAHRLSTVRAA--HsIIVMANGQVCEAGTHEELL 409
Cdd:COG1119  153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVlVTHHVEEIPPGitH-VLLLKDGRVVAAGPKEEVL 231

NupO

COG3845

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...

197-406

8.37e-22

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

Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 97.79 E-value: 8.37e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 197 PGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVIGFISQEPVLFAT- 275
Cdd:COG3845   16 GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDAIALGIGMVHQHFMLVPNl 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 276 TIMENI-------RFGKLDASdeevytAAREAnAHEFISSF-----PDgysTVVGErgttLSGGQKQRLAIARALIKQPT 343
Cdd:COG3845   96 TVAENIvlgleptKGGRLDRK------AARAR-IRELSERYgldvdPD---AKVED----LSVGEQQRVEILKALYRGAR 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755511082 344 VLILDEATSAL-DAESERVVqEALDR-ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVceAGTHE 406
Cdd:COG3845  162 ILILDEPTAVLtPQEADELF-EILRRlAAEGKSIIFITHKLREVMAiADRVTVLRRGKV--VGTVD 224

potG

PRK11607

putrescine ABC transporter ATP-binding subunit PotG;

187-408

8.88e-22

putrescine ABC transporter ATP-binding subunit PotG;

Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 96.44 E-value: 8.88e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 187 QNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLrTLNPSWLRGqvIGFI 266
Cdd:PRK11607  23 RNLTKSFD---GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRP--INMM 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 267 SQEPVLFA-TTIMENIRFG-KLDA-SDEEVYTAARE----ANAHEFISSFPDgystvvgergtTLSGGQKQRLAIARALI 339
Cdd:PRK11607  97 FQSYALFPhMTVEQNIAFGlKQDKlPKAEIASRVNEmlglVHMQEFAKRKPH-----------QLSGGQRQRVALARSLA 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755511082 340 KQPTVLILDEATSALDAE-SERVVQEALD-RASAGRTVLVIAH-RLSTVRAAHSIIVMANGQVCEAGTHEEL 408
Cdd:PRK11607 166 KRPKLLLLDEPMGALDKKlRDRMQLEVVDiLERVGVTCVMVTHdQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237

ABC_YhbG

cd03218

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...

201-421

9.42e-22

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.

Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 93.38 E-value: 9.42e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 201 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLnPSWLRGQV-IGFISQEPVLFAT-TIM 278
Cdd:cd03218   15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL-PMHKRARLgIGYLPQEASIFRKlTVE 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 279 ENIRfgkldASDEEVY--TAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD- 355
Cdd:cd03218   94 ENIL-----AVLEIRGlsKKEREEKLEELLEEF--HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDp 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755511082 356 ---AESERVVQEALDRasaGRTVLVIAHrlsTVRAAHSII----VMANGQVCEAGTHEELLKkgglySELIRR 421
Cdd:cd03218  167 iavQDIQKIIKILKDR---GIGVLITDH---NVRETLSITdrayIIYEGKVLAEGTPEEIAA-----NELVRK 228

ABC_6TM_LmrA_like

cd18551

Six-transmembrane helical domain of the multidrug resistance ABC transporter LmrA and similar ...

2-157

9.72e-22

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: 94.81 E-value: 9.72e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   2 LSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESccckAE 81
Cdd:cd18551  134 LDWVLTLVTLAVVPLAFLIILPLGRRIRKASKRAQDALGELSAALERALSAIRTVKASNAEERETKRGGEAAER----LY 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  82 ELGRGI----ALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLV-ASQTVQrSMASLSVLFGQVVRGLSAGAR 156
Cdd:cd18551  210 RAGLKAakieALIGPLMGLAVQLALLVVLGVGGARVASGALTVGTLVAFLLyLFQLIT-PLSQLSSFFTQLQKALGALER 288


                 .
gi 755511082 157 V 157
Cdd:cd18551  289 I 289

ABC_KpsT_Wzt

cd03220

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...

173-403

1.33e-21

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: 92.60 E-value: 1.33e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 173 YCIPNKdIRGSITFQNVTFSYPCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGhdlrt 252
Cdd:cd03220   10 YPTYKG-GSSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 253 lNPSWLRGQVIGFisqEPVLfatTIMENIRF-----GKLDASDEEVYtaareanahEFISSFPDgystvVGERGT----T 323
Cdd:cd03220   84 -RVSSLLGLGGGF---NPEL---TGRENIYLngrllGLSRKEIDEKI---------DEIIEFSE-----LGDFIDlpvkT 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 324 LSGGQKQRLAIARALIKQPTVLILDEATSALDAE-SERVVQEALDRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCE 401
Cdd:cd03220  143 YSSGMKARLAFAIATALEPDILLIDEVLAVGDAAfQEKCQRRLRELLKQGKTVILVSHDPSSIKRlCDRALVLEKGKIRF 222


                 ..
gi 755511082 402 AG 403
Cdd:cd03220  223 DG 224

PRK10535

macrolide ABC transporter ATP-binding protein/permease MacB;

187-399

2.29e-21

macrolide ABC transporter ATP-binding protein/permease MacB;

Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 96.72 E-value: 2.29e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 187 QNVTFSYPCRPG-FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNP---SWLRGQV 262
Cdd:PRK10535   8 KDIRRSYPSGEEqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDAdalAQLRREH 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 263 IGFISQEPVLFA-TTIMENIRFGKLDASDEevyTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQ 341
Cdd:PRK10535  88 FGFIFQRYHLLShLTAAQNVEVPAVYAGLE---RKQRLLRAQELLQRL--GLEDRVEYQPSQLSGGQQQRVSIARALMNG 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755511082 342 PTVLILDEATSALDAESERVVQEALDRASA-GRTVLVIAHRLSTVRAAHSIIVMANGQV 399
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDrGHTVIIVTHDPQVAAQAERVIEIRDGEI 221

cbiO

PRK13646

energy-coupling factor transporter ATPase;

183-412

2.43e-21

energy-coupling factor transporter ATPase;

Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 93.69 E-value: 2.43e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 183 SITFQNVTFSYpcRPG----FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDghDLRTLNPS-- 256
Cdd:PRK13646   2 TIRFDNVSYTY--QKGtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD--DITITHKTkd 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 257 -WLRG--QVIGFISQ--EPVLFATTIMENIRFG----KLDAsdEEVytaarEANAHEFISSFpdGYS-TVVGERGTTLSG 326
Cdd:PRK13646  78 kYIRPvrKRIGMVFQfpESQLFEDTVEREIIFGpknfKMNL--DEV-----KNYAHRLLMDL--GFSrDVMSQSPFQMSG 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 327 GQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAG 403
Cdd:PRK13646 149 GQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVaRYADEVIVMKEGSIVSQT 228


                 ....*....
gi 755511082 404 THEELLKKG 412
Cdd:PRK13646 229 SPKELFKDK 237

nickel_nikE

TIGR02769

nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...

201-401

3.42e-21

nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]

Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 92.56 E-value: 3.42e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  201 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRG-----QVIGFISQEPVLFAT 275
Cdd:TIGR02769  26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfrrdvQLVFQDSPSAVNPRM 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  276 TIMENIR-----FGKLDASdeevytaAREANAHEFISSFpDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEA 350
Cdd:TIGR02769 106 TVRQIIGeplrhLTSLDES-------EQKARIAELLDMV-GLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEA 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 755511082  351 TSALDAESERVVQEALD--RASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCE 401
Cdd:TIGR02769 178 VSNLDMVLQAVILELLRklQQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVE 231

btuD

PRK09536

corrinoid ABC transporter ATPase; Reviewed

201-414

3.46e-21

corrinoid ABC transporter ATPase; Reviewed

Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 94.91 E-value: 3.46e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 201 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLrGQVIGFISQEPVL-FATTIME 279
Cdd:PRK09536  18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAA-SRRVASVPQDTSLsFEFDVRQ 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 280 NIRFGK------LDASDEEVYTAAREANAHEFISSFPDgystvvgERGTTLSGGQKQRLAIARALIKQPTVLILDEATSA 353
Cdd:PRK09536  97 VVEMGRtphrsrFDTWTETDRAAVERAMERTGVAQFAD-------RPVTSLSGGERQRVLLARALAQATPVLLLDEPTAS 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755511082 354 LDAESE-RVVQEALDRASAGRTVLVIAHRLS-TVRAAHSIIVMANGQVCEAGTHEELLKKGGL 414
Cdd:PRK09536 170 LDINHQvRTLELVRRLVDDGKTAVAAIHDLDlAARYCDELVLLADGRVRAAGPPADVLTADTL 232

PRK14247

phosphate ABC transporter ATP-binding protein; Provisional

201-409

3.61e-21

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 92.28 E-value: 3.61e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 201 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYD--PEA---GSVTLDGHDLRTLNPSWLRGQViGFISQEPVLFAT 275
Cdd:PRK14247  18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEArvsGEVYLDGQDIFKMDVIELRRRV-QMVFQIPNPIPN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 276 -TIMENIRFG----KLDASDEEVYTAAREANAHefiSSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEA 350
Cdd:PRK14247  97 lSIFENVALGlklnRLVKSKKELQERVRWALEK---AQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEP 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 351 TSALDAESERVVQEALDRASAGRTVLVIAH-RLSTVRAAHSIIVMANGQVCEAGTHEELL 409
Cdd:PRK14247 174 TANLDPENTAKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWGPTREVF 233

ABC_membrane

pfam00664

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

2-137

3.76e-21

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: 92.71 E-value: 3.76e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082    2 LSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCcckaE 81
Cdd:pfam00664 139 YGWKLTLVLLAVLPLYILVSAVFAKILRKLSRKEQKAVAKASSVAEESLSGIRTVKAFGREEYELEKYDKALEEA----L 214

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   82 ELGRGIALFQGLSNIA----FNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSM 137
Cdd:pfam00664 215 KAGIKKAVANGLSFGItqfiGYLSYALALWFGAYLVISGELSVGDLVAFLSLFAQLFGPL 274

Uup

COG0488

ATPase components of ABC transporters with duplicated ATPase domains [General function ...

186-380

4.32e-21

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

Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.52 E-value: 4.32e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 186 FQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDghdlrtlnpswlRGQVIGF 265
Cdd:COG0488    1 LENLSKSFGGRP---LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP------------KGLRIGY 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 266 ISQEPVLFAT-TIMENI-----RFGKLDASDEEVYTA--------AREANAHEFISSFpDGYS------TVVGERG---- 321
Cdd:COG0488   66 LPQEPPLDDDlTVLDTVldgdaELRALEAELEELEAKlaepdedlERLAELQEEFEAL-GGWEaearaeEILSGLGfpee 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755511082 322 ------TTLSGGQKQRLAIARALIKQPTVLILDEATSALDAEServVQ--EALDRASAGrTVLVIAH 380
Cdd:COG0488  145 dldrpvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEwlEEFLKNYPG-TVLVVSH 207

PRK15134

microcin C ABC transporter ATP-binding protein YejF; Provisional

187-403

5.61e-21

microcin C ABC transporter ATP-binding protein YejF; Provisional

Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 95.16 E-value: 5.61e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 187 QNVTFSYPCRPGF--------NVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEaGSVTLDGHDLRTLNpswl 258
Cdd:PRK15134 279 EQLQVAFPIRKGIlkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLN---- 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 259 RGQVIGFISQEPVLF-------------ATTIMENIRFGKLDAS----DEEVYTAARE-----ANAHEFISSFpdgystv 316
Cdd:PRK15134 354 RRQLLPVRHRIQVVFqdpnsslnprlnvLQIIEEGLRVHQPTLSaaqrEQQVIAVMEEvgldpETRHRYPAEF------- 426

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 317 vgergttlSGGQKQRLAIARALIKQPTVLILDEATSALDaeseRVVQE---ALDRASAGR---TVLVIAHRLSTVRA-AH 389
Cdd:PRK15134 427 --------SGGQRQRIAIARALILKPSLIILDEPTSSLD----KTVQAqilALLKSLQQKhqlAYLFISHDLHVVRAlCH 494

                        250
                 ....*....|....
gi 755511082 390 SIIVMANGQVCEAG 403
Cdd:PRK15134 495 QVIVLRQGEVVEQG 508

PRK14239

phosphate transporter ATP-binding protein; Provisional

202-382

7.05e-21

phosphate transporter ATP-binding protein; Provisional

Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 91.38 E-value: 7.05e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 202 LKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYD--PE---AGSVTLDGHDL--RTLNPSWLRGQvIGFISQEPVLFA 274
Cdd:PRK14239  21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDlnPEvtiTGSIVYNGHNIysPRTDTVDLRKE-IGMVFQQPNPFP 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 275 TTIMENIRFG-KLDA-SDEEVYTAAREANAHEfiSSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATS 352
Cdd:PRK14239 100 MSIYENVVYGlRLKGiKDKQVLDEAVEKSLKG--ASIWDEVKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177

                        170       180       190
                 ....*....|....*....|....*....|
gi 755511082 353 ALDAESERVVQEALDRASAGRTVLVIAHRL 382
Cdd:PRK14239 178 ALDPISAGKIEETLLGLKDDYTMLLVTRSM 207

SapF

COG4167

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

187-409

7.83e-21

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

Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 91.44 E-value: 7.83e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 187 QNVTFSYPCRPG------FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWlRG 260
Cdd:COG4167    8 RNLSKTFKYRTGlfrrqqFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY-RC 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 261 QVIGFISQEPvlfATTIMENIRFGK-LDA--------SDEEvytaaREANAHEFIssfpdgysTVVGERG-------TTL 324
Cdd:COG4167   87 KHIRMIFQDP---NTSLNPRLNIGQiLEEplrlntdlTAEE-----REERIFATL--------RLVGLLPehanfypHML 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 325 SGGQKQRLAIARALIKQPTVLILDEATSALDAeSERV--------VQEALdrasaGRTVLVIAHRLSTVR-AAHSIIVMA 395
Cdd:COG4167  151 SSGQKQRVALARALILQPKIIIADEALAALDM-SVRSqiinlmleLQEKL-----GISYIYVSQHLGIVKhISDKVLVMH 224

                        250
                 ....*....|....
gi 755511082 396 NGQVCEAGTHEELL 409
Cdd:COG4167  225 QGEVVEYGKTAEVF 238

ABC_putative_ATPase

cd03269

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...

200-403

8.52e-21

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 90.03 E-value: 8.52e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 200 NVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLrtlnpSWLRGQVIGFISQEPVLF-ATTIM 278
Cdd:cd03269   14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-----DIAARNRIGYLPEERGLYpKMKVI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 279 ENIR-FGKL-DASDEEvytAAREANahEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDA 356
Cdd:cd03269   89 DQLVyLAQLkGLKKEE---ARRRID--EWLERL--ELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDP 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 755511082 357 ESERVVQEAL-DRASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAG 403
Cdd:cd03269  162 VNVELLKDVIrELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210

AztA

NF040873

zinc ABC transporter ATP-binding protein AztA;

192-394

8.56e-21

zinc ABC transporter ATP-binding protein AztA;

Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 89.60 E-value: 8.56e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 192 SYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSwlrgqvigfISQEPV 271
Cdd:NF040873   1 GYGGRP---VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQ---------RSEVPD 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 272 LFATTIMENIRFG---------KLDASDEEVYTAAREANahefissfpdGYSTVVGERGTTLSGGQKQRLAIARALIKQP 342
Cdd:NF040873  69 SLPLTVRDLVAMGrwarrglwrRLTRDDRAAVDDALERV----------GLADLAGRQLGELSGGQRQRALLAQGLAQEA 138

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755511082 343 TVLILDEATSALDAESERVVQEALDRASA-GRTVLVIAHRLSTVRAAHSIIVM 394
Cdd:NF040873 139 DLLLLDEPTTGLDAESRERIIALLAEEHArGATVVVVTHDLELVRRADPCVLL 191

cbiO

PRK13649

energy-coupling factor transporter ATPase;

183-411

1.06e-20

energy-coupling factor transporter ATPase;

Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 91.73 E-value: 1.06e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 183 SITFQNVTFSYPCRPGFN--VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPS---- 256
Cdd:PRK13649   2 GINLQNVSYTYQAGTPFEgrALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkdik 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 257 WLRGQViGFISQ--EPVLFATTIMENIRFG--KLDASDEEVYTAAREANAHEFISSfpdgysTVVGERGTTLSGGQKQRL 332
Cdd:PRK13649  82 QIRKKV-GLVFQfpESQLFEETVLKDVAFGpqNFGVSQEEAEALAREKLALVGISE------SLFEKNPFELSGGQMRRV 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 333 AIARALIKQPTVLILDEATSALDAESERVVQEALDRA-SAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEELLK 410
Cdd:PRK13649 155 AIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLhQSGMTIVLVTHLMDDVaNYADFVYVLEKGKLVLSGKPKDIFQ 234


                 .
gi 755511082 411 K 411
Cdd:PRK13649 235 D 235

ntrCD

TIGR01184

nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...

202-397

1.13e-20

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: 90.22 E-value: 1.13e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  202 LKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSwlRGQVIGFISQEPVLfatTIMENI 281
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD--RMVVFQNYSLLPWL---TVRENI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  282 RFGkLDASDEEVYTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERV 361
Cdd:TIGR01184  76 ALA-VDRVLPDLSKSERRAIVEEHIALV--GLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 755511082  362 VQEALDR--ASAGRTVLVIAHRL-STVRAAHSIIVMANG 397
Cdd:TIGR01184 153 LQEELMQiwEEHRVTVLMVTHDVdEALLLSDRVVMLTNG 191

PTZ00243

ABC transporter; Provisional

201-410

1.27e-20

ABC transporter; Provisional

Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 95.23 E-value: 1.27e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  201 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVtldghdlrtlnpsWLRgQVIGFISQEPVLFATTIMEN 280
Cdd:PTZ00243  675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-------------WAE-RSIAYVPQQAWIMNATVRGN 740

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  281 IRFgkldaSDEEvyTAAREANA------HEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSAL 354
Cdd:PTZ00243  741 ILF-----FDEE--DAARLADAvrvsqlEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 755511082  355 DAE-SERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELLK 410
Cdd:PTZ00243  814 DAHvGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSADFMR 870

ABC_6TM_ABCB9_like

cd18784

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and ...

2-157

1.33e-20

Six-transmembrane helical domain (6-TMD) of ATP-binding cassette sub-family B member 9 and similar proteins; ATP-binding cassette sub-family B member 9 is also known as transporter associated with antigen processing, TAP-like protein, TAPL, and ABCB9. It is a half transporter comprises a homodimeric lysosomal peptide transport complex. It belongs to the ABC_6TM_TAP_ABCB8_10_like subgroup of the ABC_6TM exporter family. The ABC_6TM exporter family represents the six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. In addition to ABC exporters, ABC transporters include two classes of ABC importers, classified depending on details of their architecture and mechanism. Only the ABC exporters are included in the ABC_6TM exporter family. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs. The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting chemical diversity of the translocated substrates, whereas NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional unit.

Pssm-ID: 350057 [Multi-domain] Cd Length: 289 Bit Score: 91.60 E-value: 1.33e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   2 LSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESccckAE 81
Cdd:cd18784  134 LSWQLSLVTLIGLPLIAIVSKVYGDYYKKLSKAVQDSLAKANEVAEETISSIRTVRSFANEDGEANRYSEKLKD----TY 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  82 ELGRGIALFQG----LSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 157
Cdd:cd18784  210 KLKIKEALAYGgyvwSNELTELALTVSTLYYGGHLVITGQISGGNLISFILYQLELGSCLESVGSVYTGLMQAVGAAEKV 289

ABC_DrrA

cd03265

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...

198-408

1.59e-20

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.

Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 89.74 E-value: 1.59e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 198 GFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTlNPSWLRgQVIGFISQEPVL-FATT 276
Cdd:cd03265   12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVR-RRIGIVFQDLSVdDELT 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 277 IMENIR-FGKLDAsdeeVYTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD 355
Cdd:cd03265   90 GWENLYiHARLYG----VPGAERRERIDELLDFV--GLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLD 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 755511082 356 AESERVVQEALDR--ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEEL 408
Cdd:cd03265  164 PQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQlCDRVAIIDHGRIIAEGTPEEL 219

lolD

PRK11629

lipoprotein-releasing ABC transporter ATP-binding protein LolD;

200-399

2.00e-20

lipoprotein-releasing ABC transporter ATP-binding protein LolD;

Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 89.87 E-value: 2.00e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 200 NVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSW---LRGQVIGFISQ-EPVLFAT 275
Cdd:PRK11629  23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaeLRNQKLGFIYQfHHLLPDF 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 276 TIMENIRFGKLDASdeeVYTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD 355
Cdd:PRK11629 103 TALENVAMPLLIGK---KKPAEINSRALEMLAAV--GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLD 177

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 755511082 356 AESERVVQEALDR--ASAGRTVLVIAHRLSTVRAAHSIIVMANGQV 399
Cdd:PRK11629 178 ARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRL 223

nikE

PRK10419

nickel ABC transporter ATP-binding protein NikE;

196-401

6.77e-20

nickel ABC transporter ATP-binding protein NikE;

Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 88.98 E-value: 6.77e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 196 RPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRG--------------- 260
Cdd:PRK10419  22 HQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAfrrdiqmvfqdsisa 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 261 ----QVIGFISQEPVLFATTIMEnirfgkldasdeevytAAREANAHEFISSFpDGYSTVVGERGTTLSGGQKQRLAIAR 336
Cdd:PRK10419 102 vnprKTVREIIREPLRHLLSLDK----------------AERLARASEMLRAV-DLDDSVLDKRPPQLSGGQLQRVCLAR 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755511082 337 ALIKQPTVLILDEATSALDaeseRVVQ-EALD-----RASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCE 401
Cdd:PRK10419 165 ALAVEPKLLILDEAVSNLD----LVLQaGVIRllkklQQQFGTACLFITHDLRLVeRFCQRVMVMDNGQIVE 232

ABCD_peroxisomal_ALDP

cd03223

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...

184-390

7.60e-20

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).

Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 86.05 E-value: 7.60e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVasllerfydpeagsvtldghdLRTLN---PsWLRG 260
Cdd:cd03223    1 IELENLSLATP--DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSL---------------------FRALAglwP-WGSG 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 261 QV-------IGFISQEPVLFATTIMENIrfgkldasdeeVYTAAREanahefissfpdgystvvgergttLSGGQKQRLA 333
Cdd:cd03223   57 RIgmpegedLLFLPQRPYLPLGTLREQL-----------IYPWDDV------------------------LSGGEQQRLA 101

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755511082 334 IARALIKQPTVLILDEATSALDAESERVVQEALDRASAgrTVLVIAHRlSTVRAAHS 390
Cdd:cd03223  102 FARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELGI--TVISVGHR-PSLWKFHD 155

ABCF_EF-3

cd03221

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...

184-380

1.16e-19

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

Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 84.81 E-value: 1.16e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTldghdlrtlnpsWLRGQVI 263
Cdd:cd03221    1 IELENLSKTYGGKL---LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT------------WGSTVKI 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQepvlfattimenirfgkldasdeevytaareanahefissfpdgystvvgergttLSGGQKQRLAIARALIKQPT 343
Cdd:cd03221   66 GYFEQ-------------------------------------------------------LSGGEKMRLALAKLLLENPN 90

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 755511082 344 VLILDEATSALDAESERVVQEALdRASAGrTVLVIAH 380
Cdd:cd03221   91 LLLLDEPTNHLDLESIEALEEAL-KEYPG-TVILVSH 125

3a01204

TIGR00955

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

195-410

1.33e-19

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

Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 91.26 E-value: 1.33e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  195 CRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLErFYDPE----AGSVTLDGHdlrTLNPSWLRgQVIGFISQEP 270
Cdd:TIGR00955  34 ERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGM---PIDAKEMR-AISAYVQQDD 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  271 VLFAT-TIMENIRFGKLDASDEEVYTAAREANAHEFIS--SFPDGYSTVVGERGTT--LSGGQKQRLAIARALIKQPTVL 345
Cdd:TIGR00955 109 LFIPTlTVREHLMFQAHLRMPRRVTKKEKRERVDEVLQalGLRKCANTRIGVPGRVkgLSGGERKRLAFASELLTDPPLL 188

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755511082  346 ILDEATSALDAES-ERVVQEALDRASAGRTVLVIAHRLST--VRAAHSIIVMANGQVCEAGTHEELLK 410
Cdd:TIGR00955 189 FCDEPTSGLDSFMaYSVVQVLKGLAQKGKTIICTIHQPSSelFELFDKIILMAEGRVAYLGSPDQAVP 256

PRK14246

phosphate ABC transporter ATP-binding protein; Provisional

201-409

1.43e-19

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 87.80 E-value: 1.43e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 201 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERF---YDPEA---GSVTLDGHDLRTLNPSWLRGQViGFISQEPVLFA 274
Cdd:PRK14246  25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLieiYDSKIkvdGKVLYFGKDIFQIDAIKLRKEV-GMVFQQPNPFP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 275 -TTIMENIRFGKLDASDEEvytaAREANAHEFISSFPDGYSTVVGER----GTTLSGGQKQRLAIARALIKQPTVLILDE 349
Cdd:PRK14246 104 hLSIYDNIAYPLKSHGIKE----KREIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLMDE 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755511082 350 ATSALDAESERVVQEALDRASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEELL 409
Cdd:PRK14246 180 PTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEIF 240

ssuB

PRK11247

aliphatic sulfonates transport ATP-binding subunit; Provisional

184-399

2.35e-19

aliphatic sulfonates transport ATP-binding subunit; Provisional

Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 87.04 E-value: 2.35e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRpgfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVtLDG----HDLRtlnpswlr 259
Cdd:PRK11247  13 LLLNAVSKRYGER---TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGtaplAEAR-------- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 260 gQVIGFISQEPVLFA-TTIMENIRFG-KLDASDeevytAAREANAHEfissfpdGYSTVVGERGTTLSGGQKQRLAIARA 337
Cdd:PRK11247  81 -EDTRLMFQDARLLPwKKVIDNVGLGlKGQWRD-----AALQALAAV-------GLADRANEWPAALSGGQKQRVALARA 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755511082 338 LIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLS-TVRAAHSIIVMANGQV 399
Cdd:PRK11247 148 LIHRPGLLLLDEPLGALDALTRIEMQDLIESlwQQHGFTVLLVTHDVSeAVAMADRVLLIEEGKI 212

cbiO

PRK13645

energy-coupling factor transporter ATPase;

179-418

2.76e-19

energy-coupling factor transporter ATPase;

Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 87.76 E-value: 2.76e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 179 DIRGSITFQNVTFSYPCRPGFN--VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLrtlnPS 256
Cdd:PRK13645   2 DFSKDIILDNVSYTYAKKTPFEfkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAI----PA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 257 WLRG--------QVIGFISQEP--VLFATTIMENIRFG--KLDASDEEVYTAAREANAhefISSFPDGYstvVGERGTTL 324
Cdd:PRK13645  78 NLKKikevkrlrKEIGLVFQFPeyQLFQETIEKDIAFGpvNLGENKQEAYKKVPELLK---LVQLPEDY---VKRSPFEL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 325 SGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTV-RAAHSIIVMANGQVCE 401
Cdd:PRK13645 152 SGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKeyKKRIIMVTHNMDQVlRIADEVIVMHEGKVIS 231

                        250
                 ....*....|....*..
gi 755511082 402 AGTHEELLKKGGLYSEL 418
Cdd:PRK13645 232 IGSPFEIFSNQELLTKI 248

ABC_6TM_bac_exporter_ABCB8_10_like

cd18575

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

3-155

3.17e-19

Pssm-ID: 350019 [Multi-domain] Cd Length: 289 Bit Score: 87.54 E-value: 3.17e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   3 SPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAEE 82
Cdd:cd18575  135 SPKLTLLVLLVIPLVVLPIILFGRRVRRLSRASQDRLADLSAFAEETLSAIKTVQAFTREDAERQRFATAVEAAFAAALR 214

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755511082  83 LGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRglSAGA 155
Cdd:cd18575  215 RIRARALLTALVIFLVFGAIVFVLWLGAHDVLAGRMSAGELSQFVFYAVLAAGSVGALSEVWGDLQR--AAGA 285

cbiO

PRK13636

cobalt transporter ATP-binding subunit; Provisional

184-424

5.29e-19

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 86.83 E-value: 5.29e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLR-GQV 262
Cdd:PRK13636   6 LKVEELNYNYS--DGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKlRES 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 263 IGFISQEP--VLFATTIMENIRFGKLDAS--DEEVYTAAREANAHEFISSFPDgystvvgERGTTLSGGQKQRLAIARAL 338
Cdd:PRK13636  84 VGMVFQDPdnQLFSASVYQDVSFGAVNLKlpEDEVRKRVDNALKRTGIEHLKD-------KPTHCLSFGQKKRVAIAGVL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 339 IKQPTVLILDEATSALD----AESERVVQEALDraSAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEELLKKgg 413
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDpmgvSEIMKLLVEMQK--ELGLTIIIATHDIDIVPLyCDNVFVMKEGRVILQGNPKEVFAE-- 232

                        250
                 ....*....|.
gi 755511082 414 lySELIRRQTL 424
Cdd:PRK13636 233 --KEMLRKVNL 241

ABC_Carb_Monos_II

cd03215

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

201-399

5.44e-19

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: 84.41 E-value: 5.44e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 201 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVIGFISQEPV---LFAT-T 276
Cdd:cd03215   15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVPEDRKregLVLDlS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 277 IMENIRFGKLdasdeevytaareanahefissfpdgystvvgergttLSGGQKQRLAIARALIKQPTVLILDEATSALDA 356
Cdd:cd03215   95 VAENIALSSL-------------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 755511082 357 ESERVVQEALDR-ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQV 399
Cdd:cd03215  138 GAKAEIYRLIRElADAGKAVLLISSELDELLGlCDRILVMYEGRI 182

cbiO

PRK13652

cobalt transporter ATP-binding subunit; Provisional

184-425

5.79e-19

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 86.40 E-value: 5.79e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYpcRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgQVI 263
Cdd:PRK13652   4 IETRDLCYSY--SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVR-KFV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEP--VLFATTIMENIRFGKLDASDEEVYTAAREANAHEFIssfpdGYSTVVGERGTTLSGGQKQRLAIARALIKQ 341
Cdd:PRK13652  81 GLVFQNPddQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHML-----GLEELRDRVPHHLSGGEKKRVAIAGVIAME 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 342 PTVLILDEATSALDAESERVVQEALDRASA--GRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEELLkkggLYSEL 418
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEIF----LQPDL 231


                 ....*..
gi 755511082 419 IRRQTLD 425
Cdd:PRK13652 232 LARVHLD 238

ABC_CcmA_heme_exporter

cd03231

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...

196-380

1.20e-18

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.

Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 83.70 E-value: 1.20e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 196 RPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGqvIGFISQEPVLFAT 275
Cdd:cd03231   10 RDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARG--LLYLGHAPGIKTT 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 276 -TIMENIRFGKLDASDEEVYTAAREANAHEFiSSFPDGYstvvgergttLSGGQKQRLAIARALIKQPTVLILDEATSAL 354
Cdd:cd03231   88 lSVLENLRFWHADHSDEQVEEALARVGLNGF-EDRPVAQ----------LSAGQQRRVALARLLLSGRPLWILDEPTTAL 156

                        170       180
                 ....*....|....*....|....*..
gi 755511082 355 DAESERVVQEAL-DRASAGRTVLVIAH 380
Cdd:cd03231  157 DKAGVARFAEAMaGHCARGGMVVLTTH 183

PRK10261

glutathione transporter ATP-binding protein; Provisional

187-403

1.65e-18

glutathione transporter ATP-binding protein; Provisional

Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 87.99 E-value: 1.65e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 187 QNVTFSYPCRPG-FNVLK-------DFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWL 258
Cdd:PRK10261 317 RNLVTRFPLRSGlLNRVTrevhaveKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKL 396

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 259 RG--QVIGFISQEPvlFAT---------TIMENIRFGKLDASDEevyTAAREANAHEFISSFPDGYSTVVGErgttLSGG 327
Cdd:PRK10261 397 QAlrRDIQFIFQDP--YASldprqtvgdSIMEPLRVHGLLPGKA---AAARVAWLLERVGLLPEHAWRYPHE----FSGG 467

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755511082 328 QKQRLAIARALIKQPTVLILDEATSALDAE-SERVVQEALD-RASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAG 403
Cdd:PRK10261 468 QRQRICIARALALNPKVIIADEAVSALDVSiRGQIINLLLDlQRDFGIAYLFISHDMAVVeRISHRVAVMYLGQIVEIG 546

met_CoM_red_A2

TIGR03269

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...

206-409

2.35e-18

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

Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 87.17 E-value: 2.35e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  206 TLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTL----DGHDLRTLNPSwLRGQV---IGFISQEPVLFA-TTI 277
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD-GRGRAkryIGILHQEYDLYPhRTV 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  278 MENIRFG-KLDASDE-----EVYT----AAREANAHEFISSFPDgystvvgergtTLSGGQKQRLAIARALIKQPTVLIL 347
Cdd:TIGR03269 383 LDNLTEAiGLELPDElarmkAVITlkmvGFDEEKAEEILDKYPD-----------ELSEGERHRVALAQVLIKEPRIVIL 451

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755511082  348 DEATSALDAESERVVQEAL--DRASAGRTVLVIAHRLSTV-----RAAhsiiVMANGQVCEAGTHEELL 409
Cdd:TIGR03269 452 DEPTGTMDPITKVDVTHSIlkAREEMEQTFIIVSHDMDFVldvcdRAA----LMRDGKIVKIGDPEEIV 516

NupO

COG3845

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...

198-399

4.40e-18

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

Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 86.23 E-value: 4.40e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 198 GFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLL--ERfyDPEAGSVTLDGHDLRTLNPSWLRGQVIGFISQEPVLFAT 275
Cdd:COG3845  270 GVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALagLR--PPASGSIRLDGEDITGLSPRERRRLGVAYIPEDRLGRGL 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 276 ----TIMENI-----------RFGKLDasdeevyTAAREANAHEFISSF---PDGYSTVVGergtTLSGGQKQRLAIARA 337
Cdd:COG3845  348 vpdmSVAENLilgryrrppfsRGGFLD-------RKAIRAFAEELIEEFdvrTPGPDTPAR----SLSGGNQQKVILARE 416

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755511082 338 LIKQPTVLILDEATSALDAES-ERVVQEALDRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQV 399
Cdd:COG3845  417 LSRDPKLLIAAQPTRGLDVGAiEFIHQRLLELRDAGAAVLLISEDLDEILAlSDRIAVMYEGRI 480

PRK10895

lipopolysaccharide ABC transporter ATP-binding protein; Provisional

198-409

5.32e-18

lipopolysaccharide ABC transporter ATP-binding protein; Provisional

Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 83.02 E-value: 5.32e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 198 GFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHD--LRTLNPSWLRGqvIGFISQEPVLFAT 275
Cdd:PRK10895  15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDisLLPLHARARRG--IGYLPQEASIFRR 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 276 TIMENIRFGKLDASDeEVYTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALD 355
Cdd:PRK10895  93 LSVYDNLMAVLQIRD-DLSAEQREDRANELMEEF--HIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755511082 356 AES----ERVVQEALDRasaGRTVLVIAHRL-STVRAAHSIIVMANGQVCEAGTHEELL 409
Cdd:PRK10895 170 PISvidiKRIIEHLRDS---GLGVLITDHNVrETLAVCERAYIVSQGHLIAHGTPTEIL 225

PRK10619

histidine ABC transporter ATP-binding protein HisP;

201-409

5.66e-18

histidine ABC transporter ATP-binding protein HisP;

Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 83.09 E-value: 5.66e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 201 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSwlRGQVIGFISQEPVLFAT----- 275
Cdd:PRK10619  20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDK--DGQLKVADKNQLRLLRTrltmv 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 276 ----------TIMENIR--------FGKLDASDEEVYTAAREANAHEFISSFPdgystvvgergTTLSGGQKQRLAIARA 337
Cdd:PRK10619  98 fqhfnlwshmTVLENVMeapiqvlgLSKQEARERAVKYLAKVGIDERAQGKYP-----------VHLSGGQQQRVSIARA 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755511082 338 LIKQPTVLILDEATSALD----AESERVVQEAldrASAGRTVLVIAHRLSTVRAAHS-IIVMANGQVCEAGTHEELL 409
Cdd:PRK10619 167 LAMEPEVLLFDEPTSALDpelvGEVLRIMQQL---AEEGKTMVVVTHEMGFARHVSShVIFLHQGKIEEEGAPEQLF 240

PRK15056

manganese/iron ABC transporter ATP-binding protein;

183-427

6.32e-18

manganese/iron ABC transporter ATP-binding protein;

Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 83.39 E-value: 6.32e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 183 SITFQNVTFSYpcRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLnpswLRGQV 262
Cdd:PRK15056   6 GIVVNDVTVTW--RNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA----LQKNL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 263 IGFISQE-------PVLFATTIMENiRFGKL------DASDEEVYTAAREAnahefiSSFPDGYSTVVGErgttLSGGQK 329
Cdd:PRK15056  80 VAYVPQSeevdwsfPVLVEDVVMMG-RYGHMgwlrraKKRDRQIVTAALAR------VDMVEFRHRQIGE----LSGGQK 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 330 QRLAIARALIKQPTVLILDEATSALDAESE-RVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEEL 408
Cdd:PRK15056 149 KRVFLARAIAQQGQVILLDEPFTGVDVKTEaRIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETT 228

                        250       260
                 ....*....|....*....|..
gi 755511082 409 LKKGGL---YSELIRRQTLDAS 427
Cdd:PRK15056 229 FTAENLelaFSGVLRHVALNGS 250

livG

PRK11300

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

207-408

1.04e-17

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

Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 82.35 E-value: 1.04e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 207 LKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLnPSWL---RGQVIGFisQEPVLFAT-TIMENIr 282
Cdd:PRK11300  26 LEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGL-PGHQiarMGVVRTF--QHVRLFREmTVIENL- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 283 fgkLDASDEEVYT----------AAR--EANAHEFISSFPD--GYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILD 348
Cdd:PRK11300 102 ---LVAQHQQLKTglfsgllktpAFRraESEALDRAATWLErvGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLD 178

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755511082 349 EATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEEL 408
Cdd:PRK11300 179 EPAAGLNPKETKELDELIAelRNEHNVTVLLIEHDMKLVMGiSDRIYVVNQGTPLANGTPEEI 241

PRK15439

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

198-408

1.29e-17

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.10 E-value: 1.29e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 198 GFNVLK--DFTLKlpSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVIGFISQEPVLFAT 275
Cdd:PRK15439  23 GVEVLKgiDFTLH--AGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLVPQEPLLFPN 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 276 -TIMENIRFG--KLDASDEEVYTAAREANAHEFISSfpdgystvvgeRGTTLSGGQKQRLAIARALIKQPTVLILDEATS 352
Cdd:PRK15439 101 lSVKENILFGlpKRQASMQKMKQLLAALGCQLDLDS-----------SAGSLEVADRQIVEILRGLMRDSRILILDEPTA 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755511082 353 ALD-AESERVVQEALDRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEEL 408
Cdd:PRK15439 170 SLTpAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGKTADL 227

ABC_FeS_Assembly

cd03217

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...

201-412

1.48e-17

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: 80.65 E-value: 1.48e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 201 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEA--GSVTLDGHDLRTLNPS--WLRGQVIGFisQEPVLFA-T 275
Cdd:cd03217   15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVteGEILFKGEDITDLPPEerARLGIFLAF--QYPPEIPgV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 276 TIMENIRFgkldasdeevytaareanahefissfpdgystvVGErgtTLSGGQKQRLAIARALIKQPTVLILDEATSALD 355
Cdd:cd03217   93 KNADFLRY---------------------------------VNE---GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755511082 356 AESERVVQEALDR-ASAGRTVLVIAHR---LSTVRA--AHsiiVMANGQVCEAGTHE---ELLKKG 412
Cdd:cd03217  137 IDALRLVAEVINKlREEGKSVLIITHYqrlLDYIKPdrVH---VLYDGRIVKSGDKElalEIEKKG 199

PRK14258

phosphate ABC transporter ATP-binding protein; Provisional

183-385

1.82e-17

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 82.01 E-value: 1.82e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 183 SITFQNVTFSYPCRpgfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEA-----GSVTLDGHDL--RTLNP 255
Cdd:PRK14258   7 AIKVNNLSFYYDTQ---KILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 256 SWLRGQViGFISQEPVLFATTIMENIRFG--------KLDAsDEEVYTAAREANahefissFPDGYSTVVGERGTTLSGG 327
Cdd:PRK14258  84 NRLRRQV-SMVHPKPNLFPMSVYDNVAYGvkivgwrpKLEI-DDIVESALKDAD-------LWDEIKHKIHKSALDLSGG 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 328 QKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTV 385
Cdd:PRK14258 155 QQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQslRLRSELTMVIVSHNLHQV 214

PRK09984

phosphonate ABC transporter ATP-binding protein;

207-408

1.89e-17

phosphonate ABC transporter ATP-binding protein;

Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 81.98 E-value: 1.89e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 207 LKLPSGKIVALVGQSGGGKTTV----ASLLERFYDPEA------GSVTLDGHDLRTLNPSwlRGQViGFISQEPVLF-AT 275
Cdd:PRK09984  25 LNIHHGEMVALLGPSGSGKSTLlrhlSGLITGDKSAGShiellgRTVQREGRLARDIRKS--RANT-GYIFQQFNLVnRL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 276 TIMENIRFGKLDASD-----EEVYTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEA 350
Cdd:PRK09984 102 SVLENVLIGALGSTPfwrtcFSWFTREQKQRALQALTRV--GMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEP 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755511082 351 TSALDAESERVVQEALD--RASAGRTVLVIAHRLS-TVRAAHSIIVMANGQVCEAGTHEEL 408
Cdd:PRK09984 180 IASLDPESARIVMDTLRdiNQNDGITVVVTLHQVDyALRYCERIVALRQGHVFYDGSSQQF 240

PRK15079

oligopeptide ABC transporter ATP-binding protein OppF; Provisional

203-408

2.40e-17

oligopeptide ABC transporter ATP-binding protein OppF; Provisional

Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 82.83 E-value: 2.40e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 203 KDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRG--QVIGFISQEPV-------LF 273
Cdd:PRK15079  38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAvrSDIQMIFQDPLaslnprmTI 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 274 ATTIMENIRFGKLDASDEEVYTAAREANA-------------HEFissfpdgystvvgergttlSGGQKQRLAIARALIK 340
Cdd:PRK15079 118 GEIIAEPLRTYHPKLSRQEVKDRVKAMMLkvgllpnlinrypHEF-------------------SGGQCQRIGIARALIL 178

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755511082 341 QPTVLILDEATSALDAESE-RVVQ--EALDRaSAGRTVLVIAHRLSTVR-AAHSIIVMANGQVCEAGTHEEL 408
Cdd:PRK15079 179 EPKLIICDEPVSALDVSIQaQVVNllQQLQR-EMGLSLIFIAHDLAVVKhISDRVLVMYLGHAVELGTYDEV 249

PRK14271

phosphate ABC transporter ATP-binding protein; Provisional

188-409

2.44e-17

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 81.68 E-value: 2.44e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 188 NVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDP-----EAGSVTLDGHDLRTLNPSWLRGQV 262
Cdd:PRK14271  26 NLTLGFA---GKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSIFNYRDVLEFRRR 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 263 IGFISQEPVLFATTIMENI----RFGKLDASDEevYTAAREANAHEFisSFPDGYSTVVGERGTTLSGGQKQRLAIARAL 338
Cdd:PRK14271 103 VGMLFQRPNPFPMSIMDNVlagvRAHKLVPRKE--FRGVAQARLTEV--GLWDAVKDRLSDSPFRLSGGQQQLLCLARTL 178

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755511082 339 IKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIAHRLS-TVRAAHSIIVMANGQVCEAGTHEELL 409
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAqAARISDRAALFFDGRLVEEGPTEQLF 250

PRK14267

phosphate ABC transporter ATP-binding protein; Provisional

201-410

2.78e-17

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 81.04 E-value: 2.78e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 201 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYD--PEA---GSVTLDGHDLRT--LNPSWLRGQViGFISQEPVLF 273
Cdd:PRK14267  19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElnEEArveGEVRLFGRNIYSpdVDPIEVRREV-GMVFQYPNPF 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 274 A-TTIMENIRFG-KL-------DASDEEVYTAAREANAHEFISSFPDGYSTvvgergtTLSGGQKQRLAIARALIKQPTV 344
Cdd:PRK14267  98 PhLTIYDNVAIGvKLnglvkskKELDERVEWALKKAALWDEVKDRLNDYPS-------NLSGGQRQRLVIARALAMKPKI 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755511082 345 LILDEATSALDAESERVVQEALDRASAGRTVLVIAHR-LSTVRAAHSIIVMANGQVCEAGTHEELLK 410
Cdd:PRK14267 171 LLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237

TagH

COG1134

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...

183-422

3.64e-17

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

Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 80.51 E-value: 3.64e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 183 SITFQNVTFSYPCRPG-------------------FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSV 243
Cdd:COG1134    4 MIEVENVSKSYRLYHEpsrslkelllrrrrtrreeFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 244 TLDGhdlrtlNPSWLRGQVIGFisqEPVLfatTIMENIRFGK--LDASDEEVytAAREANAHEF--ISSFPDgysTVVGe 319
Cdd:COG1134   84 EVNG------RVSALLELGAGF---HPEL---TGRENIYLNGrlLGLSRKEI--DEKFDEIVEFaeLGDFID---QPVK- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 320 rgtTLSGGQKQRLAIARALIKQPTVLILDEATSALDAE-SERVVQEALDRASAGRTVLVIAHRLSTVRA-AHSIIVMANG 397
Cdd:COG1134  146 ---TYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfQKKCLARIRELRESGRTVIFVSHSMGAVRRlCDRAIWLEKG 222

                        250       260
                 ....*....|....*....|....*
gi 755511082 398 QVCEAGTHEELLKkggLYSELIRRQ 422
Cdd:COG1134  223 RLVMDGDPEEVIA---AYEALLAGR 244

PRK15112

peptide ABC transporter ATP-binding protein SapF;

190-409

3.85e-17

peptide ABC transporter ATP-binding protein SapF;

Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 80.99 E-value: 3.85e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 190 TFSYpcRPGF------NVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWlRGQVI 263
Cdd:PRK15112  13 TFRY--RTGWfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY-RSQRI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEPvlfATTIMENIRFGK-LDAS---DEEVYTAAREANAHEFISS---FPDGystvVGERGTTLSGGQKQRLAIAR 336
Cdd:PRK15112  90 RMIFQDP---STSLNPRQRISQiLDFPlrlNTDLEPEQREKQIIETLRQvglLPDH----ASYYPHMLAPGQKQRLGLAR 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755511082 337 ALIKQPTVLILDEATSALD-AESERVVQEALD-RASAGRTVLVIAHRLSTVR-AAHSIIVMANGQVCEAGTHEELL 409
Cdd:PRK15112 163 ALILRPKVIIADEALASLDmSMRSQLINLMLElQEKQGISYIYVTQHLGMMKhISDQVLVMHQGEVVERGSTADVL 238

ABC_6TM_YknU_like

cd18542

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

1-127

4.12e-17

Six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the uncharacterized ABC transporter YknU and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.

Pssm-ID: 349986 [Multi-domain] Cd Length: 292 Bit Score: 81.32 E-value: 4.12e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   1 MLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKA 80
Cdd:cd18542  136 SINWKLTLISLAIIPFIALFSYVFFKKVRPAFEEIREQEGELNTVLQENLTGVRVVKAFAREDYEIEKFDKENEEYRDLN 215

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 755511082  81 EELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFL 127
Cdd:cd18542  216 IKLAKLLAKYWPLMDFLSGLQIVLVLWVGGYLVINGEITLGELVAFI 262

PRK10575

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

177-410

4.98e-17

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

Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.60 E-value: 4.98e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 177 NKDIRGSITFQ--NVTFSYPCRpgfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLN 254
Cdd:PRK10575   3 EYTNHSDTTFAlrNVSFRVPGR---TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 255 PSWLRGQVIGFISQEPVLFATTIMENI------------RFGKLDAS--DEEVYTAAREANAHEFISSfpdgystvvger 320
Cdd:PRK10575  80 SKAFARKVAYLPQQLPAAEGMTVRELVaigrypwhgalgRFGAADREkvEEAISLVGLKPLAHRLVDS------------ 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 321 gttLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGRTVLVIA--HRLS-TVRAAHSIIVMANG 397
Cdd:PRK10575 148 ---LSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAvlHDINmAARYCDYLVALRGG 224

                        250
                 ....*....|...
gi 755511082 398 QVCEAGTHEELLK 410
Cdd:PRK10575 225 EMIAQGTPAELMR 237

rim_protein

TIGR01257

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...

194-421

7.60e-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: 83.52 E-value: 7.60e-17

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   194 PC-RPGFNVLkdfTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTlNPSWLRgQVIGFISQEPVL 272
Cdd:TIGR01257  940 PSgRPAVDRL---NITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVR-QSLGMCPQHNIL 1014

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   273 FA-TTIMENIRF-GKLDASDEEVYTAAREANAHEfissfpDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEA 350
Cdd:TIGR01257 1015 FHhLTVAEHILFyAQLKGRSWEEAQLEMEAMLED------TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755511082   351 TSALDAESERVVQEALDRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTheELLKKG----GLYSELIRR 421
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLlGDRIAIISQGRLYCSGT--PLFLKNcfgtGFYLTLVRK 1162

ABC_6TM_TAP1

cd18589

Six-transmembrane helical domain 1 (6-TMD1) of the ABC transporter associated with antigen ...

1-127

7.80e-17

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: 80.59 E-value: 7.80e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   1 MLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESC--CC 78
Cdd:cd18589  133 WLSPKLALLTALGLPLLLLVPKFVGKFQQSLAVQVQKSLARANQVAVETFSAMKTVRSFANEEGEAQRYRQRLQKTyrLN 212

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 755511082  79 KAEELGRGIALF-QGLSNIAfncMVLGTLFIGGSLVAGQQLKGGDLMSFL 127
Cdd:cd18589  213 KKEAAAYAVSMWtSSFSGLA---LKVGILYYGGQLVTAGTVSSGDLVTFV 259

PhnK

COG1101

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

201-399

1.74e-16

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

Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 78.97 E-value: 1.74e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 201 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLnPSWLRGQVIGFISQEPVL---FATTI 277
Cdd:COG1101   21 ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL-PEYKRAKYIGRVFQDPMMgtaPSMTI 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 278 MEN------------IRFGKldasdeevyTAAREANAHEFISSFPDGY----STVVGergtTLSGGQKQRLAIARALIKQ 341
Cdd:COG1101  100 EENlalayrrgkrrgLRRGL---------TKKRRELFRELLATLGLGLenrlDTKVG----LLSGGQRQALSLLMATLTK 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 342 PTVLILDEATSALD---AE-----SERVVQEaldrasAGRTVLVIAHRLstvRAAHS----IIVMANGQV 399
Cdd:COG1101  167 PKLLLLDEHTAALDpktAAlvlelTEKIVEE------NNLTTLMVTHNM---EQALDygnrLIMMHEGRI 227

PRK09700

D-allose ABC transporter ATP-binding protein AlsA;

184-397

3.05e-16

D-allose ABC transporter ATP-binding protein AlsA;

Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.60 E-value: 3.05e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVI 263
Cdd:PRK09700   6 ISMAGIGKSFG---PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQE-PVLFATTIMENIRFGKL--------DASDeevYTAAREANAhefISSFPDGYSTVVGERGTTLSGGQKQRLAI 334
Cdd:PRK09700  83 GIIYQElSVIDELTVLENLYIGRHltkkvcgvNIID---WREMRVRAA---MMLLRVGLKVDLDEKVANLSISHKQMLEI 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755511082 335 ARALIKQPTVLILDEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRA-AHSIIVMANG 397
Cdd:PRK09700 157 AKTLMLDAKVIIMDEPTSSLtNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDG 221

PRK10253

iron-enterobactin ABC transporter ATP-binding protein;

199-421

3.50e-16

iron-enterobactin ABC transporter ATP-binding protein;

Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 78.10 E-value: 3.50e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 199 FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLnPSWLRGQVIGFISQEPVLFA-TTI 277
Cdd:PRK10253  20 YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHY-ASKEVARRIGLLAQNATTPGdITV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 278 MENIR---------FGKLDASDEEVYTAAREANahefissfpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILD 348
Cdd:PRK10253  99 QELVArgryphqplFTRWRKEDEEAVTKAMQAT----------GITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755511082 349 EATSALDAESERVVQEALDRAS--AGRTVLVIAHRLS-TVRAAHSIIVMANGQVCEAGTHEELLKkgglySELIRR 421
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELNreKGYTLAAVLHDLNqACRYASHLIALREGKIVAQGAPKEIVT-----AELIER 239

znuC

PRK09544

high-affinity zinc transporter ATPase; Reviewed

184-406

4.45e-16

high-affinity zinc transporter ATPase; Reviewed

Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 77.46 E-value: 4.45e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRpgfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDgHDLRtlnpswlrgqvI 263
Cdd:PRK09544   5 VSLENVSVSFGQR---RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRN-GKLR-----------I 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEPVLFATTIMENIRFGKL--DASDEEVYTAAREANAHEFISsFPdgystvvgerGTTLSGGQKQRLAIARALIKQ 341
Cdd:PRK09544  70 GYVPQKLYLDTTLPLTVNRFLRLrpGTKKEDILPALKRVQAGHLID-AP----------MQKLSGGETQRVLLARALLNR 138

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755511082 342 PTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHE 406
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDqlRRELDCAVLMVSHDLHLVMAKTDEVLCLNHHICCSGTPE 205

ABC_6TM_Tm287_like

cd18548

Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from ...

1-157

4.89e-16

Six-transmembrane helical domain Tm287 of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins; This group represents the six-transmembrane helical domain (Tm287) of a heterodimeric ABC transporter Tm287/288 from Thermotoga maritima and similar proteins. This TMD possesses the ATP-binding cassette (ABC) exporter fold, which is characterized by 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds, a various type of lipids and polypeptides. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting significant structural diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane by alternating between inward- and outward-facing conformations. Moreover, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.

Pssm-ID: 349992 [Multi-domain] Cd Length: 292 Bit Score: 78.21 E-value: 4.89e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   1 MLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKA 80
Cdd:cd18548  136 RINPKLALILLVAIPILALVVFLIMKKAIPLFKKVQKKLDRLNRVVRENLTGIRVIRAFNREDYEEERFDKANDDLTDTS 215

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755511082  81 EELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFL-VASQTVQrSMASLSVLFGQVVRGLSAGARV 157
Cdd:cd18548  216 LKAGRLMALLNPLMMLIMNLAIVAILWFGGHLINAGSLQVGDLVAFInYLMQILM-SLMMLSMVFVMLPRASASAKRI 292

ABC_6TM_Pgp_ABCB1_D2_like

cd18578

Six-transmembrane helical domain 2 (TMD2) of P-glycoprotein 1 (Pgp) and related proteins; ...

2-167

5.52e-16

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: 78.26 E-value: 5.52e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   2 LSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESccCKAE 81
Cdd:cd18578  152 YGWKLALVGLATVPLLLLAGYLRMRLLSGFEEKNKKAYEESSKIASEAVSNIRTVASLTLEDYFLEKYEEALEE--PLKK 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  82 ELGRGI--ALFQGLSN-IAFNCMVLGtLFIGGSLVAGQQLKGGD----LMSFLVASQTVQRSMAslsvLFGQVVRGLSAG 154
Cdd:cd18578  230 GLRRALisGLGFGLSQsLTFFAYALA-FWYGGRLVANGEYTFEQffivFMALIFGAQSAGQAFS----FAPDIAKAKAAA 304

                        170
                 ....*....|...
gi 755511082 155 ARVFEYMALSPVI 167
Cdd:cd18578  305 ARIFRLLDRKPEI 317

ccmA

TIGR01189

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...

196-379

5.74e-16

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]

Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 76.24 E-value: 5.74e-16

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  196 RPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWlrGQVIGFISQEPVLFAT 275
Cdd:TIGR01189  10 RGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP--HENILYLGHLPGLKPE 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  276 -TIMENIRFGK--LDASDEEVYTAAREANAHEFiSSFPDGYstvvgergttLSGGQKQRLAIARALIKQPTVLILDEATS 352
Cdd:TIGR01189  88 lSALENLHFWAaiHGGAQRTIEDALAAVGLTGF-EDLPAAQ----------LSAGQQRRLALARLWLSRRPLWILDEPTT 156

                         170       180
                  ....*....|....*....|....*..
gi 755511082  353 ALDAESERVVQEALdRASAGRTVLVIA 379
Cdd:TIGR01189 157 ALDKAGVALLAGLL-RAHLARGGIVLL 182

phnK

PRK11701

phosphonate C-P lyase system protein PhnK; Provisional

187-403

6.52e-16

phosphonate C-P lyase system protein PhnK; Provisional

Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 77.27 E-value: 6.52e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 187 QNVTFSYPCRPGFnvlKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDG-----HDLRTLNPSWLRGQ 261
Cdd:PRK11701  10 RGLTKLYGPRKGC---RDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERRRL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 262 V---IGFISQEPvlfattiMENIRFG---------KLDASDEEVYTAAREANAH-----EFISSFPDgystvvgERGTTL 324
Cdd:PRK11701  87 LrteWGFVHQHP-------RDGLRMQvsaggnigeRLMAVGARHYGDIRATAGDwlervEIDAARID-------DLPTTF 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 325 SGGQKQRLAIARALIKQPTVLILDEATSALDAEservVQ-EALD--R---ASAGRTVLVIAHRLSTVR-AAHSIIVMANG 397
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVS----VQaRLLDllRglvRELGLAVVIVTHDLAVARlLAHRLLVMKQG 228


                 ....*.
gi 755511082 398 QVCEAG 403
Cdd:PRK11701 229 RVVESG 234

PRK10908

cell division ATP-binding protein FtsE;

184-399

6.68e-16

cell division ATP-binding protein FtsE;

Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 76.45 E-value: 6.68e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYpcRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPS---WLRG 260
Cdd:PRK10908   2 IRFEHVSKAY--LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRevpFLRR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 261 QvIGFISQEP-VLFATTIMENIRFGKL--DASDEE----VYTAAREANAHEFISSFPdgystvvgergTTLSGGQKQRLA 333
Cdd:PRK10908  80 Q-IGMIFQDHhLLMDRTVYDNVAIPLIiaGASGDDirrrVSAALDKVGLLDKAKNFP-----------IQLSGGEQQRVG 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 334 IARALIKQPTVLILDEATSALD-AESERVVQ--EALDRasAGRTVLVIAHRLSTV-RAAHSIIVMANGQV 399
Cdd:PRK10908 148 IARAVVNKPAVLLADEPTGNLDdALSEGILRlfEEFNR--VGVTVLMATHDIGLIsRRSYRMLTLSDGHL 215

ABCG_White

cd03234

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...

201-403

1.40e-15

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: 75.77 E-value: 1.40e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 201 VLKDFTLKLPSGKIVALVGQSGGGKTT----VASLLERFYDPEaGSVTLDGHDLRtlnpswlRGQV---IGFISQEPVLF 273
Cdd:cd03234   22 ILNDVSLHVESGQVMAILGSSGSGKTTlldaISGRVEGGGTTS-GQILFNGQPRK-------PDQFqkcVAYVRQDDILL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 274 AT-TIMENIRFGKLDASDEEVYTAAREANAhEFISSFPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATS 352
Cdd:cd03234   94 PGlTVRETLTYTAILRLPRKSSDAIRKKRV-EDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTS 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755511082 353 ALDAESERVVQEALDR-ASAGRTVLVIAH--RLSTVRAAHSIIVMANGQVCEAG 403
Cdd:cd03234  173 GLDSFTALNLVSTLSQlARRNRIVILTIHqpRSDLFRLFDRILLLSSGEIVYSG 226

MK0520

COG2401

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...

199-381

1.97e-15

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

Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 74.99 E-value: 1.97e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 199 FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFY--DPEAGSVTLDGHDlrtlnpswlrgqvigfISQEpvlfaTT 276
Cdd:COG2401   43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQ----------------FGRE-----AS 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 277 IMENIrfGKLDASDE--EVYTAAREANAHEFISSFPdgystvvgergtTLSGGQKQRLAIARALIKQPTVLILDEATSAL 354
Cdd:COG2401  102 LIDAI--GRKGDFKDavELLNAVGLSDAVLWLRRFK------------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167

                        170       180
                 ....*....|....*....|....*....
gi 755511082 355 DAESERVVQEALDRAS--AGRTVLVIAHR 381
Cdd:COG2401  168 DRQTAKRVARNLQKLArrAGITLVVATHH 196

cbiO

PRK13643

energy-coupling factor transporter ATPase;

184-411

2.15e-15

energy-coupling factor transporter ATPase;

Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 76.31 E-value: 2.15e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSY-PCRP-GFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTL------DGHDLRTLNP 255
Cdd:PRK13643   2 IKFEKVNYTYqPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsSTSKQKEIKP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 256 swLRGQV-IGFISQEPVLFATTIMENIRFG--KLDASDEEVYTAAreANAHEFIssfpdGYSTVVGERGT-TLSGGQKQR 331
Cdd:PRK13643  82 --VRKKVgVVFQFPESQLFEETVLKDVAFGpqNFGIPKEKAEKIA--AEKLEMV-----GLADEFWEKSPfELSGGQMRR 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 332 LAIARALIKQPTVLILDEATSALDAESERVVQEALDRA-SAGRTVLVIAHRLSTVR-AAHSIIVMANGQVCEAGTHEELL 409
Cdd:PRK13643 153 VAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIhQSGQTVVLVTHLMDDVAdYADYVYLLEKGHIISCGTPSDVF 232


                 ..
gi 755511082 410 KK 411
Cdd:PRK13643 233 QE 234

PRK13651

cobalt transporter ATP-binding subunit; Provisional

184-410

2.22e-15

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 76.66 E-value: 2.22e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSY-PCRP-GFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTL---DGHDL-RTLNPSW 257
Cdd:PRK13651   3 IKVKNIVKIFnKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKkKTKEKEK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 258 --------------------LRGQViGFISQ--EPVLFATTIMENIRFGKLD--ASDEEVYTAAREanahefissfpdgY 313
Cdd:PRK13651  83 vleklviqktrfkkikkikeIRRRV-GVVFQfaEYQLFEQTIEKDIIFGPVSmgVSKEEAKKRAAK-------------Y 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 314 STVVG------ERGT-TLSGGQKQRLAIARALIKQPTVLILDEATSALDAEServVQEALD----RASAGRTVLVIAHRL 382
Cdd:PRK13651 149 IELVGldesylQRSPfELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQG---VKEILEifdnLNKQGKTIILVTHDL 225

                        250       260
                 ....*....|....*....|....*....
gi 755511082 383 STV-RAAHSIIVMANGQVCEAGTHEELLK 410
Cdd:PRK13651 226 DNVlEWTKRTIFFKDGKIIKDGDTYDILS 254

ABCG_PDR_domain1

cd03233

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...

196-385

2.30e-15

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: 74.61 E-value: 2.30e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 196 RPGFNVLKDFTLKLPSGKIVALVGQSGGGKTT----VASLLERFYDPEaGSVTLDGHDLRTlNPSWLRGQVIgFISQEPV 271
Cdd:cd03233   17 RSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTllkaLANRTEGNVSVE-GDIHYNGIPYKE-FAEKYPGEII-YVSEEDV 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 272 LFAT-TIMENIRFgkldasdeevytaAREANAHEFIssfpdgystvvgeRGttLSGGQKQRLAIARALIKQPTVLILDEA 350
Cdd:cd03233   94 HFPTlTVRETLDF-------------ALRCKGNEFV-------------RG--ISGGERKRVSIAEALVSRASVLCWDNS 145

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 755511082 351 TSALDAEServvqeALDRASAGRTvlvIAHRLSTV 385
Cdd:cd03233  146 TRGLDSST------ALEILKCIRT---MADVLKTT 171

PRK10762

D-ribose transporter ATP binding protein; Provisional

197-382

3.22e-15

D-ribose transporter ATP binding protein; Provisional

Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 77.74 E-value: 3.22e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 197 PGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVIGFISQEPVLFAT- 275
Cdd:PRK10762  15 PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGIIHQELNLIPQl 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 276 TIMENI--------RFGKLDASdeEVYTAAREANAHEFISSFPDgysTVVGErgttLSGGQKQRLAIARALIKQPTVLIL 347
Cdd:PRK10762  95 TIAENIflgrefvnRFGRIDWK--KMYAEADKLLARLNLRFSSD---KLVGE----LSIGEQQMVEIAKVLSFESKVIIM 165

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 755511082 348 DEATSAL-DAESE---RVVQEALDRasaGRTVLVIAHRL 382
Cdd:PRK10762 166 DEPTDALtDTETEslfRVIRELKSQ---GRGIVYISHRL 201

PRK10261

glutathione transporter ATP-binding protein; Provisional

196-410

3.30e-15

glutathione transporter ATP-binding protein; Provisional

Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 77.97 E-value: 3.30e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 196 RPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWL-------------RGQV 262
Cdd:PRK10261  26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIelseqsaaqmrhvRGAD 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 263 IGFISQEPV-----LFAT--TIMENIRFGKlDASDEEVYTAA-------REANAHEFISSFPDgystvvgergtTLSGGQ 328
Cdd:PRK10261 106 MAMIFQEPMtslnpVFTVgeQIAESIRLHQ-GASREEAMVEAkrmldqvRIPEAQTILSRYPH-----------QLSGGM 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 329 KQRLAIARALIKQPTVLILDEATSALDAESE-------RVVQEALDRAsagrtVLVIAHRLSTV-RAAHSIIVMANGQVC 400
Cdd:PRK10261 174 RQRVMIAMALSCRPAVLIADEPTTALDVTIQaqilqliKVLQKEMSMG-----VIFITHDMGVVaEIADRVLVMYQGEAV 248

                        250
                 ....*....|
gi 755511082 401 EAGTHEELLK 410
Cdd:PRK10261 249 ETGSVEQIFH 258

PRK15134

microcin C ABC transporter ATP-binding protein YejF; Provisional

201-409

3.48e-15

microcin C ABC transporter ATP-binding protein YejF; Provisional

Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 77.44 E-value: 3.48e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 201 VLKDFTLKLPSGKIVALVGQSGGGKTTVA-SLLERFYDPEA----GSVTLDGHDL-----RTLNPswLRGQVIGFISQEP 270
Cdd:PRK15134  24 VVNDVSLQIEAGETLALVGESGSGKSVTAlSILRLLPSPPVvypsGDIRFHGESLlhaseQTLRG--VRGNKIAMIFQEP 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 271 VlfattimenIRFGKLDASDEEVYTA-------AREANAHEFISSFPDgystvVGERGTT---------LSGGQKQRLAI 334
Cdd:PRK15134 102 M---------VSLNPLHTLEKQLYEVlslhrgmRREAARGEILNCLDR-----VGIRQAAkrltdyphqLSGGERQRVMI 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755511082 335 ARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEELL 409
Cdd:PRK15134 168 AMALLTRPELLIADEPTTALDVSVQAQILQLLRelQQELNMGLLFITHNLSIVRKlADRVAVMQNGRCVEQNRAATLF 245

PRK11000

maltose/maltodextrin ABC transporter ATP-binding protein MalK;

183-408

4.92e-15

maltose/maltodextrin ABC transporter ATP-binding protein MalK;

Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 76.22 E-value: 4.92e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 183 SITFQNVTFSYpcrpGFNVL-KDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSwLRGq 261
Cdd:PRK11000   3 SVTLRNVTKAY----GDVVIsKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA-ERG- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 262 vIGFISQEPVLFA-TTIMENIRFG-KLdASDEEVYTAAREANAHEFISsfpdgYSTVVGERGTTLSGGQKQRLAIARALI 339
Cdd:PRK11000  77 -VGMVFQSYALYPhLSVAENMSFGlKL-AGAKKEEINQRVNQVAEVLQ-----LAHLLDRKPKALSGGQRQRVAIGRTLV 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755511082 340 KQPTVLILDEATSALDAeSERV---VQEALDRASAGRTVLVIAHrlSTVRA---AHSIIVMANGQVCEAGTHEEL 408
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDA-ALRVqmrIEISRLHKRLGRTMIYVTH--DQVEAmtlADKIVVLDAGRVAQVGKPLEL 221

MglA

COG1129

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

201-410

5.30e-15

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

Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 76.98 E-value: 5.30e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 201 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPS--WLRGqvIGFIS----QEPVLFA 274
Cdd:COG1129  267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdaIRAG--IAYVPedrkGEGLVLD 344

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 275 TTIMENI---------RFGKLDASDEEvytaareANAHEFISSF---PDGYSTVVGergtTLSGGQKQRLAIARALIKQP 342
Cdd:COG1129  345 LSIRENItlasldrlsRGGLLDRRRER-------ALAEEYIKRLrikTPSPEQPVG----NLSGGNQQKVVLAKWLATDP 413

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 343 TVLILDEATSALD--AESE--RVVQEAldrASAGRTVLVIahrlST-----VRAAHSIIVMANGQVC-----EAGTHEEL 408
Cdd:COG1129  414 KVLILDEPTRGIDvgAKAEiyRLIREL---AAEGKAVIVI----SSelpelLGLSDRILVMREGRIVgeldrEEATEEAI 486


                 ..
gi 755511082 409 LK 410
Cdd:COG1129  487 MA 488

modC

PRK11144

molybdenum ABC transporter ATP-binding protein ModC;

204-407

6.12e-15

molybdenum ABC transporter ATP-binding protein ModC;

Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 75.68 E-value: 6.12e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 204 DFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGhdlRTLNPS----WL----RGqvIGFISQEPVLFA- 274
Cdd:PRK11144  16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNG---RVLFDAekgiCLppekRR--IGYVFQDARLFPh 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 275 TTIMENIRFGKLDASDEE----VYTAAREAnaheFISSFPdgystvvgergTTLSGGQKQRLAIARALIKQPTVLILDEA 350
Cdd:PRK11144  91 YKVRGNLRYGMAKSMVAQfdkiVALLGIEP----LLDRYP-----------GSLSGGEKQRVAIGRALLTAPELLLMDEP 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755511082 351 TSALDAESERVVQEALDRASagRTV----LVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEE 407
Cdd:PRK11144 156 LASLDLPRKRELLPYLERLA--REInipiLYVSHSLDEIlRLADRVVVLEQGKVKAFGPLEE 215

PRK13549

xylose transporter ATP-binding subunit; Provisional

197-398

1.17e-14

xylose transporter ATP-binding subunit; Provisional

Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 75.74 E-value: 1.17e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 197 PGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYdPEA---GSVTLDGHDLR--TLNPSWLRGQVIgfISQEPV 271
Cdd:PRK13549  16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHGtyeGEIIFEGEELQasNIRDTERAGIAI--IHQELA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 272 LFAT-TIMENI-------RFGKLDasDEEVYTAAREANAHEFISSFPDgysTVVGErgttLSGGQKQRLAIARALIKQPT 343
Cdd:PRK13549  93 LVKElSVLENIflgneitPGGIMD--YDAMYLRAQKLLAQLKLDINPA---TPVGN----LGLGQQQLVEIAKALNKQAR 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755511082 344 VLILDEATSALDAESERVVQEAL-DRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQ 398
Cdd:PRK13549 164 LLILDEPTASLTESETAVLLDIIrDLKAHGIACIYISHKLNEVKAiSDTICVIRDGR 220

ABC_6TM_Rv0194_D1_like

cd18543

Six-transmembrane helical domain 1 (TMD1) of the multidrug efflux ABC transporter Rv0194 and ...

2-157

1.31e-14

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: 74.06 E-value: 1.31e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   2 LSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEER--------YQAEL 73
Cdd:cd18543  136 LSPPLALVALASLPPLVLVARRFRRRYFPASRRAQDQAGDLATVVEESVTGIRVVKAFGRERRELDRfeaaarrlRATRL 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  74 EscccKAEELGRGIALFQGLSNIAfncmVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSA 153
Cdd:cd18543  216 R----AARLRARFWPLLEALPELG----LAAVLALGGWLVANGSLTLGTLVAFSAYLTMLVWPVRMLGWLLAMAQRARAA 287


                 ....
gi 755511082 154 GARV 157
Cdd:cd18543  288 AERV 291

PRK13537

nodulation factor ABC transporter ATP-binding protein NodI;

184-409

1.31e-14

nodulation factor ABC transporter ATP-binding protein NodI;

Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 74.07 E-value: 1.31e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRpgfNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLrtlnPSWLR---- 259
Cdd:PRK13537   8 IDFRNVEKRYGDK---LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV----PSRARharq 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 260 --GQVIGFISQEPVLfatTIMENIR-FGK---LDASDeevyTAAREANAHEFiSSFPDGYSTVVGErgttLSGGQKQRLA 333
Cdd:PRK13537  81 rvGVVPQFDNLDPDF---TVRENLLvFGRyfgLSAAA----ARALVPPLLEF-AKLENKADAKVGE----LSGGMKRRLT 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755511082 334 IARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEELL 409
Cdd:PRK13537 149 LARALVNDPDVLVLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALI 226

met_CoM_red_A2

TIGR03269

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...

184-411

1.43e-14

Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 75.61 E-value: 1.43e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  184 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERF--YDPEAGSVTLDghdlRTLNPSWLRGQ 261
Cdd:TIGR03269   1 IEVKNLTKKFD---GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIYH----VALCEKCGYVE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  262 VIGFISQE-PVLFATTIMENIRFGKLDasdEEVYTAAREANAHEF----------------ISSFPD-GYS--------- 314
Cdd:TIGR03269  74 RPSKVGEPcPVCGGTLEPEEVDFWNLS---DKLRRRIRKRIAIMLqrtfalygddtvldnvLEALEEiGYEgkeavgrav 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  315 -----TVVGERGT----TLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRAsagrtvlVIAHRLSTV 385
Cdd:TIGR03269 151 dliemVQLSHRIThiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEA-------VKASGISMV 223

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 755511082  386 RAAH----------SIIVMANGQVCEAGTHEELLKK 411
Cdd:TIGR03269 224 LTSHwpeviedlsdKAIWLENGEIKEEGTPDEVVAV 259

ABC_ABC_ChvD

TIGR03719

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...

185-380

1.90e-14

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

Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 75.36 E-value: 1.90e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  185 TFQNVTFSYPcrPGFNVLKDFTLK-LPSGKIvALVGQSGGGKTTVASL---LERFYDPEAgsvtldghdlrtlnpsWLR- 259
Cdd:TIGR03719   6 TMNRVSKVVP--PKKEILKDISLSfFPGAKI-GVLGLNGAGKSTLLRImagVDKDFNGEA----------------RPQp 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  260 GQVIGFISQEPVLFAT-TIMENIRFG---KLDASDE--EVYTAARE---------------------ANAHEFISSF--- 309
Cdd:TIGR03719  67 GIKVGYLPQEPQLDPTkTVRENVEEGvaeIKDALDRfnEISAKYAEpdadfdklaaeqaelqeiidaADAWDLDSQLeia 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  310 ------PDGYSTVvgergTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAES----ERVVQEaldraSAGrTVLVIA 379
Cdd:TIGR03719 147 mdalrcPPWDADV-----TKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESvawlERHLQE-----YPG-TVVAVT 215


                  .
gi 755511082  380 H 380
Cdd:TIGR03719 216 H 216

ABC_6TM_TAP2

cd18590

Six-transmembrane helical domain 2 (6-TMD2) of the ABC transporter associated with antigen ...

2-157

2.00e-14

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: 73.53 E-value: 2.00e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   2 LSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAE 81
Cdd:cd18590  134 LSWQLTLLTLIEMPLTAIAQKVYNTYHQKLSQAVQDSIAKAGELAREAVSSIRTVRSFKAEEEEACRYSEALERTYNLKD 213

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755511082  82 ELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 157
Cdd:cd18590  214 RRDTVRAVYLLVRRVLQLGVQVLMLYCGRQLIQSGHLTTGSLVSFILYQKNLGSYVRTLVYIYGDMLSNVGAAAKV 289

araG

PRK11288

L-arabinose ABC transporter ATP-binding protein AraG;

186-408

2.09e-14

L-arabinose ABC transporter ATP-binding protein AraG;

Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.95 E-value: 2.09e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 186 FQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVIGF 265
Cdd:PRK11288   7 FDGIGKTFP---GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 266 ISQE----PVLfatTIMENIRFGKLDAS-----DEEVYTAAREANAHEFISSFPDgysTVVGErgttLSGGQKQRLAIAR 336
Cdd:PRK11288  84 IYQElhlvPEM---TVAENLYLGQLPHKggivnRRLLNYEAREQLEHLGVDIDPD---TPLKY----LSIGQRQMVEIAK 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755511082 337 ALIKQPTVLILDEATSALDA-ESE---RVVQEALDRasaGRTVLVIAHRLSTV-RAAHSIIVMANGQvcEAGTHEEL 408
Cdd:PRK11288 154 ALARNARVIAFDEPTSSLSArEIEqlfRVIRELRAE---GRVILYVSHRMEEIfALCDAITVFKDGR--YVATFDDM 225

livF

PRK11614

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

184-409

3.00e-14

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

Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 71.83 E-value: 3.00e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLerFYDPEA--GSVTLDGHDLRTLNPSWLRGQ 261
Cdd:PRK11614   6 LSFDKVSAHYG---KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTL--CGDPRAtsGRIVFDGKDITDWQTAKIMRE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 262 VIGFISQEPVLFA-TTIMENIRFGKLDASDEEVYTaaREANAHEFissFPDGYSTVVgERGTTLSGGQKQRLAIARALIK 340
Cdd:PRK11614  81 AVAIVPEGRRVFSrMTVEENLAMGGFFAERDQFQE--RIKWVYEL---FPRLHERRI-QRAGTMSGGEQQMLAIGRALMS 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755511082 341 QPTVLILDEATSALdaeSERVVQEALD-----RASAGRTVLVIAHRLSTVRAAHSIIVMANGQVCEAGTHEELL 409
Cdd:PRK11614 155 QPRLLLLDEPSLGL---APIIIQQIFDtieqlREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALL 225

PRK13536

nodulation factor ABC transporter ATP-binding protein NodI;

183-391

3.73e-14

nodulation factor ABC transporter ATP-binding protein NodI;

Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 73.33 E-value: 3.73e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 183 SITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLrtlnPSWLRG-- 260
Cdd:PRK13536  41 AIDLAGVSKSYGDKA---VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV----PARARLar 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 261 QVIGFISQEPVL-FATTIMENI----RFGKLDASD-EEVYTAAREANAHEfissfpdgysTVVGERGTTLSGGQKQRLAI 334
Cdd:PRK13536 114 ARIGVVPQFDNLdLEFTVRENLlvfgRYFGMSTREiEAVIPSLLEFARLE----------SKADARVSDLSGGMKRRLTL 183

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755511082 335 ARALIKQPTVLILDEATSALDAESERVVQEALDRASA-GRTVLVIAH----------RLSTVRAAHSI 391
Cdd:PRK13536 184 ARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLArGKTILLTTHfmeeaerlcdRLCVLEAGRKI 251

PRK10584

putative ABC transporter ATP-binding protein YbbA; Provisional

200-377

3.80e-14

putative ABC transporter ATP-binding protein YbbA; Provisional

Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 71.35 E-value: 3.80e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 200 NVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNP---SWLRGQVIGFISQEPVLFAT- 275
Cdd:PRK10584  24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEearAKLRAKHVGFVFQSFMLIPTl 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 276 TIMENIRFGKL--DASDEEVYTAAREANAHefissfpdgysTVVGER----GTTLSGGQKQRLAIARALIKQPTVLILDE 349
Cdd:PRK10584 104 NALENVELPALlrGESSRQSRNGAKALLEQ-----------LGLGKRldhlPAQLSGGEQQRVALARAFNGRPDVLFADE 172

                        170       180       190
                 ....*....|....*....|....*....|.
gi 755511082 350 ATSALDAES-ERVVQE--ALDRASAGRTVLV 377
Cdd:PRK10584 173 PTGNLDRQTgDKIADLlfSLNREHGTTLILV 203

ABCG_PDR_domain2

cd03232

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...

182-397

5.06e-14

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: 70.35 E-value: 5.06e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 182 GSITFQNVTFSYPCRPGF-NVLKDFTLKLPSGKIVALVGQSGGGKTTVASLL-ERfydPEAGSVT----LDGhdlRTLNP 255
Cdd:cd03232    2 SVLTWKNLNYTVPVKGGKrQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLaGR---KTAGVITgeilING---RPLDK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 256 SWLRgqVIGFISQEPVLFAT-TIMENIRFgkldasdeevytaarEANAhefissfpdgystvvgeRGttLSGGQKQRLAI 334
Cdd:cd03232   76 NFQR--STGYVEQQDVHSPNlTVREALRF---------------SALL-----------------RG--LSVEQRKRLTI 119

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755511082 335 ARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRAAH--SIIVMANG 397
Cdd:cd03232  120 GVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKlADSGQAILCTIHQPSASIFEKfdRLLLLKRG 185

nikD

PRK10418

nickel transporter ATP-binding protein NikD; Provisional

203-408

5.60e-14

nickel transporter ATP-binding protein NikD; Provisional

Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 71.65 E-value: 5.60e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 203 KDFTLKLPSGKIVALVGQSGGGKT-TVASLLERFydPE-----AGSVTLDGhdlRTLNPSWLRGQVIGFISQEP------ 270
Cdd:PRK10418  20 HGVSLTLQRGRVLALVGGSGSGKSlTCAAALGIL--PAgvrqtAGRVLLDG---KPVAPCALRGRKIATIMQNPrsafnp 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 271 -VLFATTIMENIR-FGKLdaSDEEVYTAAREA----NAHEFISSFPdgystvvgergTTLSGGQKQRLAIARALIKQPTV 344
Cdd:PRK10418  95 lHTMHTHARETCLaLGKP--ADDATLTAALEAvgleNAARVLKLYP-----------FEMSGGMLQRMMIALALLCEAPF 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755511082 345 LILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEEL 408
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESivQKRALGMLLVTHDMGVVaRLADDVAVMSHGRIVEQGDVETL 228

cbiO

PRK13638

energy-coupling factor ABC transporter ATP-binding protein;

201-424

1.56e-13

energy-coupling factor ABC transporter ATP-binding protein;

Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 70.42 E-value: 1.56e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 201 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDL----RTLNPswLRGQViGFISQEP--VLFA 274
Cdd:PRK13638  16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdyskRGLLA--LRQQV-ATVFQDPeqQIFY 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 275 TTIMENIRFG--KLDASDEEVytaAREAnahefissfpDGYSTVVGERG------TTLSGGQKQRLAIARALIKQPTVLI 346
Cdd:PRK13638  93 TDIDSDIAFSlrNLGVPEAEI---TRRV----------DEALTLVDAQHfrhqpiQCLSHGQKKRVAIAGALVLQARYLL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 347 LDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEELLKKGglysELIRRQTL 424
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTHGAPGEVFACT----EAMEQAGL 235

PRK10522

multidrug transporter membrane component/ATP-binding component; Provisional

184-401

1.88e-13

multidrug transporter membrane component/ATP-binding component; Provisional

Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 72.31 E-value: 1.88e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPcRPGFNVlKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGqvi 263
Cdd:PRK10522 323 LELRNVTFAYQ-DNGFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRK--- 397

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 gfisqepvLFATTIMENIRFGKL-----DASDEEVYTA--AREANAHEFissfpdgysTVVGERGTT--LSGGQKQRLAI 334
Cdd:PRK10522 398 --------LFSAVFTDFHLFDQLlgpegKPANPALVEKwlERLKMAHKL---------ELEDGRISNlkLSKGQKKRLAL 460

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755511082 335 ARALIKQPTVLILDEATSALDAESERVV-QEALDRASA-GRTVLVIAHRLSTVRAAHSIIVMANGQVCE 401
Cdd:PRK10522 461 LLALAEERDILLLDEWAADQDPHFRREFyQVLLPLLQEmGKTIFAISHDDHYFIHADRLLEMRNGQLSE 529

xylG

TIGR02633

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...

198-398

2.17e-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: 71.78 E-value: 2.17e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  198 GFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYdPEA---GSVTLDGHDLRTLNPSWLRGQVIGFISQEPVLFA 274
Cdd:TIGR02633  13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHGtwdGEIYWSGSPLKASNIRDTERAGIVIIHQELTLVP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  275 T-TIMENIRFGK------LDASDEEVYTAAREANAHEFISSFPDgySTVVGERGttlsGGQKQRLAIARALIKQPTVLIL 347
Cdd:TIGR02633  92 ElSVAENIFLGNeitlpgGRMAYNAMYLRAKNLLRELQLDADNV--TRPVGDYG----GGQQQLVEIAKALNKQARLLIL 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755511082  348 DEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQ 398
Cdd:TIGR02633 166 DEPSSSLtEKETEILLDIIRDLKAHGVACVYISHKLNEVKAvCDTICVIRDGQ 218

PRK13539

cytochrome c biogenesis protein CcmA; Provisional

201-380

3.93e-13

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 67.98 E-value: 3.93e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 201 VLKDFTLKLPSGKIVALVGQSGGGKTT----VASLLErfydPEAGSVTLDGHDLRTLNPswlrGQVIGFISQ----EPVL 272
Cdd:PRK13539  17 LFSGLSFTLAAGEALVLTGPNGSGKTTllrlIAGLLP----PAAGTIKLDGGDIDDPDV----AEACHYLGHrnamKPAL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 273 fatTIMENIRFGKldasdeEVYtAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATS 352
Cdd:PRK13539  89 ---TVAENLEFWA------AFL-GGEELDIAAALEAV--GLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTA 156

                        170       180
                 ....*....|....*....|....*....
gi 755511082 353 ALDAESERVVQEAL-DRASAGRTVLVIAH 380
Cdd:PRK13539 157 ALDAAAVALFAELIrAHLAQGGIVIAATH 185

dppD

PRK11022

dipeptide transporter ATP-binding subunit; Provisional

212-410

5.15e-13

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 69.77 E-value: 5.15e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 212 GKIVALVGQSGGGKTtVASL----LERFydP---EAGSVTLDGHDLRTLNPSWLR---GQVIGFISQEPVL-------FA 274
Cdd:PRK11022  33 GEVVGIVGESGSGKS-VSSLaimgLIDY--PgrvMAEKLEFNGQDLQRISEKERRnlvGAEVAMIFQDPMTslnpcytVG 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 275 TTIMENIRFGKLDASdeevytAAREANAHEFIS--SFPDGYSTVvGERGTTLSGGQKQRLAIARALIKQPTVLILDEATS 352
Cdd:PRK11022 110 FQIMEAIKVHQGGNK------KTRRQRAIDLLNqvGIPDPASRL-DVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTT 182

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755511082 353 ALDAESE-RVVQEALDRASAGRTVLV-IAHRLSTV-RAAHSIIVMANGQVCEAGTHEELLK 410
Cdd:PRK11022 183 ALDVTIQaQIIELLLELQQKENMALVlITHDLALVaEAAHKIIVMYAGQVVETGKAHDIFR 243

GguA

NF040905

sugar ABC transporter ATP-binding protein;

197-401

6.63e-13

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 70.20 E-value: 6.63e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 197 PGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYdPEA---GSVTLDGH--DLRTLNPSWLRGQVIgfISQE-- 269
Cdd:NF040905  12 PGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PHGsyeGEILFDGEvcRFKDIRDSEALGIVI--IHQEla 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 270 --PVLfatTIMENI-------RFGKLDAsdEEVYTAAREANAHEFISSFPDgysTVVGERGTtlsgGQKQRLAIARALIK 340
Cdd:NF040905  89 liPYL---SIAENIflgneraKRGVIDW--NETNRRARELLAKVGLDESPD---TLVTDIGV----GKQQLVEIAKALSK 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755511082 341 QPTVLILDEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCE 401
Cdd:NF040905 157 DVKLLILDEPTAALnEEDSAALLDLLLELKAQGITSIIISHKLNEIRRvADSITVLRDGRTIE 219

ABC_6TM_TmrB_like

cd18541

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

2-140

7.23e-13

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: 68.98 E-value: 7.23e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   2 LSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAE 81
Cdd:cd18541  138 ISPKLTLIALLPLPLLALLVYRLGKKIHKRFRKVQEAFSDLSDRVQESFSGIRVIKAFVQEEAEIERFDKLNEEYVEKNL 217

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755511082  82 ELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFL---------------VASqTVQRSMASL 140
Cdd:cd18541  218 RLARVDALFFPLIGLLIGLSFLIVLWYGGRLVIRGTITLGDLVAFNsylgmliwpmmalgwVIN-LIQRGAASL 290

ABC_NatA_like

cd03267

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...

201-399

9.08e-13

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.

Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 67.74 E-value: 9.08e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 201 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLR--GQVIGFISQE----PVLFA 274
Cdd:cd03267   36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRriGVVFGQKTQLwwdlPVIDS 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 275 TTIMENI------RFGK--------LDASdEEVYTAAREanahefissfpdgystvvgergttLSGGQKQRLAIARALIK 340
Cdd:cd03267  116 FYLLAAIydlppaRFKKrldelselLDLE-ELLDTPVRQ------------------------LSLGQRMRAEIAAALLH 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755511082 341 QPTVLILDEATSALDAESERVVQEALDRASAGR--TVLVIAHRLSTVRA-AHSIIVMANGQV 399
Cdd:cd03267  171 EPEILFLDEPTIGLDVVAQENIRNFLKEYNRERgtTVLLTSHYMKDIEAlARRVLVIDKGRL 232

ABC_UvrA_II

cd03271

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...

200-404

1.08e-12

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: 67.64 E-value: 1.08e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 200 NVLKDFTLKLPSGKIVALVGQSGGGKTT------VASLLERFYdpeAGSVTLDGHD----LRTLnpswlrGQVIgFISQE 269
Cdd:cd03271    9 NNLKNIDVDIPLGVLTCVTGVSGSGKSSlindtlYPALARRLH---LKKEQPGNHDriegLEHI------DKVI-VIDQS 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 270 PV--------LFATTIMENIR--F-------------------GK-----LDASDEEvytaareanAHEFISSFPD---- 311
Cdd:cd03271   79 PIgrtprsnpATYTGVFDEIRelFcevckgkrynretlevrykGKsiadvLDMTVEE---------ALEFFENIPKiark 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 312 ---------GYSTVvGERGTTLSGGQKQRLAIARALIKQ---PTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVI 378
Cdd:cd03271  150 lqtlcdvglGYIKL-GQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRlVDKGNTVVVI 228

                        250       260       270
                 ....*....|....*....|....*....|..
gi 755511082 379 AHRLSTVRAAHSIIVM------ANGQVCEAGT 404
Cdd:cd03271  229 EHNLDVIKCADWIIDLgpeggdGGGQVVASGT 260

PRK03695

vitamin B12-transporter ATPase; Provisional

205-414

6.69e-12

vitamin B12-transporter ATPase; Provisional

Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 65.34 E-value: 6.69e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 205 FTLKLPSGKIVALVGQSGGGKTT----VASLLerfydPEAGSVTLDGHDLRTLNPSWLRGQVIGFISQEPVLFATTImen 280
Cdd:PRK03695  15 LSAEVRAGEILHLVGPNGAGKSTllarMAGLL-----PGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPV--- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 281 irFGKLDAS-DEEVYTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQR-------LAIARALIKQPTVLILDEATS 352
Cdd:PRK03695  87 --FQYLTLHqPDKTRTEAVASALNEVAEAL--GLDDKLGRSVNQLSGGEWQRvrlaavvLQVWPDINPAGQLLLLDEPMN 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755511082 353 ALDaeserVVQE-ALDR-----ASAGRTVLVIAHRLS-TVRAAHSIIVMANGQVCEAGTHEELLKKGGL 414
Cdd:PRK03695 163 SLD-----VAQQaALDRllselCQQGIAVVMSSHDLNhTLRHADRVWLLKQGKLLASGRRDEVLTPENL 226

ABC_ABC_ChvD

TIGR03719

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...

184-384

7.66e-12

Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 67.27 E-value: 7.66e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  184 ITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLdGHDLRtlnpswlrgqvI 263
Cdd:TIGR03719 323 IEAENLTKAFGDKL---LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVK-----------L 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  264 GFISQ--EPVLFATTIMENIRFGkldasDEEVYTAAREANAHEFISSF----PDgYSTVVGErgttLSGGQKQRLAIARA 337
Cdd:TIGR03719 388 AYVDQsrDALDPNKTVWEEISGG-----LDIIKLGKREIPSRAYVGRFnfkgSD-QQKKVGQ----LSGGERNRVHLAKT 457

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755511082  338 LIKQPTVLILDEATSALDAESERVVQEALDrASAGrTVLVIAH------RLST 384
Cdd:TIGR03719 458 LKSGGNVLLLDEPTNDLDVETLRALEEALL-NFAG-CAVVISHdrwfldRIAT 508

ABC_6TM_Tm288_like

cd18547

Six-transmembrane helical domain Tm288 of a heterodimeric ABC transporter Tm287/288 from ...

1-157

1.42e-11

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: 65.12 E-value: 1.42e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   1 MLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQA---ELESCC 77
Cdd:cd18547  142 YISPLLTLIVLVTVPLSLLVTKFIAKRSQKYFRKQQKALGELNGYIEEMISGQKVVKAFNREEEAIEEFDEineELYKAS 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  78 CKAEELGrGIA--LFQGLSNIAFncmvLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGA 155
Cdd:cd18547  222 FKAQFYS-GLLmpIMNFINNLGY----VLVAVVGGLLVINGALTVGVIQAFLQYSRQFSQPINQISQQINSLQSALAGAE 296


                 ..
gi 755511082 156 RV 157
Cdd:cd18547  297 RV 298

oppD

PRK09473

oligopeptide transporter ATP-binding component; Provisional

178-443

1.86e-11

oligopeptide transporter ATP-binding component; Provisional

Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 65.13 E-value: 1.86e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 178 KDIRgsitfqnVTFSYPcrPG-FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPE---AGSVTLDGHDLRTL 253
Cdd:PRK09473  16 KDLR-------VTFSTP--DGdVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 254 NPSWL---RGQVIGFISQEPVL-----------FATTIMENIRFGKLDASDEEV--YTAAREANAHEFISSFPDGYStvv 317
Cdd:PRK09473  87 PEKELnklRAEQISMIFQDPMTslnpymrvgeqLMEVLMLHKGMSKAEAFEESVrmLDAVKMPEARKRMKMYPHEFS--- 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 318 gergttlsGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRA-AHSIIVM 394
Cdd:PRK09473 164 --------GGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNelKREFNTAIIMITHDLGVVAGiCDKVLVM 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 755511082 395 ANGQVCEAGTHEELLKKG------GLYSELIRRQTLDASLTSTP--PAEKPEDPKSC 443
Cdd:PRK09473 236 YAGRTMEYGNARDVFYQPshpysiGLLNAVPRLDAEGESLLTIPgnPPNLLRLPKGC 292

PRK11831

phospholipid ABC transporter ATP-binding protein MlaF;

179-408

2.06e-11

phospholipid ABC transporter ATP-binding protein MlaF;

Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 64.02 E-value: 2.06e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 179 DIRGsitfqnVTFSYPCRPGFNvlkDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWL 258
Cdd:PRK11831   9 DMRG------VSFTRGNRCIFD---NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 259 RG--QVIGFISQEPVLFA-TTIMENIRFgkldasdeevytAAREanaHefiSSFPDG--YSTV------VGERG------ 321
Cdd:PRK11831  80 YTvrKRMSMLFQSGALFTdMNVFDNVAY------------PLRE---H---TQLPAPllHSTVmmkleaVGLRGaaklmp 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 322 TTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVR--AAHSIIVmANG 397
Cdd:PRK11831 142 SELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISElnSALGVTCVVVSHDVPEVLsiADHAYIV-ADK 220

                        250
                 ....*....|.
gi 755511082 398 QVCEAGTHEEL 408
Cdd:PRK11831 221 KIVAHGSAQAL 231

PRK11819

putative ABC transporter ATP-binding protein; Reviewed

185-380

2.34e-11

putative ABC transporter ATP-binding protein; Reviewed

Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.53 E-value: 2.34e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 185 TFQNVTFSYPcrPGFNVLKDFTLK-LPSGKIvALVGQSGGGKTTVASL---LERFYDPEAgsvtldghdlrTLNPswlrG 260
Cdd:PRK11819   8 TMNRVSKVVP--PKKQILKDISLSfFPGAKI-GVLGLNGAGKSTLLRImagVDKEFEGEA-----------RPAP----G 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 261 QVIGFISQEPVLFAT-TIMENIRFG---KLDASDE--EVY------------TAAREA---------NAHEFISSF---- 309
Cdd:PRK11819  70 IKVGYLPQEPQLDPEkTVRENVEEGvaeVKAALDRfnEIYaayaepdadfdaLAAEQGelqeiidaaDAWDLDSQLeiam 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 310 -----PDGYSTVvgergTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAES----ERVVQEaldraSAGrTVLVIAH 380
Cdd:PRK11819 150 dalrcPPWDAKV-----TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESvawlEQFLHD-----YPG-TVVAVTH 218

3a01205

TIGR00956

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

199-385

3.92e-11

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

Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.52 E-value: 3.92e-11

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   199 FNVLKDFTLKLPSGKIVALVGQSGGGKTT----VASLLERFYDPEAGSVTLDGHDLRTLNPSwLRGQVIgFISQEPVLFA 274
Cdd:TIGR00956   74 FDILKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYDGITPEEIKKH-YRGDVV-YNAETDVHFP 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   275 T-TIMENIRFG--------KLDASDEEVYtAAREANAHEFISSFPDGYSTVVGE---RGttLSGGQKQRLAIARALIKQP 342
Cdd:TIGR00956  152 HlTVGETLDFAarcktpqnRPDGVSREEY-AKHIADVYMATYGLSHTRNTKVGNdfvRG--VSGGERKRVSIAEASLGGA 228

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 755511082   343 TVLILDEATSALDAEServvqeALDRASAGRTVLVIAHRLSTV 385
Cdd:TIGR00956  229 KIQCWDNATRGLDSAT------ALEFIRALKTSANILDTTPLV 265

PRK11147

ABC transporter ATPase component; Reviewed

182-380

5.36e-11

ABC transporter ATPase component; Reviewed

Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.59 E-value: 5.36e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 182 GSITF--QNVTFSYPcrpGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVT---------LDGHdl 250
Cdd:PRK11147 316 GKIVFemENVNYQID---GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHcgtklevayFDQH-- 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 251 R-TLNPSwlrgqvigfisqepvlfaTTIMENIRFGKldasdEEVYTAAREANAHEFISSF---PDGYSTVVgergTTLSG 326
Cdd:PRK11147 391 RaELDPE------------------KTVMDNLAEGK-----QEVMVNGRPRHVLGYLQDFlfhPKRAMTPV----KALSG 443

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755511082 327 GQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAgrTVLVIAH 380
Cdd:PRK11147 444 GERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQG--TVLLVSH 495

ABC_6TM_exporter_like

cd18564

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

1-157

5.42e-11

Six-transmembrane helical domain (TMD) of an uncharacterized ABC exporter, and similar proteins; This group includes a subunit of six transmembrane (TM) helices typically found in the ATP-binding cassette (ABC) transporters that function as exporters, which contain 6 TM helices per subunit (domain), or a total of 12 TM helices for the complete transporter. The ABC exporters are found in both prokaryotes and eukaryotes, where they mediate the cellular secretion of toxic compounds and a various type of lipids. ABC transporters typically consist of two transmembrane domains (TMDs) and two nucleotide-binding domains (NBDs). The sequences and structures of the TMDs are quite varied between the different type of transporters, suggesting the chemical diversity of the translocated substrates, while NBDs are conserved among all ABC transporters. The two NBDs together bind and hydrolyze ATP, thereby providing the driving force for transport, while the TMDs participate in substrate recognition and translocation across the lipid membrane. However, some ABC genes are organized as half-transporters, which must form either homodimers or heterodimers to form a functional transporter. The ABC exporters play a role in multidrug resistance to antibiotics and anticancer agents, and mutations in these proteins have been shown to cause severe human diseases such as cystic fibrosis.

Pssm-ID: 350008 [Multi-domain] Cd Length: 307 Bit Score: 63.30 E-value: 5.42e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   1 MLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAE-LESccCK 79
Cdd:cd18564  151 WLDWQLALIALAVAPLLLLAARRFSRRIKEASREQRRREGALASVAQESLSAIRVVQAFGREEHEERRFAREnRKS--LR 228

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755511082  80 AEELGRGI-ALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 157
Cdd:cd18564  229 AGLRAARLqALLSPVVDVLVAVGTALVLWFGAWLVLAGRLTPGDLLVFLAYLKNLYKPVRDLAKLTGRIAKASASAERV 307

PLN03211

ABC transporter G-25; Provisional

212-398

7.87e-11

ABC transporter G-25; Provisional

Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 64.13 E-value: 7.87e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 212 GKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRgqvIGFISQEPVLFA-TTIMENIRFGKLDASD 290
Cdd:PLN03211  94 GEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKR---TGFVTQDDILYPhLTVRETLVFCSLLRLP 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 291 EEVYTAAREANAHEFISSF--PDGYSTVVGE---RGttLSGGQKQRLAIARALIKQPTVLILDEATSALDAESE-RVVQE 364
Cdd:PLN03211 171 KSLTKQEKILVAESVISELglTKCENTIIGNsfiRG--ISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAyRLVLT 248

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 755511082 365 ALDRASAGRTVLVIAHRLST--VRAAHSIIVMANGQ 398
Cdd:PLN03211 249 LGSLAQKGKTIVTSMHQPSSrvYQMFDSVLVLSEGR 284

uvra

TIGR00630

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...

286-408

8.82e-11

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: 64.26 E-value: 8.82e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  286 LDASDEEvytaareanAHEFISSFPD-------------GYSTVvGERGTTLSGGQKQRLAIARALIKQ---PTVLILDE 349
Cdd:TIGR00630 789 LDMTVEE---------AYEFFEAVPSisrklqtlcdvglGYIRL-GQPATTLSGGEAQRIKLAKELSKRstgRTLYILDE 858

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755511082  350 ATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRAAHSIIVM------ANGQVCEAGTHEEL 408
Cdd:TIGR00630 859 PTTGLHFDDIKKLLEVLQRlVDKGNTVVVIEHNLDVIKTADYIIDLgpeggdGGGTVVASGTPEEV 924

hmuV

PRK13547

heme ABC transporter ATP-binding protein;

196-410

9.54e-11

heme ABC transporter ATP-binding protein;

Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.15 E-value: 9.54e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 196 RPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTV-ASLLERFYDPEA-------GSVTLDGHDLRTLNPSWL-RGQVIGFI 266
Cdd:PRK13547  11 RRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLlKALAGDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLaRLRAVLPQ 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 267 SQEPVlFATTIMENI---------RFGKLDASDEEVYTAAREANahefissfpdGYSTVVGERGTTLSGGQKQRLAIARA 337
Cdd:PRK13547  91 AAQPA-FAFSAREIVllgrypharRAGALTHRDGEIAWQALALA----------GATALVGRDVTTLSGGELARVQFARV 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 338 L---------IKQPTVLILDEATSALD-AESERVVQEALDRASAGRT-VLVIAHRLS-TVRAAHSIIVMANGQVCEAGTH 405
Cdd:PRK13547 160 LaqlwpphdaAQPPRYLLLDEPTAALDlAHQHRLLDTVRRLARDWNLgVLAIVHDPNlAARHADRIAMLADGAIVAHGAP 239


                 ....*
gi 755511082 406 EELLK 410
Cdd:PRK13547 240 ADVLT 244

Rli1

COG1245

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...

202-380

3.06e-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: 62.11 E-value: 3.06e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 202 LKDFTLKLPSGKI-----VALVGQSGGGKTTVASLLERFYDPEAGSVTLDghdlrtlnpswLRgqvigfISQEPvlfatt 276
Cdd:COG1245  351 YGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-----------LK------ISYKP------ 407

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 277 imeniRFGKLDaSDEEVYTAAREANAHEFISSFpdgYSTVVGER----------GTTLSGGQKQRLAIARALIKQPTVLI 346
Cdd:COG1245  408 -----QYISPD-YDGTVEEFLRSANTDDFGSSY---YKTEIIKPlgleklldknVKDLSGGELQRVAIAACLSRDADLYL 478

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 755511082 347 LDEATSALDAEsERV-VQEALDR--ASAGRTVLVIAH 380
Cdd:COG1245  479 LDEPSAHLDVE-QRLaVAKAIRRfaENRGKTAMVVDH 514

PRK10762

D-ribose transporter ATP binding protein; Provisional

205-409

3.70e-10

D-ribose transporter ATP binding protein; Provisional

Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.94 E-value: 3.70e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 205 FTLKlpSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVIGFISQEP----VLFATTIMEN 280
Cdd:PRK10762 273 FTLR--KGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISEDRkrdgLVLGMSVKEN 350

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 281 I----------RFGKLDASDEevytaaREAnAHEFISSF----PdGYSTVVGErgttLSGGQKQRLAIARALIKQPTVLI 346
Cdd:PRK10762 351 MsltalryfsrAGGSLKHADE------QQA-VSDFIRLFniktP-SMEQAIGL----LSGGNQQKVAIARGLMTRPKVLI 418

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 347 LDEATSALDAESERVVQEALDRASA-GRTVLVIAHRLSTVRA-AHSIIVMANGQVC-----EAGTHEELL 409
Cdd:PRK10762 419 LDEPTRGVDVGAKKEIYQLINQFKAeGLSIILVSSEMPEVLGmSDRILVMHEGRISgeftrEQATQEKLM 488

3a01205

TIGR00956

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

212-385

4.65e-10

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

Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 62.05 E-value: 4.65e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   212 GKIVALVGQSGGGKTTvasLLERFYDPEAGSVTLDGHDL---RTLNPSWLRgqVIGFISQEPVLFAT-TIMENIRFGKLD 287
Cdd:TIGR00956  789 GTLTALMGASGAGKTT---LLNVLAERVTTGVITGGDRLvngRPLDSSFQR--SIGYVQQQDLHLPTsTVRESLRFSAYL 863

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   288 ASDEEVYTAAREANAHEFI-----SSFPDGystVVGERGTTLSGGQKQRLAIARALIKQPTVLI-LDEATSALDAESERV 361
Cdd:TIGR00956  864 RQPKSVSKSEKMEYVEEVIkllemESYADA---VVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWS 940

                          170       180
                   ....*....|....*....|....*
gi 755511082   362 VQEALDR-ASAGRTVLVIAHRLSTV 385
Cdd:TIGR00956  941 ICKLMRKlADHGQAILCTIHQPSAI 965

AAA

smart00382

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

211-392

6.28e-10

Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 57.38 E-value: 6.28e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   211 SGKIVALVGQSGGGKTTVASLLERFYDPEAGSVtldghdlRTLNPSWLRGQVIGFISQEPVlfattimenirfgkldasd 290
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV-------IYIDGEDILEEVLDQLLLIIV------------------- 54

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   291 eevytaareanahefissfpdgystvvGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALD--- 367
Cdd:smart00382  55 ---------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrl 107

                          170       180
                   ....*....|....*....|....*....
gi 755511082   368 ----RASAGRTVLVIAHRLSTVRAAHSII 392
Cdd:smart00382 108 llllKSEKNLTVILTTNDEKDLGPALLRR 136

ugpC

PRK11650

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

183-408

6.68e-10

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

Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 60.24 E-value: 6.68e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 183 SITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTT----VASLlERFydpEAGSVTLDGHDLRTLNPSwL 258
Cdd:PRK11650   3 GLKLQAVRKSYD--GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTllrmVAGL-ERI---TSGEIWIGGRVVNELEPA-D 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 259 RGqvIGFISQEPVLFA-TTIMENIRFG----KLDAS--DEEVYTAAREANAHEFISSFPdgystvvgergTTLSGGQKQR 331
Cdd:PRK11650  76 RD--IAMVFQNYALYPhMSVRENMAYGlkirGMPKAeiEERVAEAARILELEPLLDRKP-----------RELSGGQRQR 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 332 LAIARALIKQPTVLILDEATSALDAE---SERVVQEALDRaSAGRTVLVIAHrlSTVRA---AHSIIVMANGQVCEAGTH 405
Cdd:PRK11650 143 VAMGRAIVREPAVFLFDEPLSNLDAKlrvQMRLEIQRLHR-RLKTTSLYVTH--DQVEAmtlADRVVVMNGGVAEQIGTP 219


                 ...
gi 755511082 406 EEL 408
Cdd:PRK11650 220 VEV 222

PRK15093

peptide ABC transporter ATP-binding protein SapD;

206-409

7.29e-10

peptide ABC transporter ATP-binding protein SapD;

Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 60.20 E-value: 7.29e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 206 TLKLPSGKIVALVGQSGGGKTTVASLL----ERFYDPEAGSVTLDGHDLRTLNPSWLR---GQVIGFISQEP-------V 271
Cdd:PRK15093  27 SMTLTEGEIRGLVGESGSGKSLIAKAIcgvtKDNWRVTADRMRFDDIDLLRLSPRERRklvGHNVSMIFQEPqscldpsE 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 272 LFATTIMENI-----------RFGKLDASDEEVYTAAREANAHEFISSFPdgYStvvgergttLSGGQKQRLAIARALIK 340
Cdd:PRK15093 107 RVGRQLMQNIpgwtykgrwwqRFGWRKRRAIELLHRVGIKDHKDAMRSFP--YE---------LTEGECQKVMIAIALAN 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755511082 341 QPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTV-RAAHSIIVMANGQVCEAGTHEELL 409
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTTQAQIFRLLTRlnQNNNTTILLISHDLQMLsQWADKINVLYCGQTVETAPSKELV 247

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

202-441

7.68e-10

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 61.29 E-value: 7.68e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 202 LKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRtlNPSWlRGQV---IGFISQ------EPVL 272
Cdd:NF033858  17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DARH-RRAVcprIAYMPQglgknlYPTL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 273 fatTIMENIRF-GKL---DAsdeevytAAREANAHEF-----ISSFPD---GystvvgergtTLSGGQKQRLAIARALIK 340
Cdd:NF033858  94 ---SVFENLDFfGRLfgqDA-------AERRRRIDELlratgLAPFADrpaG----------KLSGGMKQKLGLCCALIH 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 341 QPTVLILDEATSALDAESERVVQEALDRASAGR---TVLViahrlSTV------RAAHsIIVMANGQVCEAGTHEELLKK 411
Cdd:NF033858 154 DPDLLILDEPTTGVDPLSRRQFWELIDRIRAERpgmSVLV-----ATAymeeaeRFDW-LVAMDAGRVLATGTPAELLAR 227

                        250       260       270
                 ....*....|....*....|....*....|
gi 755511082 412 GGlyselirRQTLDASLTSTPPAEKPEDPK 441
Cdd:NF033858 228 TG-------ADTLEAAFIALLPEEKRRGHQ 250

PRK13538

cytochrome c biogenesis heme-transporting ATPase CcmA;

204-389

8.13e-10

cytochrome c biogenesis heme-transporting ATPase CcmA;

Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 58.28 E-value: 8.13e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 204 DFTLKlpSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLR-----GQVIGFisqEPVLfatTIM 278
Cdd:PRK13538  21 SFTLN--AGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQdllylGHQPGI---KTEL---TAL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 279 ENIRF-GKL-DASDEEVYTAAREAnahefissfpdgystvVGERGT------TLSGGQKQRLAIARALIKQPTVLILDEA 350
Cdd:PRK13538  93 ENLRFyQRLhGPGDDEALWEALAQ----------------VGLAGFedvpvrQLSAGQQRRVALARLWLTRAPLWILDEP 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 755511082 351 TSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRAAH 389
Cdd:PRK13538 157 FTAIDKQGVARLEALLAQhAEQGGMVILTTHQDLPVASDK 196

ABC_RNaseL_inhibitor_domain2

cd03237

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...

202-380

9.10e-10

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: 58.96 E-value: 9.10e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 202 LKDFTLKLPSG-----KIVALVGQSGGGKTTVASLLerfydpeAGSVTLDGHDLRTLNPSwlrgqvIGFISQEPVLFATT 276
Cdd:cd03237   10 LGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKML-------AGVLKPDEGDIEIELDT------VSYKPQYIKADYEG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 277 IMENIRFGKLDASDEEVYTAAREANahefissfPDGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDA 356
Cdd:cd03237   77 TVRDLLSSITKDFYTHPYFKTEIAK--------PLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDV 148

                        170       180
                 ....*....|....*....|....*.
gi 755511082 357 ESERVVQEALDR--ASAGRTVLVIAH 380
Cdd:cd03237  149 EQRLMASKVIRRfaENNEKTAFVVEH 174

PvdE

COG4615

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...

183-380

1.31e-09

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: 60.20 E-value: 1.31e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 183 SITFQNVTFSYPC---RPGFnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLR 259
Cdd:COG4615  327 TLELRGVTYRYPGedgDEGF-TLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYR 405

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 260 gQVIGFISQEPVLFATTImenirfGKLDASDEEVytaareanAHEFIS--------SFPDG-YSTvvgergTTLSGGQKQ 330
Cdd:COG4615  406 -QLFSAVFSDFHLFDRLL------GLDGEADPAR--------ARELLErleldhkvSVEDGrFST------TDLSQGQRK 464

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 755511082 331 RLAIARALIKQPTVLILDEATSALDAESERVVQEAL--DRASAGRTVLVIAH 380
Cdd:COG4615  465 RLALLVALLEDRPILVFDEWAADQDPEFRRVFYTELlpELKARGKTVIAISH 516

PRK11819

putative ABC transporter ATP-binding protein; Reviewed

184-380

1.89e-09

putative ABC transporter ATP-binding protein; Reviewed

Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 59.75 E-value: 1.89e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYpcrpGFNVL-KDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLdghdlrtlnpswlrGQ- 261
Cdd:PRK11819 325 IEAENLSKSF----GDRLLiDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI--------------GEt 386

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 262 -VIGFISQ-----EPvlfATTIMENIrfgkldaSD--EEVYTAAREANAHEFISSF----PDgYSTVVGergtTLSGGQK 329
Cdd:PRK11819 387 vKLAYVDQsrdalDP---NKTVWEEI-------SGglDIIKVGNREIPSRAYVGRFnfkgGD-QQKKVG----VLSGGER 451

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755511082 330 QRLAIARALIKQPTVLILDEATSALDAESERVVQEALDrASAGrTVLVIAH 380
Cdd:PRK11819 452 NRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALL-EFPG-CAVVISH 500

PRK13409

ribosome biogenesis/translation initiation ATPase RLI;

205-382

2.83e-09

ribosome biogenesis/translation initiation ATPase RLI;

Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 59.05 E-value: 2.83e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 205 FTL-KLPS---GKIVALVGQSGGGKTTVASLLerfydpeAGSVT--LDGHDLrtlNPSWlrgqvigfisqEPVL--FATT 276
Cdd:PRK13409  88 FKLyGLPIpkeGKVTGILGPNGIGKTTAVKIL-------SGELIpnLGDYEE---EPSW-----------DEVLkrFRGT 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 277 IMENIrFGKLdaSDEEVyTAAREANAHEFISSFPDGysTV------VGERG-------------------TTLSGGQKQR 331
Cdd:PRK13409 147 ELQNY-FKKL--YNGEI-KVVHKPQYVDLIPKVFKG--KVrellkkVDERGkldevverlglenildrdiSELSGGELQR 220

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 755511082 332 LAIARALIKQPTVLILDEATSALDAEsERV-VQEALDRASAGRTVLVIAHRL 382
Cdd:PRK13409 221 VAIAAALLRDADFYFFDEPTSYLDIR-QRLnVARLIRELAEGKYVLVVEHDL 271

PRK13540

cytochrome c biogenesis protein CcmA; Provisional

188-387

3.10e-09

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.50 E-value: 3.10e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 188 NVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWlrGQVIGFIS 267
Cdd:PRK13540   6 ELDFDYHDQP---LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTY--QKQLCFVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 268 QE----PVLfatTIMENIRFgkldasdeEVYTAAREANAHEFISSFPDGYstVVGERGTTLSGGQKQRLAIARALIKQPT 343
Cdd:PRK13540  81 HRsginPYL---TLRENCLY--------DIHFSPGAVGITELCRLFSLEH--LIDYPCGLLSSGQKRQVALLRLWMSKAK 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 755511082 344 VLILDEATSALDAESERVVQEALD--RASAGRTVLVIAHRLSTVRA 387
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQehRAKGGAVLLTSHQDLPLNKA 193

ycf16

CHL00131

sulfate ABC transporter protein; Validated

201-418

6.28e-09

sulfate ABC transporter protein; Validated

Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 56.57 E-value: 6.28e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 201 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERF--YDPEAGSVTLDGHDLRTLNPSwLRGQVIGFIS-QEPVlfatTI 277
Cdd:CHL00131  22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHpaYKILEGDILFKGESILDLEPE-ERAHLGIFLAfQYPI----EI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 278 --MENIRFGKLDASDEEVYTAAREANAHEFISSFPDGySTVVGERGTTL--------SGGQKQRLAIARALIKQPTVLIL 347
Cdd:CHL00131  97 pgVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEK-LKLVGMDPSFLsrnvnegfSGGEKKRNEILQMALLDSELAIL 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755511082 348 DEATSALDAESERVVQEALDR-ASAGRTVLVIAH--RLSTVRAAHSIIVMANGQVCEAGTHE---ELLKKGglYSEL 418
Cdd:CHL00131 176 DETDSGLDIDALKIIAEGINKlMTSENSIILITHyqRLLDYIKPDYVHVMQNGKIIKTGDAElakELEKKG--YDWL 250

PRK15064

ABC transporter ATP-binding protein; Provisional

181-414

6.78e-09

ABC transporter ATP-binding protein; Provisional

Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 57.98 E-value: 6.78e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 181 RGSITFQNVTFSYPCRPGFnvlKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTldghdlrtlnpsWLRG 260
Cdd:PRK15064 317 RNALEVENLTKGFDNGPLF---KNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK------------WSEN 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 261 QVIGFISQEPVL-FAT--TIMENIRFGKLDASDEevyTAAREANAHEFISSfpDGystvVGERGTTLSGGQKQRLAIARA 337
Cdd:PRK15064 382 ANIGYYAQDHAYdFENdlTLFDWMSQWRQEGDDE---QAVRGTLGRLLFSQ--DD----IKKSVKVLSGGEKGRMLFGKL 452

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755511082 338 LIKQPTVLILDEATSALDAESERVVQEALDRASAgrTVLVIAHRLSTVR--AAHSIIVMANGQVCEAGTHEELLKKGGL 414
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMDMESIESLNMALEKYEG--TLIFVSHDREFVSslATRIIEITPDGVVDFSGTYEEYLRSQGI 529

sufC

PRK09580

cysteine desulfurase ATPase component; Reviewed

201-422

6.98e-09

cysteine desulfurase ATPase component; Reviewed

Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 56.34 E-value: 6.98e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 201 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLL--ERFYDPEAGSVTLDGHDLRTLNPSWLRGQVIGFISQEPV------- 271
Cdd:PRK09580  16 ILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLagREDYEVTGGTVEFKGKDLLELSPEDRAGEGIFMAFQYPVeipgvsn 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 272 -LFATTIMENIR-FGKLDASDEEVYTAAREANAHefISSFPDGYSTVVGERGttLSGGQKQRLAIARALIKQPTVLILDE 349
Cdd:PRK09580  96 qFFLQTALNAVRsYRGQEPLDRFDFQDLMEEKIA--LLKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELCILDE 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 350 ATSALDAESERVVQEALDRASAG-RTVLVIAHR---LSTVRAAHsIIVMANGQVCEAGTH---EELLKKGglYSELIRRQ 422
Cdd:PRK09580 172 SDSGLDIDALKIVADGVNSLRDGkRSFIIVTHYqriLDYIKPDY-VHVLYQGRIVKSGDFtlvKQLEEQG--YGWLTEQQ 248

ABC_6TM_YwjA_like

cd18549

Six-transmembrane helical domain of an uncharacterized ABC transporter YwjA and similar ...

1-127

7.12e-09

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: 56.69 E-value: 7.12e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   1 MLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAE----LESC 76
Cdd:cd18549  139 TINVPLTLIVFALLPLMIIFTIYFNKKMKKAFRRVREKIGEINAQLEDSLSGIRVVKAFANEEYEIEKFDEGndrfLESK 218

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 755511082  77 cckaEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFL 127
Cdd:cd18549  219 ----KKAYKAMAYFFSGMNFFTNLLNLVVLVAGGYFIIKGEITLGDLVAFL 265

Rli1

COG1245

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...

205-384

8.54e-09

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

Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 57.49 E-value: 8.54e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 205 FTL-KLP---SGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDghdlrtlnPSWlrgqvigfisqEPVL--FATTIM 278
Cdd:COG1245   88 FRLyGLPvpkKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEE--------PSW-----------DEVLkrFRGTEL 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 279 ENiRFGKLdaSDEEVyTAAREANAHEFISSFPDGysTV------VGERG-------------------TTLSGGQKQRLA 333
Cdd:COG1245  149 QD-YFKKL--ANGEI-KVAHKPQYVDLIPKVFKG--TVrellekVDERGkldelaeklglenildrdiSELSGGELQRVA 222

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755511082 334 IARALIKQPTVLILDEATSALD----AESERVVQEAldrASAGRTVLVIAHRLST 384
Cdd:COG1245  223 IAAALLRDADFYFFDEPSSYLDiyqrLNVARLIREL---AEEGKYVLVVEHDLAI 274

ABC_RNaseL_inhibitor_domain1

cd03236

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...

196-383

9.23e-09

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.

Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 55.84 E-value: 9.23e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 196 RPGFNVLKDFTLKLP-SGKIVALVGQSGGGKTTVASLLerfydpeAGSVT--LDGHDLrtlNPSWlrGQVIGFisqepvl 272
Cdd:cd03236    9 RYGPNSFKLHRLPVPrEGQVLGLVGPNGIGKSTALKIL-------AGKLKpnLGKFDD---PPDW--DEILDE------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 273 FATTIMEN----IRFGKLDASDEEVYT----AAREANAHEFISS-----FPDGYSTVVGERG------TTLSGGQKQRLA 333
Cdd:cd03236   70 FRGSELQNyftkLLEGDVKVIVKPQYVdlipKAVKGKVGELLKKkdergKLDELVDQLELRHvldrniDQLSGGELQRVA 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755511082 334 IARALIKQPTVLILDEATSALDAESE----RVVQEaldRASAGRTVLVIAHRLS 383
Cdd:cd03236  150 IAAALARDADFYFFDEPSSYLDIKQRlnaaRLIRE---LAEDDNYVLVVEHDLA 200

ABC_UvrA

cd03238

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...

202-398

9.31e-09

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: 54.64 E-value: 9.31e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 202 LKDFTLKLPSGKIVALVGQSGGGKTTVasLLERFYdpEAGSVTLDghDLRTLNPswlRGQVIgFISQEPVLFATTImeni 281
Cdd:cd03238   11 LQNLDVSIPLNVLVVVTGVSGSGKSTL--VNEGLY--ASGKARLI--SFLPKFS---RNKLI-FIDQLQFLIDVGL---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 282 rfgkldasdeevytaareanahefissfpdGYSTVvGERGTTLSGGQKQRLAIARALIKQP--TVLILDEATSALDAESE 359
Cdd:cd03238   77 ------------------------------GYLTL-GQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDI 125

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 755511082 360 RVVQEALDR-ASAGRTVLVIAHRLSTVRAAHSIIVMANGQ 398
Cdd:cd03238  126 NQLLEVIKGlIDLGNTVILIEHNLDVLSSADWIIDFGPGS 165

ABC_6TM_exporter_like

cd18563

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

2-157

1.85e-08

Pssm-ID: 350007 [Multi-domain] Cd Length: 296 Bit Score: 55.59 E-value: 1.85e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   2 LSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAE 81
Cdd:cd18563  141 LNWKLALLVLIPVPLVVWGSYFFWKKIRRLFHRQWRRWSRLNSVLNDTLPGIRVVKAFGQEKREIKRFDEANQELLDANI 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  82 ELGRGIALFQGLSNIafnCMVLGTLFI---GGSLVAGQQLKGGDLMSFLV-ASQTVQRsMASLSVLFGQVVRGLSAGARV 157
Cdd:cd18563  221 RAEKLWATFFPLLTF---LTSLGTLIVwyfGGRQVLSGTMTLGTLVAFLSyLGMFYGP-LQWLSRLNNWITRALTSAERI 296

UvrA

COG0178

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

322-410

2.41e-08

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

Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 56.57 E-value: 2.41e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 322 TTLSGGQKQRLAIARALIK---QPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRAAHSIIVM--- 394
Cdd:COG0178  825 TTLSGGEAQRVKLASELSKrstGKTLYILDEPTTGLHFHDIRKLLEVLHRlVDKGNTVVVIEHNLDVIKTADWIIDLgpe 904

                         90
                 ....*....|....*....
gi 755511082 395 ---ANGQVCEAGTHEELLK 410
Cdd:COG0178  905 ggdGGGEIVAEGTPEEVAK 923

3a01203

TIGR00954

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...

184-383

2.94e-08

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]

Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 55.91 E-value: 2.94e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  184 ITFQNVTFSYPcrPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDghdlrtlnpswlRGQVI 263
Cdd:TIGR00954 452 IKFENIPLVTP--NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP------------AKGKL 517

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  264 GFISQEPVLFATTIMENI-------RFGKLDASDEEVYTAAREANAHEFISSfpDGYSTVVGERGTTLSGGQKQRLAIAR 336
Cdd:TIGR00954 518 FYVPQRPYMTLGTLRDQIiypdsseDMKRRGLSDKDLEQILDNVQLTHILER--EGGWSAVQDWMDVLSGGEKQRIAMAR 595

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 755511082  337 ALIKQPTVLILDEATSALDAESERVVQEALDRasAGRTVLVIAHRLS 383
Cdd:TIGR00954 596 LFYHKPQFAILDECTSAVSVDVEGYMYRLCRE--FGITLFSVSHRKS 640

PRK13409

ribosome biogenesis/translation initiation ATPase RLI;

202-380

1.06e-07

ribosome biogenesis/translation initiation ATPase RLI;

Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 1.06e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 202 LKDFTLKLPSGKI-----VALVGQSGGGKTTVASLLERFYDPEAGSVTLDghdlrtlnpswLRgqvigfISQEPvlfatt 276
Cdd:PRK13409 350 LGDFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-----------LK------ISYKP------ 406

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 277 imENIRfgklDASDEEVYtaareanahEFISSFPDGYST---------------VVGERGTTLSGGQKQRLAIARALIKQ 341
Cdd:PRK13409 407 --QYIK----PDYDGTVE---------DLLRSITDDLGSsyykseiikplqlerLLDKNVKDLSGGELQRVAIAACLSRD 471

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 755511082 342 PTVLILDEATSALDAESERVVQEALDRASAGR--TVLVIAH 380
Cdd:PRK13409 472 ADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDH 512

ABC_6TM_exporter_like

cd18550

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

1-141

1.09e-07

Pssm-ID: 349994 [Multi-domain] Cd Length: 294 Bit Score: 53.26 E-value: 1.09e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   1 MLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEAL--GNVRTVRAFAMEKREEERYQAElesccc 78
Cdd:cd18550  136 ALDWRLALLSLVLLPLFVLPTRRVGRRRRKLTREQQEKLAELNSIMQETLsvSGALLVKLFGREDDEAARFARR------ 209

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  79 kAEELGR--------GIALFQGLSnIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSF--------------LVASQTVQRS 136
Cdd:cd18550  210 -SRELRDlgvrqalaGRWFFAALG-LFTAIGPALVYWVGGLLVIGGGLTIGTLVAFtallgrlygpltqlLNIQVDLMTS 287


                 ....*
gi 755511082 137 MASLS 141
Cdd:cd18550  288 LALFE 292

PRK15439

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

198-399

1.15e-07

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 53.90 E-value: 1.15e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 198 GFnvlKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNP---------------------- 255
Cdd:PRK15439 278 GF---RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTaqrlarglvylpedrqssglyl 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 256 -SWLRGQVIGFISQEPVLFATTIMENIRFgkldasdeEVYTAAREANahefissFPDGYSTVvgergTTLSGGQKQRLAI 334
Cdd:PRK15439 355 dAPLAWNVCALTHNRRGFWIKPARENAVL--------ERYRRALNIK-------FNHAEQAA-----RTLSGGNQQKVLI 414

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755511082 335 ARALIKQPTVLILDEATSALDAeSER--VVQEALDRASAGRTVLVIAHRLSTV-RAAHSIIVMANGQV 399
Cdd:PRK15439 415 AKCLEASPQLLIVDEPTRGVDV-SARndIYQLIRSIAAQNVAVLFISSDLEEIeQMADRVLVMHQGEI 481

40850658_otr

NF000106

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

300-420

1.23e-07

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

Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.20 E-value: 1.23e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 300 ANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVV-QEALDRASAGRTVLVI 378
Cdd:NF000106 123 ARADELLERF--SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVwDEVRSMVRDGATVLLT 200

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 755511082 379 AHRLSTV-RAAHSIIVMANGQVCEAGTHEELLKKGGLYSELIR 420
Cdd:NF000106 201 TQYMEEAeQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQIR 243

xylG

TIGR02633

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...

187-400

1.24e-07

Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 53.68 E-value: 1.24e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  187 QNVTFSYPCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKT-TVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVI-- 263
Cdd:TIGR02633 261 RNLTCWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGKPVDIRNPAQAIRAGIam 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  264 --------GFISQEPVLFATTIMENIRF---GKLDASDEE--VYTAAREANAHEFISSFPDGystvvgergtTLSGGQKQ 330
Cdd:TIGR02633 341 vpedrkrhGIVPILGVGKNITLSVLKSFcfkMRIDAAAELqiIGSAIQRLKVKTASPFLPIG----------RLSGGNQQ 410

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755511082  331 RLAIARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVC 400
Cdd:TIGR02633 411 KAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQlAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLK 482

COG4586

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

323-419

1.58e-07

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

Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 52.78 E-value: 1.58e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 323 TLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR--ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQV 399
Cdd:COG4586  154 QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEynRERGTTILLTSHDMDDIEAlCDRVIVIDHGRI 233

                         90       100
                 ....*....|....*....|
gi 755511082 400 CEAGTHEELLKKGGLYSELI 419
Cdd:COG4586  234 IYDGSLEELKERFGPYKTIV 253

tagH

PRK13545

teichoic acids export protein ATP-binding subunit; Provisional

184-409

1.78e-07

teichoic acids export protein ATP-binding subunit; Provisional

Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 53.36 E-value: 1.78e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPC--RPgFNVLKDF----------------TLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTL 245
Cdd:PRK13545   5 VKFEHVTKKYKMynKP-FDKLKDLffrskdgeyhyalnniSFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 246 DGHDLRTLNPSWLRGQVIGfisqepvlfattiMENIRFGKL--DASDEEVYTAAREANAHEFISSFpdgystvVGERGTT 323
Cdd:PRK13545  84 KGSAALIAISSGLNGQLTG-------------IENIELKGLmmGLTKEKIKEIIPEIIEFADIGKF-------IYQPVKT 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 324 LSGGQKQRLAIARALIKQPTVLILDEATSALDaesERVVQEALDRASA----GRTVLVIAHRLSTVRA-AHSIIVMANGQ 398
Cdd:PRK13545 144 YSSGMKSRLGFAISVHINPDILVIDEALSVGD---QTFTKKCLDKMNEfkeqGKTIFFISHSLSQVKSfCTKALWLHYGQ 220

                        250
                 ....*....|.
gi 755511082 399 VCEAGTHEELL 409
Cdd:PRK13545 221 VKEYGDIKEVV 231

ABC_6TM_PrtD_LapB_HlyB_like

cd18566

Six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems ...

2-126

3.16e-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: 3.16e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   2 LSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAE 81
Cdd:cd18566  139 LGGKLVLVPLVLLGLFVLVAILLGPILRRALKERSRADERRQNFLIETLTGIHTIKAMAMEPQMLRRYERLQANAAYAGF 218

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 755511082  82 ELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSF 126
Cdd:cd18566  219 KVAKINAVAQTLGQLFSQVSMVAVVAFGALLVINGDLTVGALIAC 263

PLN03140

ABC transporter G family member; Provisional

201-404

3.56e-07

ABC transporter G family member; Provisional

Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.93 E-value: 3.56e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  201 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLerfydpeAGSVT---LDGhDLRtlnpswlrgqVIGFISQEPVlFA--- 274
Cdd:PLN03140  895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVL-------AGRKTggyIEG-DIR----------ISGFPKKQET-FAris 955

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  275 ------------TTIMENIRFGKL-----DASDEEVYTAAREANAHEFISSFPDgysTVVGERGTT-LSGGQKQRLAIAR 336
Cdd:PLN03140  956 gyceqndihspqVTVRESLIYSAFlrlpkEVSKEEKMMFVDEVMELVELDNLKD---AIVGLPGVTgLSTEQRKRLTIAV 1032

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755511082  337 ALIKQPTVLILDEATSALDAESERVVQEAL-DRASAGRTVLVIAHRLS--TVRAAHSIIVMA-NGQVCEAGT 404
Cdd:PLN03140 1033 ELVANPSIIFMDEPTSGLDARAAAIVMRTVrNTVDTGRTVVCTIHQPSidIFEAFDELLLMKrGGQVIYSGP 1104

PRK10938

putative molybdenum transport ATP-binding protein ModF; Provisional

184-385

3.97e-07

putative molybdenum transport ATP-binding protein ModF; Provisional

Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 52.32 E-value: 3.97e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPgfnVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYdPEAGS--VTLDGHDLRTLNPSWLRGQ 261
Cdd:PRK10938 261 IVLNNGVVSYNDRP---ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDH-PQGYSndLTLFGRRRGSGETIWDIKK 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 262 VIGFISQEPVL---FATTIMENIRFGKLDASDeeVYTAAREAN---AHEFISSFpdGYSTVVGERG-TTLSGGQkQRLA- 333
Cdd:PRK10938 337 HIGYVSSSLHLdyrVSTSVRNVILSGFFDSIG--IYQAVSDRQqklAQQWLDIL--GIDKRTADAPfHSLSWGQ-QRLAl 411

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755511082 334 IARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLV------------IAHRLSTV 385
Cdd:PRK10938 412 IVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVlISEGETQLLfvshhaedapacITHRLEFV 476

ABC_RNaseL_inhibitor

cd03222

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...

311-398

3.98e-07

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.

Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 49.88 E-value: 3.98e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 311 DGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRAS--AGRTVLVIAHRLSTVRAA 388
Cdd:cd03222   59 DGITPVYKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSeeGKKTALVVEHDLAVLDYL 138

                         90
                 ....*....|
gi 755511082 389 HSIIVMANGQ 398
Cdd:cd03222  139 SDRIHVFEGE 148

rim_protein

TIGR01257

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...

212-413

4.29e-07

Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 52.71 E-value: 4.29e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   212 GKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTlNPSWLRgQVIGFISQepvlfattimenirFGKLD---A 288
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVH-QNMGYCPQ--------------FDAIDdllT 2028

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   289 SDEEVYTAAR---------EANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDAESE 359
Cdd:TIGR01257 2029 GREHLYLYARlrgvpaeeiEKVANWSIQSL--GLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 755511082   360 RVVQEAL-DRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEELLKKGG 413
Cdd:TIGR01257 2107 RMLWNTIvSIIREGRAVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQHLKSKFG 2162

PRK10982

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

312-415

5.18e-07

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 51.65 E-value: 5.18e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 312 GYSTVVGergtTLSGGQKQRLAIARALIKQPTVLILDEATSALD--AESErVVQEALDRASAGRTVLVIAHRLSTVRA-A 388
Cdd:PRK10982 384 GHRTQIG----SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDvgAKFE-IYQLIAELAKKDKGIIIISSEMPELLGiT 458

                         90       100       110
                 ....*....|....*....|....*....|....
gi 755511082 389 HSIIVMANGQVceAG-------THEELLKKGGLY 415
Cdd:PRK10982 459 DRILVMSNGLV--AGivdtkttTQNEILRLASLH 490

uvrA

PRK00349

excinuclease ABC subunit UvrA;

312-415

6.32e-07

excinuclease ABC subunit UvrA;

Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 52.00 E-value: 6.32e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 312 GYSTVvGERGTTLSGGQKQRLAIARALIKQPT---VLILDEATSALDAESER----VVQEALDRasaGRTVLVIAHRLST 384
Cdd:PRK00349 820 GYIKL-GQPATTLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDIRklleVLHRLVDK---GNTVVVIEHNLDV 895

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 755511082 385 VRAAHSIIVM------ANGQVCEAGTHEELLKKGGLY 415
Cdd:PRK00349 896 IKTADWIIDLgpeggdGGGEIVATGTPEEVAKVEASY 932

PRK13546

teichoic acids export ABC transporter ATP-binding subunit TagH;

199-411

9.39e-07

teichoic acids export ABC transporter ATP-binding subunit TagH;

Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.20 E-value: 9.39e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 199 FNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVIGfisqepvlfattiM 278
Cdd:PRK13546  37 FFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTG-------------I 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 279 ENIRFGKL--DASDEEVYTAARE----ANAHEFISSFPDGYSTvvgergttlsgGQKQRLAIARALIKQPTVLILDEATS 352
Cdd:PRK13546 104 ENIEFKMLcmGFKRKEIKAMTPKiiefSELGEFIYQPVKKYSS-----------GMRAKLGFSINITVNPDILVIDEALS 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755511082 353 ALDaesERVVQEALDR----ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEELLKK 411
Cdd:PRK13546 173 VGD---QTFAQKCLDKiyefKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDYGELDDVLPK 233

PRK10938

putative molybdenum transport ATP-binding protein ModF; Provisional

207-437

9.79e-07

putative molybdenum transport ATP-binding protein ModF; Provisional

Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 9.79e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 207 LKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTL---------NPSWLRGQViGFISQEPVLFATTI 277
Cdd:PRK10938  24 LTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLsfeqlqklvSDEWQRNNT-DMLSPGEDDTGRTT 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 278 MENIRfgkldasdEEVYTAAR-EANAHEFissfpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSALDA 356
Cdd:PRK10938 103 AEIIQ--------DEVKDPARcEQLAQQF------GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDV 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 357 ESERVVQEALDR-ASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEELLKKgGLYSELIRRQTLDAslTSTPPA 434
Cdd:PRK10938 169 ASRQQLAELLASlHQSGITLVLVLNRFDEIPDfVQFAGVLADCTLAETGEREEILQQ-ALVAQLAHSEQLEG--VQLPEP 245


                 ...
gi 755511082 435 EKP 437
Cdd:PRK10938 246 DEP 248

PRK13541

cytochrome c biogenesis protein CcmA; Provisional

184-388

1.14e-06

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.10 E-value: 1.14e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPGFNVLKDFtlkLPSGkIVALVGQSGGGKTTVASLLERFYDPEAGSVTLdghdlRTLNPSWLRGQVI 263
Cdd:PRK13541   2 LSLHQLQFNIEQKNLFDLSITF---LPSA-ITYIKGANGCGKSSLLRMIAGIMQPSSGNIYY-----KNCNINNIAKPYC 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQEPVL-FATTIMENIRF-GKLDASDEEVYTAAREANAHEFISsfpdgystvvgERGTTLSGGQKQRLAIARALIKQ 341
Cdd:PRK13541  73 TYIGHNLGLkLEMTVFENLKFwSEIYNSAETLYAAIHYFKLHDLLD-----------EKCYSLSSGMQKIVAIARLIACQ 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 755511082 342 PTVLILDEATSALDAESERVVQEALD-RASAGRTVLVIAHRLSTVRAA 388
Cdd:PRK13541 142 SDLWLLDEVETNLSKENRDLLNNLIVmKANSGGIVLLSSHLESSIKSA 189

PRK09700

D-allose ABC transporter ATP-binding protein AlsA;

187-410

1.28e-06

D-allose ABC transporter ATP-binding protein AlsA;

Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 50.55 E-value: 1.28e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 187 QNVTfsypcRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTtvaSLLERFY--DPEA-GSVTLDGHDLRTLNPSWLRGQVI 263
Cdd:PRK09700 269 RNVT-----SRDRKKVRDISFSVCRGEILGFAGLVGSGRT---ELMNCLFgvDKRAgGEIRLNGKDISPRSPLDAVKKGM 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 264 GFISQ---EPVLFAT-TIMENIR-------------FGKLDASDEEVYTAAREANAHEFISSfpdgystvVGERGTTLSG 326
Cdd:PRK09700 341 AYITEsrrDNGFFPNfSIAQNMAisrslkdggykgaMGLFHEVDEQRTAENQRELLALKCHS--------VNQNITELSG 412

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 327 GQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRAA-HSIIVMANGQV----- 399
Cdd:PRK09700 413 GNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVcDRIAVFCEGRLtqilt 492

                        250
                 ....*....|..
gi 755511082 400 -CEAGTHEELLK 410
Cdd:PRK09700 493 nRDDMSEEEIMA 504

ABC_6TM_YknV_like

cd18545

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

2-157

1.77e-06

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: 49.39 E-value: 1.77e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   2 LSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQaELESCCCKAE 81
Cdd:cd18545  138 LNVRLALVTLAVLPLLVLVVFLLRRRARKAWQRVRKKISNLNAYLHESISGIRVIQSFAREDENEEIFD-ELNRENRKAN 216

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755511082  82 ElgRGIALFQGLSNIAFNCMVLGT---LFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 157
Cdd:cd18545  217 M--RAVRLNALFWPLVELISALGTalvYWYGGKLVLGGAITVGVLVAFIGYVGRFWQPIRNLSNFYNQLQSAMASAERI 293

PRK10982

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

197-398

2.06e-06

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 2.06e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 197 PGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPSWLRGQVIGFISQE-PVLFAT 275
Cdd:PRK10982   9 PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQElNLVLQR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 276 TIMENIRFGK-----LDASDEEVYTAAREANAHEFISSFPDgystvvgERGTTLSGGQKQRLAIARALIKQPTVLILDEA 350
Cdd:PRK10982  89 SVMDNMWLGRyptkgMFVDQDKMYRDTKAIFDELDIDIDPR-------AKVATLSVSQMQMIEIAKAFSYNAKIVIMDEP 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755511082 351 TSALdAESE-----RVVQEALDRasaGRTVLVIAHRLSTV-RAAHSIIVMANGQ 398
Cdd:PRK10982 162 TSSL-TEKEvnhlfTIIRKLKER---GCGIVYISHKMEEIfQLCDEITILRDGQ 211

PLN03073

ABC transporter F family; Provisional

184-380

2.30e-06

ABC transporter F family; Provisional

Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 2.30e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 184 ITFQNVTFSYPCRPGFNVLKDFTLKLPSGkiVALVGQSGGGKTTVASLLERFYDPEAGSV--------------TLDGHD 249
Cdd:PLN03073 509 ISFSDASFGYPGGPLLFKNLNFGIDLDSR--IAMVGPNGIGKSTILKLISGELQPSSGTVfrsakvrmavfsqhHVDGLD 586

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 250 LrtlnpswlrgqvigfiSQEPVLFATtimenirfgkldasdeEVYTAAREANAHEFISSFpdGYS-TVVGERGTTLSGGQ 328
Cdd:PLN03073 587 L----------------SSNPLLYMM----------------RCFPGVPEQKLRAHLGSF--GVTgNLALQPMYTLSGGQ 632

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 755511082 329 KQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASAGrtVLVIAH 380
Cdd:PLN03073 633 KSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGG--VLMVSH 682

araG

PRK11288

L-arabinose ABC transporter ATP-binding protein AraG;

211-407

3.07e-06

L-arabinose ABC transporter ATP-binding protein AraG;

Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 49.52 E-value: 3.07e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 211 SGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNPswlrGQVI--GFI------SQEPVLFATTIMENI- 281
Cdd:PRK11288 278 AGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSP----RDAIraGIMlcpedrKAEGIIPVHSVADNIn 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 282 --------RFGKLdasdeevYTAAREA-NAHEFISSF----PDGYSTVVgergtTLSGGQKQRLAIARALIKQPTVLILD 348
Cdd:PRK11288 354 isarrhhlRAGCL-------INNRWEAeNADRFIRSLniktPSREQLIM-----NLSGGNQQKAILGRWLSEDMKVILLD 421

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755511082 349 EATSALD--AESErVVQEALDRASAGRTVLVIAHRLSTVRA-AHSIIVMANGQVCEAGTHEE 407
Cdd:PRK11288 422 EPTRGIDvgAKHE-IYNVIYELAAQGVAVLFVSSDLPEVLGvADRIVVMREGRIAGELAREQ 482

ABC_6TM_exporter_like

cd18778

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

2-157

3.60e-06

Pssm-ID: 350051 [Multi-domain] Cd Length: 293 Bit Score: 48.30 E-value: 3.60e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   2 LSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAelescccKAE 81
Cdd:cd18778  138 INPKLALLTLIPIPFLALGAWLYSKKVRPRYRKVREALGELNALLQDNLSGIREIQAFGREEEEAKRFEA-------LSR 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  82 ELGRGI--ALFqgLSNIAFNCMV----LGT---LFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLS 152
Cdd:cd18778  211 RYRKAQlrAMK--LWAIFHPLMEfltsLGTvlvLGFGGRLVLAGELTIGDLVAFLLYLGLFYEPITSLHGLNEMLQRALA 288


                 ....*
gi 755511082 153 AGARV 157
Cdd:cd18778  289 GAERV 293

ABC_6TM_Rv0194_D2_like

cd18546

Six-transmembrane helical domain 2 (TMD2) of the multidrug efflux ABC transporter Rv0194 and ...

2-127

3.98e-06

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: 48.25 E-value: 3.98e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   2 LSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKAE 81
Cdd:cd18546  137 LDPRLALVALAALPPLALATRWFRRRSSRAYRRARERIAAVNADLQETLAGIRVVQAFRRERRNAERFAELSDDYRDARL 216

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 755511082  82 ELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFL 127
Cdd:cd18546  217 RAQRLVAIYFPGVELLGNLATAAVLLVGAWRVAAGTLTVGVLVAFL 262

PRK13549

xylose transporter ATP-binding subunit; Provisional

182-355

4.48e-06

xylose transporter ATP-binding subunit; Provisional

Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.77 E-value: 4.48e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 182 GSITFQ--NVTFSYPCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKT-TVASLLERFYDPEAGSVTLDGHDLRTLNPSWL 258
Cdd:PRK13549 256 GEVILEvrNLTAWDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTeLVQCLFGAYPGRWEGEIFIDGKPVKIRNPQQA 335

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 259 RGQVIGFISQE-------PVLfatTIMENI---------RFGKLDASDEEvyTAAREANAHEFI-SSFPDgystvvgERG 321
Cdd:PRK13549 336 IAQGIAMVPEDrkrdgivPVM---GVGKNItlaaldrftGGSRIDDAAEL--KTILESIQRLKVkTASPE-------LAI 403

                        170       180       190
                 ....*....|....*....|....*....|....
gi 755511082 322 TTLSGGQKQRLAIARALIKQPTVLILDEATSALD 355
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGID 437

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

204-355

4.82e-06

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 48.97 E-value: 4.82e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 204 DFT------LKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTL-----DGHDLRTlnpswlRGQViGFISQEPVL 272
Cdd:NF033858 278 DFTavdhvsFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDAGDIAT------RRRV-GYMSQAFSL 350

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 273 FAT-TIMENIrfgKLDASDEEVYTAAREANAHEFISSFpdGYSTVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEAT 351
Cdd:NF033858 351 YGElTVRQNL---ELHARLFHLPAAEIAARVAEMLERF--DLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425


                 ....
gi 755511082 352 SALD 355
Cdd:NF033858 426 SGVD 429

ABC_6TM_Pgp_ABCB1

cd18558

Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; ...

5-74

5.06e-06

Six-transmembrane helical domain of P-glycoprotein 1 (Pgp) and related proteins; P-glycoprotein 1 (permeability glycoprotein, Pgp) also known as multidrug resistance protein 1 (MDR1) or ATP-binding cassette sub-family B member 1(ABCB1) is a member of the superfamily of ATP-binding cassette (ABC) transporters. Pgp acts as an ATP-dependent efflux pump, binds drugs with diverse chemical structures and pump them out of the drug resistant cancer cells. It is responsible for decreased drug accumulation in multidrug-resistant cells and mediates the development of resistance to anticancer drugs. Pgp consists of two alpha-helical transmembrane domains (TMDs) and two cytoplasmic nucleotide-binding domains (NBDs). This protein also functions as a transporter in the blood-brain barrier. In addition to Pgp, breast cancer resistance protein (BCRP/MXR/ABC-P/ABCG2) and multidrug resistance-associated proteins (MRP1/ABCC1 and MRP2/ABCC2) function as drug efflux pumps of anticancer drugs, and overexpression of these transporters induces multidrug resistance to a broad spectrum of anticancer drugs including doxorubicin, taxol, and vinca alkaloids by actively pumping the drugs out of cells.

Pssm-ID: 350002 [Multi-domain] Cd Length: 312 Bit Score: 48.04 E-value: 5.06e-06

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   5 RLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELE 74
Cdd:cd18558  160 KLTLVILAISPVLGLSAVVWAKILSGFTDKEKKAYAKAGAVAEEVLEAFRTVIAFGGQQKEETRYAQNLE 229

ABC_6TM_PCAT1_LagD_like

cd18570

Six-transmembrane helical domain (6-TMD) of the peptidase-containing ATP-binding cassette ...

1-157

8.41e-06

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: 47.44 E-value: 8.41e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   1 MLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKA 80
Cdd:cd18570  138 FYNWKLFLITLLIIPLYILIILLFNKPFKKKNREVMESNAELNSYLIESLKGIETIKSLNAEEQFLKKIEKKFSKLLKKS 217

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755511082  81 EELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSAGARV 157
Cdd:cd18570  218 FKLGKLSNLQSSIKGLISLIGSLLILWIGSYLVIKGQLSLGQLIAFNALLGYFLGPIENLINLQPKIQEAKVAADRL 294

ABC_6TM_PrtD_LapB_HlyB_like

cd18782

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in ...

1-141

8.54e-06

uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (PrtD, LapB, HylB), and similar proteins; Uncharacterized subgroup of the six-transmembrane helical domain (6-TMD) of the ABC subunit in the type 1 secretion systems (T1SS), including PrtD, LapB, and HylB. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type 1 secretion apparatus. In the case of the Escherichia coli HlyA T1SS, these three proteins are HlyB (a dimeric ABC transporter), HlyD (MFP, oligomeric membrane fusion protein) and TolC (OMP, a trimeric oligomeric outer membrane protein). These three components assemble into a complex spanning both membranes and provide a channel for the translocation of unfolded polypeptides. In addition, PrtD is the integral membrane ATP-binding cassette component of the Erwinia chrysanthemi metalloprotease secretion system (PrtDEF). LabB is an inner-membrane transporter component of the LapBCE system that is required for the secretion of the LapA adhesion.

Pssm-ID: 350055 [Multi-domain] Cd Length: 294 Bit Score: 47.20 E-value: 8.54e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   1 MLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCKA 80
Cdd:cd18782  138 SYSPLLTLVVLATVPLQLLLTFLFGPILRRQIRRRAEASAKTQSYLVESLTGIQTVKAQNAELKARWRWQNRYARSLGEG 217

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755511082  81 EELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLS 141
Cdd:cd18782  218 FKLTVLGTTSGSLSQFLNKLSSLLVLWVGAYLVLRGELTLGQLIAFRILSGYVTGPILRLS 278

PRK00635

excinuclease ABC subunit A; Provisional

322-443

8.68e-06

excinuclease ABC subunit A; Provisional

Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.29 E-value: 8.68e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  322 TTLSGGQKQRLAIARALI---KQPTVLILDEATSALDAES-ERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMA-- 395
Cdd:PRK00635  808 SSLSGGEIQRLKLAYELLapsKKPTLYVLDEPTTGLHTHDiKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELGpe 887

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 755511082  396 ----NGQVCEAGTHEELLKKGGLYSELIR---RQTLDASLTSTPPaekPEDPKSC 443
Cdd:PRK00635  888 ggnlGGYLLASCSPEELIHLHTPTAKALRpylSSPQELPYLPDPS---PKPPVPA 939

SbcC

COG0419

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];

198-380

9.10e-06

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];

Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 46.54 E-value: 9.10e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 198 GFNVLKD-FTLKLPSGkIVALVGQSGGGKTTV---------------ASLLERF--YDPEAGSVTLD-GHDLRTLNPSWL 258
Cdd:COG0419    9 NFRSYRDtETIDFDDG-LNLIVGPNGAGKSTIleairyalygkarsrSKLRSDLinVGSEEASVELEfEHGGKRYRIERR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 259 RGQVIGFISQEP--------VLFATTIMENI--RFGKLDASDEEVYTAAREANA--HEFISSFpDGYSTVvgergTTLSG 326
Cdd:COG0419   88 QGEFAEFLEAKPserkealkRLLGLEIYEELkeRLKELEEALESALEELAELQKlkQEILAQL-SGLDPI-----ETLSG 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755511082 327 GQKQRLAIARALikqptVLILDeaTSALDAESERVVQEALDRASagrtvlVIAH 380
Cdd:COG0419  162 GERLRLALADLL-----SLILD--FGSLDEERLERLLDALEELA------IITH 202

ABC_6TM_HetC_like

cd18568

Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar ...

3-143

1.61e-05

Six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS-like HetC and similar proteins; This group represents the six-transmembrane helical domain (6-TMD) of the ABC subunit of T1SS (type 1 secretion systems), such as heterocyst differentiation protein HetC. HetC is similar to ABC protein exporters of T1SS (type 1 secretion systems) and is involved in early regulation of heterocyst differentiation in the filamentous cynobacterium Anabaena sp. T1SS are found in pathogenic Gram-negative bacteria (such as Escherichia coli, Vibrio cholerae or Bordetella pertussis) to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. ABC-transporter proteins in this group carry a proteolytic peptidase domain in their N-termini, termed as C39, which cleaves a double glycine (GG) motif-containing signal peptide from substrates before secretion.

Pssm-ID: 350012 [Multi-domain] Cd Length: 294 Bit Score: 46.40 E-value: 1.61e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   3 SPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAME----KREEERYQAELESccc 78
Cdd:cd18568  140 NLQLTLIVLAFIPLYVLLTLLSSPKLKRNSREIFQANAEQQSFLVEALTGIATIKALAAErpirWRWENKFAKALNT--- 216

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755511082  79 kaeELgRGIALFQGLSNIAFNCMVLGT---LFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVL 143
Cdd:cd18568  217 ---RF-RGQKLSIVLQLISSLINHLGTiavLWYGAYLVISGQLTIGQLVAFNMLFGSVINPLLALVGL 280

ABC_6TM_CyaB_HlyB_like

cd18588

Six-transmembrane helical domain of the ABC subunits of T1SS, CyaB/HylB, and similar proteins; ...

1-134

2.58e-05

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: 45.95 E-value: 2.58e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   1 MLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELesccckA 80
Cdd:cd18588  138 YYSPTLTLIVLASLPLYALLSLLVTPILRRRLEEKFQRGAENQSFLVETVTGIETVKSLAVEPQFQRRWEELL------A 211

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755511082  81 EELGRGIALfQGLSNIAFN-------CMVLGTLFIGGSLVAGQQLKGGDLMSF-LVASQTVQ 134
Cdd:cd18588  212 RYVKASFKT-ANLSNLASQivqliqkLTTLAILWFGAYLVMDGELTIGQLIAFnMLAGQVSQ 272

GguA

NF040905

sugar ABC transporter ATP-binding protein;

194-378

3.59e-05

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 45.94 E-value: 3.59e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 194 PCRPGFNVLKDFTLKLPSGKIVALVGQSGGGKTTVA-SLLERFYDP-EAGSVTLDGHDLRTLNPSWLRGQVIGFISQEP- 270
Cdd:NF040905 268 PLHPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAmSVFGRSYGRnISGTVFKDGKEVDVSTVSDAIDAGLAYVTEDRk 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 271 ----VLfATTIMENIRFGKLDA-SDEEVYTAAREAN-AHEFISSF----PDGYSTVVgergtTLSGGQKQRLAIARALIK 340
Cdd:NF040905 348 gyglNL-IDDIKRNITLANLGKvSRRGVIDENEEIKvAEEYRKKMniktPSVFQKVG-----NLSGGNQQKVVLSKWLFT 421

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 755511082 341 QPTVLILDEATSALD--AESE--RVVQEAldrASAGRTVLVI 378
Cdd:NF040905 422 DPDVLILDEPTRGIDvgAKYEiyTIINEL---AAEGKGVIVI 460

Zeta_toxin

pfam06414

Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is ...

202-255

5.79e-05

Zeta toxin; This family consists of several bacterial zeta toxin proteins. Zeta toxin is thought to be part of a postregulational killing system in bacteria. It relies on antitoxin/toxin systems that secure stable inheritance of low and medium copy number plasmids during cell division and kill cells that have lost the plasmid.

Pssm-ID: 428926 Cd Length: 192 Bit Score: 43.89 E-value: 5.79e-05

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 755511082  202 LKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDGHDLRTLNP 255
Cdd:pfam06414   1 LDDKTTSQERPKAILLGGQPGAGKTELARALLDELGRQGNVVRIDPDDFRELHP 54

PRK10636

putative ABC transporter ATP-binding protein; Provisional

201-366

6.34e-05

putative ABC transporter ATP-binding protein; Provisional

Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.16 E-value: 6.34e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 201 VLKDFTLKLPSGKIVALVGQSGGGKTTVASLLERFYDPEAGSVTLDghdlrtlnpswlRGQVIGFISQEPVLFattimen 280
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLA------------KGIKLGYFAQHQLEF------- 387

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 281 irfgkLDASDEEVYTAAR------EANAHEFISSFpdGYS-TVVGERGTTLSGGQKQRLAIARALIKQPTVLILDEATSA 353
Cdd:PRK10636 388 -----LRADESPLQHLARlapqelEQKLRDYLGGF--GFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNH 460

                        170
                 ....*....|...
gi 755511082 354 LDAESERVVQEAL 366
Cdd:PRK10636 461 LDLDMRQALTEAL 473

ABC_UvrA_I

cd03270

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...

322-405

1.02e-04

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.

Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 43.40 E-value: 1.02e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 322 TTLSGGQKQRLAIARALIKQPT--VLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRAAHSIIVMANGq 398
Cdd:cd03270  136 PTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRlRDLGNTVLVVEHDEDTIRAADHVIDIGPG- 214


                 ....*..
gi 755511082 399 vceAGTH 405
Cdd:cd03270  215 ---AGVH 218

ABC_Rad50

cd03240

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...

214-392

1.18e-04

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.

Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 42.98 E-value: 1.18e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 214 IVALVGQSGGGKTTVAsllerfydpEAGSVTLDGH-----DLRTLNPSWLR-GQVIGFISqepvlfattimenIRFgKLD 287
Cdd:cd03240   24 LTLIVGQNGAGKTTII---------EALKYALTGElppnsKGGAHDPKLIReGEVRAQVK-------------LAF-ENA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 288 ASDEevYTAAREANAHEFISSFPDGYST--VVGERGTtLSGGQKQ------RLAIARALIKQPTVLILDEATSALDAES- 358
Cdd:cd03240   81 NGKK--YTITRSLAILENVIFCHQGESNwpLLDMRGR-CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENi 157

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 755511082 359 ERVVQEALD--RASAGRTVLVIAHRLSTVRAAHSII 392
Cdd:cd03240  158 EESLAEIIEerKSQKNFQLIVITHDEELVDAADHIY 193

PRK11147

ABC transporter ATPase component; Reviewed

322-358

1.49e-04

ABC transporter ATPase component; Reviewed

Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 44.17 E-value: 1.49e-04

                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 755511082 322 TTLSGGQKQRLAIARALIKQPTVLILDEATSALDAES 358
Cdd:PRK11147 155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIET 191

uvra

TIGR00630

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...

322-411

1.73e-04

Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.23 E-value: 1.73e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  322 TTLSGGQKQRLAIARALIKQPT-VL-ILDEATSAL-DAESERVVQEALDRASAGRTVLVIAHRLSTVRAAHSIIVMA--- 395
Cdd:TIGR00630 487 GTLSGGEAQRIRLATQIGSGLTgVLyVLDEPSIGLhQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDIGpga 566

                          90
                  ....*....|....*....
gi 755511082  396 ---NGQVCEAGTHEELLKK 411
Cdd:TIGR00630 567 gehGGEVVASGTPEEILAN 585

PLN03073

ABC transporter F family; Provisional

323-398

1.87e-04

ABC transporter F family; Provisional

Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.08 E-value: 1.87e-04

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755511082 323 TLSGGQKQRLAIARALIKQPTVLILDEATSALDAESERVVQEALDRASagRTVLVIAHRLSTVRAAHSIIVMANGQ 398
Cdd:PLN03073 344 TFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP--KTFIVVSHAREFLNTVVTDILHLHGQ 417

ABC_Class2

cd03227

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...

209-393

2.27e-04

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: 41.58 E-value: 2.27e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 209 LPSGKIVALVGQSGGGKTTVasllerfydpeagsvtldghdLRTlnpswlrgqvIGFIsqepvlfatTIMENIRFGKLDA 288
Cdd:cd03227   18 FGEGSLTIITGPNGSGKSTI---------------------LDA----------IGLA---------LGGAQSATRRRSG 57

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 289 SDEEVYTAAREAnahEFISSFPdgystvvgergtTLSGGQKQRLAIARAL----IKQPTVLILDEATSALDAESERVVQE 364
Cdd:cd03227   58 VKAGCIVAAVSA---ELIFTRL------------QLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAE 122

                        170       180       190
                 ....*....|....*....|....*....|.
gi 755511082 365 AL-DRASAGRTVLVIAHRL-STVRAAHSIIV 393
Cdd:cd03227  123 AIlEHLVKGAQVIVITHLPeLAELADKLIHI 153

ABC_6TM_T1SS_like

cd18555

Six-transmembrane helical domain (6-TMD) of the ATP-binding cassette subunit in the type 1 ...

1-148

4.05e-04

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

Pssm-ID: 349999 [Multi-domain] Cd Length: 294 Bit Score: 42.11 E-value: 4.05e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   1 ML--SPRLTLMLAVVTpALMGVGTLMGSG-LRKLSRQCQEQIARATGVADEALGNVRTVRAFAME----KREEERYQAEL 73
Cdd:cd18555  136 MLyySPLLTLIVLLLG-LLIVLLLLLTRKkIKKLNQEEIVAQTKVQSYLTETLYGIETIKSLGSEkniyKKWENLFKKQL 214

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755511082  74 ESccckAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVV 148
Cdd:cd18555  215 KA----FKKKERLSNILNSISSSIQFIAPLLILWIGAYLVINGELTLGELIAFSSLAGSFLTPIVSLINSYNQFI 285

ABC_6TM_HMT1

cd18583

Six-transmembrane helical domain of the heavy metal tolerance protein; This group represents ...

1-151

6.16e-04

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: 41.36 E-value: 6.16e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   1 MLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELEScCCKA 80
Cdd:cd18583  134 LFDPYMGLIVAVVMVLYVWSTIKLTSWRTKLRRDMIDADREERSILTESLLNWETVKYFNREPYEKERYREAVKN-YQKA 212

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755511082  81 E-ELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGL 151
Cdd:cd18583  213 ErKYLFSLNLLNAVQSLILTLGLLAGCFLAAYQVSQGQATVGDFVTLLTYWAQLSGPLNFFATLYRSIQSDL 284

ABC_6TM_PrtD_like

cd18586

Six-transmembrane helical domain (6TM) domain of the ABC subunit (PrtD) in the T1SS ...

1-124

7.73e-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: 41.43 E-value: 7.73e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   1 MLSPRLTLMLAVVTPALMGVGTLMGSGLRKLSRQCQEQIARATGVADEALGNVRTVRAFAME----KREEERYQAELESc 76
Cdd:cd18586  135 LIHPPLGWVALVGAPVLVGLAWLNHRATRKPLGEANEAQAARDALAAETLRNAETIKALGMLgnlrRRWEARHAETLEL- 213

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 755511082  77 cckAEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDLM 124
Cdd:cd18586  214 ---QIRASDLAGAISAIGKTLRMALQSLILGVGAYLVIDGELTIGALI 258

PRK00635

excinuclease ABC subunit A; Provisional

317-397

1.31e-03

excinuclease ABC subunit A; Provisional

Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 1.31e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  317 VGERGTTLSGGQKQRLAIARALI---KQPTVLILDEATSALDAESERVVQEALDR-ASAGRTVLVIAHRLSTVRAAHSII 392
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTlVSLGHSVIYIDHDPALLKQADYLI 1772


                  ....*
gi 755511082  393 VMANG 397
Cdd:PRK00635 1773 EMGPG 1777

ABC_6TM_ATM1_ABCB7

cd18582

Six-transmembrane helical domain of the Atm1/ABC7 transporters; This group represents the Atm1 ...

10-123

4.29e-03

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: 39.02 E-value: 4.29e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  10 LAVVTPALMGVGTLMGSGLR-KLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELEscccKAEELG---- 84
Cdd:cd18582  144 ITLVTVALYVAFTIKVTEWRtKFRREMNEADNEANAKAVDSLLNYETVKYFNNEEYEAERYDKALA----KYEKAAvksq 219

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 755511082  85 RGIALFQGLSNIAFNCMVLGTLFIGGSLVAGQQLKGGDL 123
Cdd:cd18582  220 TSLALLNIGQALIISLGLTAIMLLAAQGVVAGTLTVGDF 258

YbjD

COG3593

Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...

202-303

7.32e-03

Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];

Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 38.44 E-value: 7.32e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082 202 LKDFTLKLPSGkIVALVGQSGGGKTTVASLLERFYDPEaGSVTLDGHDLRTLNPSWLRGQVIGFIsqepvlFATTIMENI 281
Cdd:COG3593   14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPS-SSRKFDEEDFYLGDDPDLPEIEIELT------FGSLLSRLL 85

                         90       100
                 ....*....|....*....|..
gi 755511082 282 RFGKLDASDEEVYTAAREANAH 303
Cdd:COG3593   86 RLLLKEEDKEELEEALEELNEE 107

ABC_6TM_exporter_like

cd18565

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

1-157

9.19e-03

Pssm-ID: 350009 [Multi-domain] Cd Length: 313 Bit Score: 37.93 E-value: 9.19e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082   1 MLSPRLTLMLAVVTPaLMGVGTLMGSG-LRKLSRQCQEQIARATGVADEALGNVRTVRAFAMEKREEERYQAELESCCCK 79
Cdd:cd18565  151 YLNWQLALVALLPVP-LIIAGTYWFQRrIEPRYRAVREAVGDLNARLENNLSGIAVIKAFTAEDFERERVADASEEYRDA 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511082  80 AEELGRGIALFQGLSNIAFNCMVLGTLFIGGSLV------AGQQLKGGDLMSFLVASQTVQRSMASLSVLFGQVVRGLSA 153
Cdd:cd18565  230 NWRAIRLRAAFFPVIRLVAGAGFVATFVVGGYWVldgpplFTGTLTVGTLVTFLFYTQRLLWPLTRLGDLIDQYQRAMAS 309


                 ....
gi 755511082 154 GARV 157
Cdd:cd18565  310 AKRV 313

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