|
Name |
Accession |
Description |
Interval |
E-value |
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
32-215 |
1.61e-47 |
|
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: 152.99 E-value: 1.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQI---EG-IDCSPKVQMAYYRQLayedmrdvs 107
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELepdEGiVTWGSTVKIGYFEQL--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 108 llqylmdetdssesfsrailnnlglnealdrscnvlSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTLEALEMFMNK 187
Cdd:cd03221 72 ------------------------------------SGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKE 115
|
170 180
....*....|....*....|....*...
gi 585044696 188 YPGIILFTSHDTRFVKHVSDKKWELTGQ 215
Cdd:cd03221 116 YPGTVILVSHDRYFLDQVATKIIELEDG 143
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-219 |
1.61e-47 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 163.31 E-value: 1.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 1 MEHLEEVEKPQSYH--EFNFPQ-----NKIydihnnypIIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTL 73
Cdd:COG0488 286 LEKLEREEPPRRDKtvEIRFPPperlgKKV--------LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 74 LEAIYHQIE---G-IDCSPKVQMAYYRQLaYEDMR-DVSLLQYLMDETDS-SESFSRAILNNLGL-NEALDRSCNVLSGG 146
Cdd:COG0488 358 LKLLAGELEpdsGtVKLGETVKIGYFDQH-QEELDpDKTVLDELRDGAPGgTEQEVRGYLGRFLFsGDDAFKPVGVLSGG 436
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 585044696 147 ERTKLSLAVLFSTKANMLILDEPTNFLDIKTLEALEMFMNKYPGIILFTSHDTRFVKHVSDKKWELTGQSLHD 219
Cdd:COG0488 437 EKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
34-218 |
7.18e-39 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 140.20 E-value: 7.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 34 AQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQIE---G-IDCSPKVQMAYYRQ------------ 97
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEpdsGeVSIPKGLRIGYLPQeppldddltvld 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 98 ------------------------LAYEDMRDVSLLQYLMDETD--SSESFSRAILNNLGLNEA-LDRSCNVLSGGERTK 150
Cdd:COG0488 81 tvldgdaelraleaeleeleaklaEPDEDLERLAELQEEFEALGgwEAEARAEEILSGLGFPEEdLDRPVSELSGGWRRR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 585044696 151 LSLA-VLFStKANMLILDEPTNFLDIKTLEALEMFMNKYPGIILFTSHDTRFVKHVSDKKWELTGQSLH 218
Cdd:COG0488 161 VALArALLS-EPDLLLLDEPTNHLDLESIEWLEEFLKNYPGTVLVVSHDRYFLDRVATRILELDRGKLT 228
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-219 |
1.01e-28 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 112.29 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 4 LEEVeKPQS--YHEFNFPQNKiyDIHNNyPIIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQI 81
Cdd:PRK15064 294 LEEV-KPSSrqNPFIRFEQDK--KLHRN-ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGEL 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 82 E----GIDCSPKVQMAYYRQLAYEDM-RDVSLL----QYLMDETDssESFSRAILNNLGL-NEALDRSCNVLSGGERTKL 151
Cdd:PRK15064 370 EpdsgTVKWSENANIGYYAQDHAYDFeNDLTLFdwmsQWRQEGDD--EQAVRGTLGRLLFsQDDIKKSVKVLSGGEKGRM 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 585044696 152 SLAVLFSTKANMLILDEPTNFLDIKTLEALEMFMNKYPGIILFTSHDTRFVKHVSDKKWELTGQSLHD 219
Cdd:PRK15064 448 LFGKLMMQKPNVLVMDEPTNHMDMESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVVD 515
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
47-171 |
7.66e-28 |
|
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: 103.11 E-value: 7.66e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 47 LTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQ---------IEGIDC------SPKVQMAYYRQL--------AYEDM 103
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLlsptegtilLDGQDLtdderkSLRKEIGYVFQDpqlfprltVRENL 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 585044696 104 RDVSLLQYLMDETDSSESfsRAILNNLGLNEALDRSCNV----LSGGERTKLSLAVLFSTKANMLILDEPTN 171
Cdd:pfam00005 81 RLGLLLKGLSKREKDARA--EEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
32-208 |
1.60e-26 |
|
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: 102.24 E-value: 1.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYH---------QIEGIDCSPKVQMA--------- 93
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGllkpdsgsiLIDGEDVRKEPREArrqigvlpd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 94 ----YYRQLAYEDMRDVSLLqYLMDETDSSESFSRaILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEP 169
Cdd:COG4555 82 erglYDRLTVRENIRYFAEL-YGLFDEELKKRIEE-LIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 585044696 170 TNFLDIKTLEALEMFMNKY---PGIILFTSHDTRFVKHVSDK 208
Cdd:COG4555 160 TNGLDVMARRLLREILRALkkeGKTVLFSSHIMQEVEALCDR 201
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
32-205 |
6.49e-26 |
|
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: 99.48 E-value: 6.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEA-----------IYHQIEGIDCSPKvqmAYYRQLAY 100
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRIlagllppsageVLWNGEPIRDARE---DYRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 101 --------EDMrdvSLLQYL-----MDETDSSESFSRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILD 167
Cdd:COG4133 80 lghadglkPEL---TVRENLrfwaaLYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 585044696 168 EPTNFLDIKTLEALEMFMNKYP---GIILFTSHDTRFVKHV 205
Cdd:COG4133 157 EPFTALDAAGVALLAELIAAHLargGAVLLTTHQPLELAAA 197
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
34-214 |
7.35e-26 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 104.65 E-value: 7.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 34 AQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQIEG----IDCSPKVQMAYYRQ------------ 97
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQAdsgrIHCGTKLEVAYFDQhraeldpektvm 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 98 --LA---YEDM---RDVSLLQYLMDETdssesFS--RAIlnnlglnealdRSCNVLSGGERTKLSLAVLFSTKANMLILD 167
Cdd:PRK11147 402 dnLAegkQEVMvngRPRHVLGYLQDFL-----FHpkRAM-----------TPVKALSGGERNRLLLARLFLKPSNLLILD 465
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 585044696 168 EPTNFLDIKTLEALEMFMNKYPGIILFTSHDTRFVKHVSDKKWELTG 214
Cdd:PRK11147 466 EPTNDLDVETLELLEELLDSYQGTVLLVSHDRQFVDNTVTECWIFEG 512
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
34-208 |
9.23e-24 |
|
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: 93.27 E-value: 9.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 34 AQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYH---------QIEGIDCS--PKVQMAyyRQLAYed 102
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGllkpssgeiLLDGKDLAslSPKELA--RKIAY-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 103 mrdvsLLQylmdetdssesfsraILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIK----TL 178
Cdd:cd03214 78 -----VPQ---------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAhqieLL 137
|
170 180 190
....*....|....*....|....*....|
gi 585044696 179 EALEMFMNKYPGIILFTSHDTRFVKHVSDK 208
Cdd:cd03214 138 ELLRRLARERGKTVVMVLHDLNLAARYADR 167
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
32-198 |
5.90e-23 |
|
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: 92.80 E-value: 5.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQ---------IEGID---CSPKvQMAyyRQLA 99
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLlkpssgevlLDGRDlasLSRR-ELA--RRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 100 Y--------EDM--RD-VSL-----LQYLMDETDSSESFSRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANM 163
Cdd:COG1120 79 YvpqeppapFGLtvRElVALgryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 585044696 164 LILDEPTNFLDIK-TLEALEMF--MNKYPGI-ILFTSHD 198
Cdd:COG1120 159 LLLDEPTSHLDLAhQLEVLELLrrLARERGRtVVMVLHD 197
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
32-201 |
4.64e-22 |
|
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: 93.46 E-value: 4.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQIE----GIDCSPKVQMAYYRQlayedMRDV- 106
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQpdsgTIEIGETVKLAYVDQ-----SRDAl 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 107 ----SLLQYLMDETD-----SSESFSRAILNNLGLNEAlD--RSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDI 175
Cdd:TIGR03719 398 dpnkTVWEEISGGLDiiklgKREIPSRAYVGRFNFKGS-DqqKKVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV 476
|
170 180
....*....|....*....|....*.
gi 585044696 176 KTLEALEMFMNKYPGIILFTSHDTRF 201
Cdd:TIGR03719 477 ETLRALEEALLNFAGCAVVISHDRWF 502
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
34-212 |
8.88e-21 |
|
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: 84.99 E-value: 8.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 34 AQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYhqieGIDCSPKVQMAYyrqlayedmrdvsllqylm 113
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIA----GLLKPTSGEILI------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 114 DETDSSESFSRAILNNLGLnealdrscnV--LSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTLEALEMFMNKYPG- 190
Cdd:cd00267 59 DGKDIAKLPLEELRRRIGY---------VpqLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEe 129
|
170 180
....*....|....*....|....
gi 585044696 191 --IILFTSHDTRFVKHVSDKKWEL 212
Cdd:cd00267 130 grTVIIVTHDPELAELAADRVIVL 153
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
41-208 |
7.48e-20 |
|
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: 83.67 E-value: 7.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 41 KGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI--YHQ-------IEGIDCSPKVQMAYYRQLAY-----EDM--- 103
Cdd:cd03225 11 DGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLngLLGptsgevlVDGKDLTKLSLKELRRKVGLvfqnpDDQffg 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 104 ----RDV--SLLQYLMDETDSSESFSRAiLNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKT 177
Cdd:cd03225 91 ptveEEVafGLENLGLPEEEIEERVEEA-LELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAG 169
|
170 180 190
....*....|....*....|....*....|....
gi 585044696 178 LEALEMFMNKYP--GI-ILFTSHDTRFVKHVSDK 208
Cdd:cd03225 170 RRELLELLKKLKaeGKtIIIVTHDLDLLLELADR 203
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
32-208 |
4.26e-19 |
|
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: 80.90 E-value: 4.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI--YHQ-------IEGIDCSPKvQMAYYRQLAYed 102
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIIlgLLKpdsgeikVLGKDIKKE-PEEVKRRIGY-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 103 mrdvsllqyLMDETdssesfsrAILNNLGLNEALDrscnvLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTLEALE 182
Cdd:cd03230 78 ---------LPEEP--------SLYENLTVRENLK-----LSGGMKQRLALAQALLHDPELLILDEPTSGLDPESRREFW 135
|
170 180
....*....|....*....|....*....
gi 585044696 183 MFMNKY---PGIILFTSHDTRFVKHVSDK 208
Cdd:cd03230 136 ELLRELkkeGKTILLSSHILEEAERLCDR 164
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
32-208 |
1.53e-18 |
|
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: 80.45 E-value: 1.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLV-KGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI----YHQ-----IEGIDCSPKVQMAYYRQLAY- 100
Cdd:COG1122 1 IELENLSFSyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLngllKPTsgevlVDGKDITKKNLRELRRKVGLv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 101 ----EDM-------RDV--SLLQYLMDETDSSEsfsRA--ILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLI 165
Cdd:COG1122 81 fqnpDDQlfaptveEDVafGPENLGLPREEIRE---RVeeALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 585044696 166 LDEPTNFLDIKTLEALEMFMNKYP--GI-ILFTSHDTRFVKHVSDK 208
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLNkeGKtVIIVTHDLDLVAELADR 203
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
32-221 |
1.77e-18 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 83.30 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQIE----GIDCSPKVQMAY------------- 94
Cdd:PRK10636 2 IVFSSLQIRRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISadggSYTFPGNWQLAWvnqetpalpqpal 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 95 ---------YRQLAYE--------DMRDVSLLQYLMDETDSSESFSRA--ILNNLGL-NEALDRSCNVLSGGERTKLSLA 154
Cdd:PRK10636 82 eyvidgdreYRQLEAQlhdanernDGHAIATIHGKLDAIDAWTIRSRAasLLHGLGFsNEQLERPVSDFSGGWRMRLNLA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 585044696 155 VLFSTKANMLILDEPTNFLDIKTLEALEMFMNKYPGIILFTSHDTRFVKHVSDKKWELTGQSLHDIT 221
Cdd:PRK10636 162 QALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFEYT 228
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
1-210 |
2.27e-18 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 82.99 E-value: 2.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 1 MEHLEEV-EKPQSYHEFNFPQNK-------IYDIHNNYPiiaqnltlvkGSQKLLTQVRFQIPYGKNIALVGANGVGKTT 72
Cdd:PLN03073 481 LGHVDAVvNDPDYKFEFPTPDDRpgppiisFSDASFGYP----------GGPLLFKNLNFGIDLDSRIAMVGPNGIGKST 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 73 LLEAIYHQIEGIDC----SPKVQMAYYRQlAYEDMRDVSL--LQYLMD-ETDSSESFSRAILNNLGL--NEALdRSCNVL 143
Cdd:PLN03073 551 ILKLISGELQPSSGtvfrSAKVRMAVFSQ-HHVDGLDLSSnpLLYMMRcFPGVPEQKLRAHLGSFGVtgNLAL-QPMYTL 628
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 585044696 144 SGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTLEALEMFMNKYPGIILFTSHDTRFVKHVSDKKW 210
Cdd:PLN03073 629 SGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQGGVLMVSHDEHLISGSVDELW 695
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
32-198 |
6.25e-18 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 81.70 E-value: 6.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQIE---G-IDCSPKVQMAYYRQlayedMRDV- 106
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQpdsGtIKIGETVKLAYVDQ-----SRDAl 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 107 ----SLLQYLMDETD-----SSESFSRAILNNLGLNEAlD--RSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDI 175
Cdd:PRK11819 400 dpnkTVWEEISGGLDiikvgNREIPSRAYVGRFNFKGG-DqqKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
|
170 180
....*....|....*....|...
gi 585044696 176 KTLEALEMFMNKYPGIILFTSHD 198
Cdd:PRK11819 479 ETLRALEEALLEFPGCAVVISHD 501
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
31-212 |
1.00e-17 |
|
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: 81.18 E-value: 1.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 31 PIIAQNLTLV-KGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQIE---------GIDCSPKVQMAYYRQLAY 100
Cdd:TIGR02857 321 SLEFSGVSVAyPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDptegsiavnGVPLADADADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 101 edmrdVSLLQYLM---------------DETDSSESFSRAILNNL------GLNEALDRSCNVLSGGERTKLSLAVLFST 159
Cdd:TIGR02857 401 -----VPQHPFLFagtiaenirlarpdaSDAEIREALERAGLDEFvaalpqGLDTPIGEGGAGLSGGQAQRLALARAFLR 475
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 585044696 160 KANMLILDEPTNFLDIKT----LEALEMFMNKYpgIILFTSHDtRFVKHVSDKKWEL 212
Cdd:TIGR02857 476 DAPLLLLDEPTAHLDAETeaevLEALRALAQGR--TVLLVTHR-LALAALADRIVVL 529
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
32-198 |
1.79e-17 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 77.80 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYH---------QIEGIDCsPKVQMAYYRQLAY-- 100
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGllrptsgevRVLGEDV-ARDPAEVRRRIGYvp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 101 ED---MRDVSLLQYL-----MDETDSSESFSRA--ILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPT 170
Cdd:COG1131 80 QEpalYPDLTVRENLrffarLYGLPRKEARERIdeLLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190
....*....|....*....|....*....|.
gi 585044696 171 NFLDIKTLEAL-EMF--MNKYPGIILFTSHD 198
Cdd:COG1131 160 SGLDPEARRELwELLreLAAEGKTVLLSTHY 190
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
41-207 |
6.63e-17 |
|
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: 75.76 E-value: 6.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 41 KGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI------YH---QIEGIDCSPK--VQMAYY------RQLAYEDM 103
Cdd:cd03226 10 KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILaglikeSSgsiLLNGKPIKAKerRKSIGYvmqdvdYQLFTDSV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 104 RDVslLQYLMDETDSSESFSRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTLEALEM 183
Cdd:cd03226 90 REE--LLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGE 167
|
170 180
....*....|....*....|....*..
gi 585044696 184 FMNKYPG---IILFTSHDTRFVKHVSD 207
Cdd:cd03226 168 LIRELAAqgkAVIVITHDYEFLAKVCD 194
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
34-197 |
1.39e-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: 74.70 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 34 AQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIY--------HQIEGIDCSPKVQMAYYRQLAYEDMRD 105
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAgllrpdsgEVRWNGTPLAEQRDEPHENILYLGHLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 106 -----VSLLQYLMDETDSSESFSRAILNNL---GLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKT 177
Cdd:TIGR01189 83 glkpeLSALENLHFWAAIHGGAQRTIEDALaavGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
170 180
....*....|....*....|...
gi 585044696 178 LEALEMFMNKY---PGIILFTSH 197
Cdd:TIGR01189 163 VALLAGLLRAHlarGGIVLLTTH 185
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
34-205 |
4.76e-16 |
|
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: 73.72 E-value: 4.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 34 AQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQI---EG-IDCSPKVQMAYYRQLAY----EDM-- 103
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLkptSGsIRVFGKPLEKERKRIGYvpqrRSIdr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 104 ------RDVSLL----QYLMDETDSSESFSRAI--LNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTN 171
Cdd:cd03235 82 dfpisvRDVVLMglygHKGLFRRLSKADKAKVDeaLERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 585044696 172 FLDIKTLEAL-EMF--MNKYPGIILFTSHD----TRFVKHV 205
Cdd:cd03235 162 GVDPKTQEDIyELLreLRREGMTILVVTHDlglvLEYFDRV 202
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
28-205 |
1.31e-15 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 72.81 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 28 NNYPIIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQI---EG-IDCSPKVQMAYYRQLAY--- 100
Cdd:COG1121 3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLpptSGtVRLFGKPPRRARRRIGYvpq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 101 ------------EDM------RDVSLLQYLmdetdSSESFSRA--ILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTK 160
Cdd:COG1121 83 raevdwdfpitvRDVvlmgryGRRGLFRRP-----SRADREAVdeALERVGLEDLADRPIGELSGGQQQRVLLARALAQD 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 585044696 161 ANMLILDEPTNFLDIKTLEAL-EMF--MNKYPGIILFTSHD----TRFVKHV 205
Cdd:COG1121 158 PDLLLLDEPFAGVDAATEEALyELLreLRREGKTILVVTHDlgavREYFDRV 209
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
32-176 |
1.50e-15 |
|
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: 72.23 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLVKGSQKLLTQVRFQIPYGKnIALVGANGVGKTTLLEAIYH-------QIE--GIDCsPKVQMAYYRQLAY-- 100
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGM-YGLLGPNGAGKTTLMRILATltppssgTIRidGQDV-LKQPQKLRRRIGYlp 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 101 ------EDMRDVSLLQYL--MDETDSSESFSRA--ILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPT 170
Cdd:cd03264 79 qefgvyPNFTVREFLDYIawLKGIPSKEVKARVdeVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPT 158
|
....*.
gi 585044696 171 NFLDIK 176
Cdd:cd03264 159 AGLDPE 164
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
40-205 |
1.75e-15 |
|
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: 74.59 E-value: 1.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 40 VKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIyhqiEGID--------CSPKVQMAYYRQLAYED--------- 102
Cdd:TIGR03719 14 VPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM----AGVDkdfngearPQPGIKVGYLPQEPQLDptktvrenv 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 103 MRDVSLLQYLMDETDS-SESFS----------------RAILNNLGLNE----------AL-----DRSCNVLSGGERTK 150
Cdd:TIGR03719 90 EEGVAEIKDALDRFNEiSAKYAepdadfdklaaeqaelQEIIDAADAWDldsqleiamdALrcppwDADVTKLSGGERRR 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 585044696 151 LSLAVLFSTKANMLILDEPTNFLDIKTLEALEMFMNKYPGIILFTSHDTRFVKHV 205
Cdd:TIGR03719 170 VALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPGTVVAVTHDRYFLDNV 224
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
32-212 |
4.42e-15 |
|
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: 73.25 E-value: 4.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLV-KGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI------YH---QIEGIDCSPKVQMAYYRQLAY- 100
Cdd:COG4988 337 IELEDVSFSyPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLlgflppYSgsiLINGVDLSDLDPASWRRQIAWv 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 101 ------------------------EDMRDVSLLQYLMDETDSsesfsraiLNNlGLNEAL-DRSCNvLSGGERTKLSLAV 155
Cdd:COG4988 417 pqnpylfagtirenlrlgrpdasdEELEAALEAAGLDEFVAA--------LPD-GLDTPLgEGGRG-LSGGQAQRLALAR 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 585044696 156 LFSTKANMLILDEPTNFLDIKT----LEALEMFMNKYpgIILFTSHDTRFVKHvSDKKWEL 212
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETeaeiLQALRRLAKGR--TVILITHRLALLAQ-ADRILVL 544
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
42-197 |
6.25e-15 |
|
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: 69.72 E-value: 6.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 42 GSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYH---------QIEGIDCSpKVQMAYYR-QLAYedmrdvsLLQ- 110
Cdd:cd03228 13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRlydptsgeiLIDGVDLR-DLDLESLRkNIAY-------VPQd 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 111 -YLMDETdssesfsraILNNLglnealdrscnvLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKT----LEALEMFM 185
Cdd:cd03228 85 pFLFSGT---------IRENI------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETealiLEALRALA 143
|
170
....*....|..
gi 585044696 186 NKYpgIILFTSH 197
Cdd:cd03228 144 KGK--TVIVIAH 153
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
14-218 |
1.12e-14 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 72.20 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 14 HEFNFPQNKIYDIHnnypiiAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI-YHQIEGIdcsPK-VQ 91
Cdd:PLN03073 166 HDGNGGGPAIKDIH------MENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMaMHAIDGI---PKnCQ 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 92 MAYYRQLAYEDmrDVSLLQYLMD--------------------------------------------------------- 114
Cdd:PLN03073 237 ILHVEQEVVGD--DTTALQCVLNtdiertqlleeeaqlvaqqrelefetetgkgkgankdgvdkdavsqrleeiykrlel 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 115 -ETDSSESFSRAILNNLGLN-EALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTLEALEMFMNKYPGII 192
Cdd:PLN03073 315 iDAYTAEARAASILAGLSFTpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPKTF 394
|
250 260
....*....|....*....|....*.
gi 585044696 193 LFTSHDTRFVKHVSDKKWELTGQSLH 218
Cdd:PLN03073 395 IVVSHAREFLNTVVTDILHLHGQKLV 420
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
35-208 |
3.89e-14 |
|
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: 68.40 E-value: 3.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 35 QNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI---YHQIEGI----DCSPKVQMAYYRQLA-------- 99
Cdd:cd03268 4 NDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIIlglIKPDSGEitfdGKSYQKNIEALRRIGalieapgf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 100 YEDMRDVSLLQYLMDETDSSESFSRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLD---IK 176
Cdd:cd03268 84 YPNLTARENLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDpdgIK 163
|
170 180 190
....*....|....*....|....*....|..
gi 585044696 177 TLEALEMFMNKYPGIILFTSHDTRFVKHVSDK 208
Cdd:cd03268 164 ELRELILSLRDQGITVLISSHLLSEIQKVADR 195
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
46-203 |
4.34e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.36 E-value: 4.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 46 LLTQVRFQIPYGKNIALVGANGVGKTTLL------------EAIYHQ-----------------------IEGIDCSPKV 90
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMkilngevllddgRIIYEQdlivarlqqdpprnvegtvydfvAEGIEEQAEY 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 91 QMAYYR--QLAYEDMRDVSL--LQYLMDETDSS-----ESFSRAILNNLGLNEalDRSCNVLSGGERTKLSLAVLFSTKA 161
Cdd:PRK11147 98 LKRYHDisHLVETDPSEKNLneLAKLQEQLDHHnlwqlENRINEVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSNP 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 585044696 162 NMLILDEPTNFLDIKTLEALEMFMNKYPGIILFTSHDTRFVK 203
Cdd:PRK11147 176 DVLLLDEPTNHLDIETIEWLEGFLKTFQGSIIFISHDRSFIR 217
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
42-207 |
5.10e-14 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 70.20 E-value: 5.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 42 GSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQIEG----IDCSPKVQMAYYRQLAYEDMR-DVSLLQYLMDET 116
Cdd:PRK10636 323 GDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPvsgeIGLAKGIKLGYFAQHQLEFLRaDESPLQHLARLA 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 117 DS-SESFSRAILNNLGLN-EALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTLEALEMFMNKYPGIILF 194
Cdd:PRK10636 403 PQeLEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGALVV 482
|
170
....*....|...
gi 585044696 195 TSHDTRFVKHVSD 207
Cdd:PRK10636 483 VSHDRHLLRSTTD 495
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
31-175 |
6.80e-14 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 68.50 E-value: 6.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 31 PIIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQIEGIDCSPKVQ---MAYY--RQLAyedmRD 105
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGdkpISMLssRQLA----RR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 106 VSLL--QYLMDE-----------------------TDSSESFSRAiLNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTK 160
Cdd:PRK11231 78 LALLpqHHLTPEgitvrelvaygrspwlslwgrlsAEDNARVNQA-MEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQD 156
|
170
....*....|....*
gi 585044696 161 ANMLILDEPTNFLDI 175
Cdd:PRK11231 157 TPVVLLDEPTTYLDI 171
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
44-177 |
8.83e-14 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 67.68 E-value: 8.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 44 QKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQIEGIDCSPKVQMayyrqLAYEDMRDVSLLQYLMDETDSSESFs 123
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDV-----PDNQFGREASLIDAIGRKGDFKDAV- 116
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 585044696 124 rAILNNLGLNEA--LDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKT 177
Cdd:COG2401 117 -ELLNAVGLSDAvlWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
43-205 |
9.50e-14 |
|
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: 66.57 E-value: 9.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 43 SQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEaiyhQIEGiDCSP---KVQMAYYRQLAYED-MRD-VSLLQ---YLMD 114
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQ----LLTG-DLKPqqgEITLDGVPVSDLEKaLSSlISVLNqrpYLFD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 115 ETdssesfsraILNNLGLNealdrscnvLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKT-LEALEMFMNKYPG-II 192
Cdd:cd03247 89 TT---------LRNNLGRR---------FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITeRQLLSLIFEVLKDkTL 150
|
170
....*....|...
gi 585044696 193 LFTSHDTRFVKHV 205
Cdd:cd03247 151 IWITHHLTGIEHM 163
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
60-208 |
1.16e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 69.07 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 60 IALVGANGVGKTT---LLEAIYHQIEGiDCSPKVQMAYYRQlaY-EDMRDVSLLQYLMDETDS-SESFSRA-ILNNLGLN 133
Cdd:PRK13409 368 IGIVGPNGIGKTTfakLLAGVLKPDEG-EVDPELKISYKPQ--YiKPDYDGTVEDLLRSITDDlGSSYYKSeIIKPLQLE 444
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 585044696 134 EALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLD----IKTLEALEMFMNKYPGIILFTSHDTRFVKHVSDK 208
Cdd:PRK13409 445 RLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrLAVAKAIRRIAEEREATALVVDHDIYMIDYISDR 523
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-181 |
2.09e-13 |
|
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: 68.54 E-value: 2.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 19 PQNKIYDIHNNYPiiaqnltlvkGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQIE---------GIDCSPK 89
Cdd:TIGR02868 333 PTLELRDLSAGYP----------GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDplqgevtldGVPVSSL 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 90 VQMAYYRQLAY--ED--MRDVSLLQYLM----DETDS--SESFSRAILNNL------GLNEALDRSCNVLSGGERTKLSL 153
Cdd:TIGR02868 403 DQDEVRRRVSVcaQDahLFDTTVRENLRlarpDATDEelWAALERVGLADWlralpdGLDTVLGEGGARLSGGERQRLAL 482
|
170 180
....*....|....*....|....*...
gi 585044696 154 AVLFSTKANMLILDEPTNFLDIKTLEAL 181
Cdd:TIGR02868 483 ARALLADAPILLLDEPTEHLDAETADEL 510
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
31-179 |
3.12e-13 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 67.56 E-value: 3.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 31 PIIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQI---------EGIDCSPKVQMAYYRQ---- 97
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLtptagtvlvAGDDVEALSARAASRRvasv 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 98 -----LAYE-DMRDVSLLQY--------LMDETDSSeSFSRAIlNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANM 163
Cdd:PRK09536 83 pqdtsLSFEfDVRQVVEMGRtphrsrfdTWTETDRA-AVERAM-ERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
|
170 180
....*....|....*....|
gi 585044696 164 LILDEPTNFLDI----KTLE 179
Cdd:PRK09536 161 LLLDEPTASLDInhqvRTLE 180
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-216 |
3.93e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.52 E-value: 3.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 1 MEHLEEVEKPQSyhefnfPQNKIYDIHNNYpIIAQNLTLVKGS-QKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI-- 77
Cdd:COG4178 339 EEALEAADALPE------AASRIETSEDGA-LALEDLTLRTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIag 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 78 ---YhqIEG-IDCSPKVQMAYYRQLAY---EDMRDVslLQYLMDETDSSESFSRAILN--NLG-LNEALDRSCN---VLS 144
Cdd:COG4178 412 lwpY--GSGrIARPAGARVLFLPQRPYlplGTLREA--LLYPATAEAFSDAELREALEavGLGhLAERLDEEADwdqVLS 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 585044696 145 GGERTKLSLAVLFSTKANMLILDEPTNFLDIKTLEAL-EMFMNKYPGI-ILFTSHDTRFVKHvSDKKWELTGQS 216
Cdd:COG4178 488 LGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALyQLLREELPGTtVISVGHRSTLAAF-HDRVLELTGDG 560
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
32-197 |
1.12e-12 |
|
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: 64.44 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIyhqiEGIdcSPK--------------VQMAYYRQ 97
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRIL----AGL--SPPlagrvllnggpldfQRDSIARG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 98 LAYEDMRD--------VSLLQYLMDETDSSESFSraILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEP 169
Cdd:cd03231 75 LLYLGHAPgikttlsvLENLRFWHADHSDEQVEE--ALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEP 152
|
170 180 190
....*....|....*....|....*....|.
gi 585044696 170 TNFLDIKTLEALEMFMNKYP---GIILFTSH 197
Cdd:cd03231 153 TTALDKAGVARFAEAMAGHCargGMVVLTTH 183
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
32-204 |
1.41e-12 |
|
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: 64.05 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLVKGSQKL----LTQVRFQIPYGKNIALVGANGVGKTTLLEAIYH---------QIEGIDCS--PKVQMAYYR 96
Cdd:cd03255 1 IELKNLSKTYGGGGEkvqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGldrptsgevRVDGTDISklSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 97 QlayedmRDVS-------LLQYL-----------MDETDSSESFSRA--ILNNLGLNEALDRSCNVLSGGERTKLSLAVL 156
Cdd:cd03255 81 R------RHIGfvfqsfnLLPDLtalenvelpllLAGVPKKERRERAeeLLERVGLGDRLNHYPSELSGGQQQRVAIARA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 585044696 157 FSTKANMLILDEPTNFLDIKT-LEALEMF--MNKYPGI-ILFTSHDTRFVKH 204
Cdd:cd03255 155 LANDPKIILADEPTGNLDSETgKEVMELLreLNKEAGTtIVVVTHDPELAEY 206
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
137-205 |
1.98e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.53 E-value: 1.98e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 585044696 137 DRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTLEALEMFMNKYPGIILFTSHDTRFVKHV 205
Cdd:PRK11819 158 DAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPGTVVAVTHDRYFLDNV 226
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
31-197 |
2.39e-12 |
|
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: 63.95 E-value: 2.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 31 PIIA-QNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI---YHQIEGIDC-------------------- 86
Cdd:COG1119 2 PLLElRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLItgdLPPTYGNDVrlfgerrggedvwelrkrig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 87 --SPKVQMAYYRQLAYEDM------------RDVsllqylmdeTDSSESFSRAILNNLGLNEALDRSCNVLSGGERTKLS 152
Cdd:COG1119 82 lvSPALQLRFPRDETVLDVvlsgffdsiglyREP---------TDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 585044696 153 LAVLFSTKANMLILDEPTNFLDIKTLEALEMFMNKY-----PGIILFTSH 197
Cdd:COG1119 153 IARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaegaPTLVLVTHH 202
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
42-181 |
2.61e-12 |
|
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: 65.17 E-value: 2.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 42 GSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI-----YHQ----IEGIDcspkvqmayYRQLAYEDMRD-VSLLQ- 110
Cdd:COG4987 346 AGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLlrfldPQSgsitLGGVD---------LRDLDEDDLRRrIAVVPq 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 111 --YLMDET----------DSSESFSRAILNNLGLNEALDR-----SCNV------LSGGERTKLSLAVLFSTKANMLILD 167
Cdd:COG4987 417 rpHLFDTTlrenlrlarpDATDEELWAALERVGLGDWLAAlpdglDTWLgeggrrLSGGERRRLALARALLRDAPILLLD 496
|
170
....*....|....
gi 585044696 168 EPTNFLDIKTLEAL 181
Cdd:COG4987 497 EPTEGLDAATEQAL 510
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
60-208 |
2.66e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 63.97 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 60 IALVGANGVGKTT---LLEAIYHQIEGIDCSPKVQMAYYRQLAYEDMrDVSLLQYLMDETDSSES---FSRAILNNLGLN 133
Cdd:cd03237 28 IGILGPNGIGKTTfikMLAGVLKPDEGDIEIELDTVSYKPQYIKADY-EGTVRDLLSSITKDFYThpyFKTEIAKPLQIE 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 585044696 134 EALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLD----IKTLEALEMFMNKYPGIILFTSHDTRFVKHVSDK 208
Cdd:cd03237 107 QILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDveqrLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADR 185
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
36-197 |
3.19e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.05 E-value: 3.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 36 NLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLE-----------AIYHQIEGIDcspKVQMAYYRQLAYEDMR 104
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKliagllnpekgEILFERQSIK---KDLCTYQKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 105 -----DVSLLQY-LMDETDSSESFSRAILNNL-GLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKT 177
Cdd:PRK13540 83 sginpYLTLRENcLYDIHFSPGAVGITELCRLfSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
170 180
....*....|....*....|...
gi 585044696 178 LEALEMFMN---KYPGIILFTSH 197
Cdd:PRK13540 163 LLTIITKIQehrAKGGAVLLTSH 185
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
42-205 |
3.27e-12 |
|
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: 64.86 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 42 GSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI---YH------QIEGIDcspkvqmayYRQLAYEDMRdvSLLQYL 112
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLlglYEptsgriLIDGID---------LRQIDPASLR--RQIGVV 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 113 MDETdssESFSRAILNNLGLN----------EALDRSC--------------------NVLSGGERTKLSLAVLFSTKAN 162
Cdd:COG2274 555 LQDV---FLFSGTIRENITLGdpdatdeeiiEAARLAGlhdfiealpmgydtvvgeggSNLSGGQRQRLAIARALLRNPR 631
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 585044696 163 MLILDEPTNFLDIKT----LEAL-EMFMNKypgIILFTSHDTRFVKHV 205
Cdd:COG2274 632 ILILDEATSALDAETeaiiLENLrRLLKGR---TVIIIAHRLSTIRLA 676
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
41-181 |
9.07e-12 |
|
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: 61.41 E-value: 9.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 41 KGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI-----YHQIEG---IDCSPKVQMAYYRQLAYEDMRDVsllqyl 112
Cdd:cd03213 19 KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagrrtGLGVSGevlINGRPLDKRSFRKIIGYVPQDDI------ 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 585044696 113 mdetdssesfsraILNNLGLNEALDRS--CNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLD-------IKTLEAL 181
Cdd:cd03213 93 -------------LHPTLTVRETLMFAakLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDsssalqvMSLLRRL 157
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
34-207 |
1.25e-11 |
|
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: 61.53 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 34 AQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI---------YHQIEG--IDCSPKVQMAYY---RQLa 99
Cdd:cd03269 3 VENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMIlgiilpdsgEVLFDGkpLDIAARNRIGYLpeeRGL- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 100 YEDMRDVSLLQYL-----MDETDSSESfSRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLD 174
Cdd:cd03269 82 YPKMKVIDQLVYLaqlkgLKKEEARRR-IDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLD 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 585044696 175 IKTLEALEMFMNKYPG---IILFTSHDTRFVKHVSD 207
Cdd:cd03269 161 PVNVELLKDVIRELARagkTVILSTHQMELVEELCD 196
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
34-197 |
1.57e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 60.97 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 34 AQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLL------------------EAIYHQIEgidcspkvqmAYY 95
Cdd:PRK13538 4 ARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLrilaglarpdagevlwqgEPIRRQRD----------EYH 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 96 RQLAY--------------EDMRdvsLLQYLMDETDSSESFsrAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKA 161
Cdd:PRK13538 74 QDLLYlghqpgikteltalENLR---FYQRLHGPGDDEALW--EALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRA 148
|
170 180 190
....*....|....*....|....*....|....*....
gi 585044696 162 NMLILDEPTNFLDIKTLEALEMFMNKYP---GIILFTSH 197
Cdd:PRK13538 149 PLWILDEPFTAIDKQGVARLEALLAQHAeqgGMVILTTH 187
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
60-175 |
2.02e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 62.49 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 60 IALVGANGVGKTT---LLEAIYHQIEGiDCSPKVQMAYYRQLAYEDMrDVSLLQYLMD--ETDSSESFSRA-ILNNLGLN 133
Cdd:COG1245 369 LGIVGPNGIGKTTfakILAGVLKPDEG-EVDEDLKISYKPQYISPDY-DGTVEEFLRSanTDDFGSSYYKTeIIKPLGLE 446
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 585044696 134 EALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDI 175
Cdd:COG1245 447 KLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
47-198 |
2.09e-11 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 61.39 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 47 LTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQIEG----------IDCSPKVQMAYYRqlAYEDMRDVSLL-----QY 111
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGqgeillngrpLSDWSAAELARHR--AYLSQQQSPPFampvfQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 112 LM----DETDSSESFSR--AILNNLGLNEALDRSCNVLSGGE--RTKLSLAVL-FSTKAN----MLILDEPTNFLDIKTL 178
Cdd:COG4138 90 LAlhqpAGASSEAVEQLlaQLAEALGLEDKLSRPLTQLSGGEwqRVRLAAVLLqVWPTINpegqLLLLDEPMNSLDVAQQ 169
|
170 180
....*....|....*....|...
gi 585044696 179 EALEMFMNKY--PGI-ILFTSHD 198
Cdd:COG4138 170 AALDRLLRELcqQGItVVMSSHD 192
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
32-207 |
2.13e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 61.74 E-value: 2.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLV-KGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLleaiYHQIEGIdCSPKVQMAYYR--QLAYEDMRDVSL 108
Cdd:PRK13652 4 IETRDLCYSySGSKEALNNINFIAPRNSRIAVIGPNGAGKSTL----FRHFNGI-LKPTSGSVLIRgePITKENIREVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 109 LQYLMDETDSSESFSRAI-------------------------LNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANM 163
Cdd:PRK13652 79 FVGLVFQNPDDQIFSPTVeqdiafgpinlgldeetvahrvssaLHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 585044696 164 LILDEPTNFLDIKTLEALEMFMNKYPG----IILFTSHDTRFVKHVSD 207
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPEtygmTVIFSTHQLDLVPEMAD 206
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
32-197 |
2.18e-11 |
|
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: 60.31 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLV--KGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYH---------QIEGIDCSPKVQMAYYRQLAY 100
Cdd:cd03246 1 LEVENVSFRypGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGllrptsgrvRLDGADISQWDPNELGDHVGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 101 EdMRDVSLlqylmdetdssesFSRAILNnlglnealdrscNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKT--- 177
Cdd:cd03246 81 L-PQDDEL-------------FSGSIAE------------NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGera 134
|
170 180
....*....|....*....|.
gi 585044696 178 -LEALEMfMNKYPGIILFTSH 197
Cdd:cd03246 135 lNQAIAA-LKAAGATRIVIAH 154
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
31-207 |
3.46e-11 |
|
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: 61.84 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 31 PII-AQNLTLV-----KGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYH---------QIEGIDCS-------- 87
Cdd:COG1123 259 PLLeVRNLSKRypvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGllrptsgsiLFDGKDLTklsrrslr 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 88 ---PKVQMAY---YRQL-----AYEDMRDVSLLQYLMDETDSSEsfsRA--ILNNLGLN-EALDRSCNVLSGGERTKLSL 153
Cdd:COG1123 339 elrRRVQMVFqdpYSSLnprmtVGDIIAEPLRLHGLLSRAERRE---RVaeLLERVGLPpDLADRYPHELSGGQRQRVAI 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 585044696 154 AVLFSTKANMLILDEPTNFLD-------IKTLEAL--EMfmnkypGI-ILFTSHDTRFVKHVSD 207
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDvsvqaqiLNLLRDLqrEL------GLtYLFISHDLAVVRYIAD 473
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
47-218 |
3.82e-11 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 60.72 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 47 LTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQIEG----------IDCSPKVQMAYYRqlAY--EDMRDVSLL---QY 111
Cdd:PRK03695 12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGsgsiqfagqpLEAWSAAELARHR--AYlsQQQTPPFAMpvfQY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 112 LM------DETDSSESFSRAILNNLGLNEALDRSCNVLSGGE--RTKLSLAVL-----FSTKANMLILDEPTNFLDIKTL 178
Cdd:PRK03695 90 LTlhqpdkTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEwqRVRLAAVVLqvwpdINPAGQLLLLDEPMNSLDVAQQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 585044696 179 EALEMFMNKYP--GI-ILFTSHDTRFVKHVSDKKWELTGQSLH 218
Cdd:PRK03695 170 AALDRLLSELCqqGIaVVMSSHDLNHTLRHADRVWLLKQGKLL 212
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
45-174 |
4.81e-11 |
|
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: 59.98 E-value: 4.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 45 KLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQIEG---------IDCSP--KVQM----AYYRQL--------AYE 101
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggttsgqilFNGQPrkPDQFqkcvAYVRQDdillpgltVRE 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 585044696 102 DMR--DVSLLQYLMDETDSSESFSRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLD 174
Cdd:cd03234 101 TLTytAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
34-210 |
5.50e-11 |
|
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: 59.89 E-value: 5.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 34 AQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQIEGIDCSP------------------------K 89
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPdegevlldgkdiydldvdvlelrrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 90 VQMAY----------YRQLAY----EDMRDVSLLQYLMdetdsSESFSRAILNNLGLNEALDRScnvLSGGERTKLSLAV 155
Cdd:cd03260 83 VGMVFqkpnpfpgsiYDNVAYglrlHGIKLKEELDERV-----EEALRKAALWDEVKDRLHALG---LSGGQQQRLCLAR 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 585044696 156 LFSTKANMLILDEPTNFLDIKTLEALEMFM----NKYPgiILFTSHDTRFVKHVSDKKW 210
Cdd:cd03260 155 ALANEPEVLLLDEPTSALDPISTAKIEELIaelkKEYT--IVIVTHNMQQAARVADRTA 211
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
41-208 |
6.53e-11 |
|
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: 59.83 E-value: 6.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 41 KGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQ---------IEGIDCSP-----------KVQMAY------ 94
Cdd:cd03257 15 GGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLlkptsgsiiFDGKDLLKlsrrlrkirrkEIQMVFqdpmss 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 95 -------YRQLAyedmrDVSLLQYLMDETDSSESFSRAILNNLGLNEA-LDRSCNVLSGGERTKLSLAVLFSTKANMLIL 166
Cdd:cd03257 95 lnprmtiGEQIA-----EPLRIHGKLSKKEARKEAVLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIARALALNPKLLIA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 585044696 167 DEPTNFLDIKT----LEALEMFMNKYPGIILFTSHDTRFVKHVSDK 208
Cdd:cd03257 170 DEPTSALDVSVqaqiLDLLKKLQEELGLTLLFITHDLGVVAKIADR 215
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
32-197 |
6.66e-11 |
|
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: 59.69 E-value: 6.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLT----LVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYH---------QIEGIDCSpKVQMAYYRQL 98
Cdd:cd03266 2 ITADALTkrfrDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGllepdagfaTVDGFDVV-KEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 99 A--------YEDMRDVSLLQYLMD----ETDSSESFSRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLIL 166
Cdd:cd03266 81 GfvsdstglYDRLTARENLEYFAGlyglKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLL 160
|
170 180 190
....*....|....*....|....*....|....
gi 585044696 167 DEPTNFLDIKTLEALEMFMNKYPGI---ILFTSH 197
Cdd:cd03266 161 DEPTTGLDVMATRALREFIRQLRALgkcILFSTH 194
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
35-208 |
7.19e-11 |
|
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: 61.07 E-value: 7.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 35 QNLTLV--KGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYH------------QIEGIDC---SPKV---QMAY 94
Cdd:COG1123 8 RDLSVRypGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllphggrisgevLLDGRDLlelSEALrgrRIGM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 95 YRQLA---------YEDMRDVSLLQYLmdetDSSESFSRAI--LNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANM 163
Cdd:COG1123 88 VFQDPmtqlnpvtvGDQIAEALENLGL----SRAEARARVLelLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 585044696 164 LILDEPTNFLDIKT----LEALEMFMNKYPGIILFTSHDTRFVKHVSDK 208
Cdd:COG1123 164 LIADEPTTALDVTTqaeiLDLLRELQRERGTTVLLITHDLGVVAEIADR 212
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
57-176 |
9.53e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.59 E-value: 9.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 57 GKNIALVGANGVGKTTLLEAIYHQIE---GIDCSP-------------KVQmAYYRQLAYEDMRDVSLLQY--------- 111
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIpnlGDYEEEpswdevlkrfrgtELQ-NYFKKLYNGEIKVVHKPQYvdlipkvfk 177
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 112 -----LMDETDSSESFsRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIK 176
Cdd:PRK13409 178 gkvreLLKKVDERGKL-DEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIR 246
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
32-175 |
1.04e-10 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 59.40 E-value: 1.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI--YHQIEGIDCS----PKVQMAyYRQLAyeDMRD 105
Cdd:PRK13548 3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsgELSPDSGEVRlngrPLADWS-PAELA--RRRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 106 VsLLQYlmdetdSSESFS-------------------------RAILNNLGLNEALDRSCNVLSGGERTKLSLA-VL--- 156
Cdd:PRK13548 80 V-LPQH------SSLSFPftveevvamgraphglsraeddalvAAALAQVDLAHLAGRDYPQLSGGEQQRVQLArVLaql 152
|
170 180
....*....|....*....|.
gi 585044696 157 --FSTKANMLILDEPTNFLDI 175
Cdd:PRK13548 153 wePDGPPRWLLLDEPTSALDL 173
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
32-204 |
1.27e-10 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 58.91 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLV-KGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYH---------QIEGIDCS--PKVQMAYYR--- 96
Cdd:COG2884 2 IRFENVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGeerptsgqvLVNGQDLSrlKRREIPYLRrri 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 97 -------QL-----AYEdmrDVSL-LQYLmdETDSSESFSR--AILNNLGLNEALDRSCNVLSGGERTKLSL--AVLfsT 159
Cdd:COG2884 82 gvvfqdfRLlpdrtVYE---NVALpLRVT--GKSRKEIRRRvrEVLDLVGLSDKAKALPHELSGGEQQRVAIarALV--N 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 585044696 160 KANMLILDEPTNFLDIKT-LEALEMFM--NKYpGI-ILFTSHDTRFVKH 204
Cdd:COG2884 155 RPELLLADEPTGNLDPETsWEIMELLEeiNRR-GTtVLIATHDLELVDR 202
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
47-202 |
1.97e-10 |
|
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: 58.19 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 47 LTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQ---------IEGIDCS--PKVQMAYYRQ---LAYEDMRDVSLLQ-- 110
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEelptsgtirVNGQDVSdlRGRAIPYLRRkigVVFQDFRLLPDRNvy 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 111 ----YLMDETDSSESFSR----AILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTL-EAL 181
Cdd:cd03292 97 envaFALEVTGVPPREIRkrvpAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTwEIM 176
|
170 180
....*....|....*....|...
gi 585044696 182 EMF--MNKYPGIILFTSHDTRFV 202
Cdd:cd03292 177 NLLkkINKAGTTVVVATHAKELV 199
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
34-197 |
2.05e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 57.96 E-value: 2.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 34 AQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI------------YHQIEGIDCSPKVQMAYyrqLAYE 101
Cdd:PRK13539 5 GEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIagllppaagtikLDGGDIDDPDVAEACHY---LGHR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 102 D-MRDV-SLLQYLmdetdsseSFSRAILNN-----------LGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDE 168
Cdd:PRK13539 82 NaMKPAlTVAENL--------EFWAAFLGGeeldiaaaleaVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDE 153
|
170 180 190
....*....|....*....|....*....|....*
gi 585044696 169 PTNFLDIktlEALEMFMN------KYPGIILFTSH 197
Cdd:PRK13539 154 PTAALDA---AAVALFAElirahlAQGGIVIAATH 185
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
32-182 |
2.81e-10 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 59.09 E-value: 2.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLVKGSQKLLTQ-VRFQIPYGKNIALVGANGVGKTTLLEAI-----YH---QIEGIDCSPKVQMAYYRQLAY-- 100
Cdd:PRK11174 350 IEAEDLEILSPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALlgflpYQgslKINGIELRELDPESWRKHLSWvg 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 101 ------------------EDMRDVSLLQyLMDETDSSEsFSRAILNnlGLNEAL-DRSCNvLSGGERTKLSLAVLFSTKA 161
Cdd:PRK11174 430 qnpqlphgtlrdnvllgnPDASDEQLQQ-ALENAWVSE-FLPLLPQ--GLDTPIgDQAAG-LSVGQAQRLALARALLQPC 504
|
170 180
....*....|....*....|....*
gi 585044696 162 NMLILDEPTNFLDI----KTLEALE 182
Cdd:PRK11174 505 QLLLLDEPTASLDAhseqLVMQALN 529
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
31-208 |
3.37e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 58.52 E-value: 3.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 31 PIIAQNLTLV--KGS---QKLLTQVRFQIPYGKNIALVGANGVGKTTLLE-----------AIYhqIEGIDCSPK-VQMA 93
Cdd:PRK13637 2 SIKIENLTHIymEGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQhlngllkptsgKII--IDGVDITDKkVKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 94 YYRqlayedmRDVSLL-QY----LMDET-DSSESFSraiLNNLGLNEA--------------------LDRSCNVLSGGE 147
Cdd:PRK13637 80 DIR-------KKVGLVfQYpeyqLFEETiEKDIAFG---PINLGLSEEeienrvkramnivgldyedyKDKSPFELSGGQ 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 585044696 148 RTKLSLAVLFSTKANMLILDEPTNFLDIKT----LEALEMFMNKYPGIILFTSHDTRFVKHVSDK 208
Cdd:PRK13637 150 KRRVAIAGVVAMEPKILILDEPTAGLDPKGrdeiLNKIKELHKEYNMTIILVSHSMEDVAKLADR 214
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
22-200 |
4.27e-10 |
|
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: 57.73 E-value: 4.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 22 KIYDIHNNYPIIAQNL-TLVKGSQKLLTQVR---FQIPYGKNIALVGANGVGKTT---LLEAIYHQIEGidcspKVQMA- 93
Cdd:cd03267 8 KSYRVYSKEPGLIGSLkSLFKRKYREVEALKgisFTIEKGEIVGFIGPNGAGKTTtlkILSGLLQPTSG-----EVRVAg 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 94 ---YYRQLAYedMRDVSLL----QYLMDETDSSESFS--RAILN---------------NLGLNEALDRSCNVLSGGERT 149
Cdd:cd03267 83 lvpWKRRKKF--LRRIGVVfgqkTQLWWDLPVIDSFYllAAIYDlpparfkkrldelseLLDLEELLDTPVRQLSLGQRM 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 585044696 150 KLSLAVLFSTKANMLILDEPTNFLDIKTLEALEMFM---NKYPGI-ILFTSHDTR 200
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLkeyNRERGTtVLLTSHYMK 215
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
35-205 |
4.48e-10 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 58.07 E-value: 4.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 35 QNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQIEGIDCSPKVQMAYYRQLAYEDM-RDVSLL---- 109
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVaRRIGLLaqna 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 110 --------QYLMDE-------------TDSSESFSRAiLNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDE 168
Cdd:PRK10253 91 ttpgditvQELVARgryphqplftrwrKEDEEAVTKA-MQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 585044696 169 PTNFLDIK-TLEALEMF--MNKYPGIILFTS-HD----TRFVKHV 205
Cdd:PRK10253 170 PTTWLDIShQIDLLELLseLNREKGYTLAAVlHDlnqaCRYASHL 214
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
41-177 |
4.99e-10 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 57.48 E-value: 4.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 41 KGSQKL--LTQVRFQIPYGKNIALVGANGVGKTTLLeAIyhqIEGID--CSPKVQM----------AYYRQLAYED---- 102
Cdd:PRK10584 18 QGEHELsiLTGVELVVKRGETIALIGESGSGKSTLL-AI---LAGLDdgSSGEVSLvgqplhqmdeEARAKLRAKHvgfv 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 103 ------------MRDVSLLQYLMDETD-SSESFSRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEP 169
Cdd:PRK10584 94 fqsfmliptlnaLENVELPALLRGESSrQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEP 173
|
....*...
gi 585044696 170 TNFLDIKT 177
Cdd:PRK10584 174 TGNLDRQT 181
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
32-204 |
5.88e-10 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 56.98 E-value: 5.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLV--KGSQKL--LTQVRFQIPYGKNIALVGANGVGKTTLLEAI----------YHqIEGIDCS--PKVQMAYY 95
Cdd:COG1136 5 LELRNLTKSygTGEGEVtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILggldrptsgeVL-IDGQDISslSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 96 RQlayedmRDVS-------LLQYL-----------MDETDSSESFSRA--ILNNLGLNEALDRSCNVLSGGERTKLSLAV 155
Cdd:COG1136 84 RR------RHIGfvfqffnLLPELtalenvalpllLAGVSRKERRERAreLLERVGLGDRLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 585044696 156 LFSTKANMLILDEPTNFLDIKT-LEALEMF--MNKYPGI-ILFTSHDTRFVKH 204
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTgEEVLELLreLNRELGTtIVMVTHDPELAAR 210
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
32-208 |
6.92e-10 |
|
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: 56.04 E-value: 6.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYH---------QIEGIDcspkvqMAYYRQLAYED 102
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGleepdsgsiLIDGED------LTDLEDELPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 103 MRDVSLL--QYLMdetdssesFSR-AILNNLGLnealdrscnVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTLE 179
Cdd:cd03229 75 RRRIGMVfqDFAL--------FPHlTVLENIAL---------GLSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRR 137
|
170 180 190
....*....|....*....|....*....|...
gi 585044696 180 ALEMFM---NKYPGI-ILFTSHDTRFVKHVSDK 208
Cdd:cd03229 138 EVRALLkslQAQLGItVVLVTHDLDEAARLADR 170
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
32-198 |
9.48e-10 |
|
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: 56.36 E-value: 9.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLV--KGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQ---------IEGIDCSPkvQMAYYRQL-- 98
Cdd:cd03263 1 LQIRNLTKTykKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGElrptsgtayINGYSIRT--DRKAARQSlg 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 99 -------------AYEDMRDVSLLQYLMDETDSSESfsRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLI 165
Cdd:cd03263 79 ycpqfdalfdeltVREHLRFYARLKGLPKSEIKEEV--ELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190
....*....|....*....|....*....|....*.
gi 585044696 166 LDEPTNFLDIKTLEALEMFMNKY---PGIILfTSHD 198
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEVrkgRSIIL-TTHS 191
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
42-181 |
9.49e-10 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 56.09 E-value: 9.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 42 GSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIY----------------------HQIEGIDCSP-----KVQM-- 92
Cdd:NF040873 3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAgvlrptsgtvrraggarvayvpQRSEVPDSLPltvrdLVAMgr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 93 ----AYYRQLAYEDMRDVSllqylmdetdssesfsrAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDE 168
Cdd:NF040873 83 warrGLWRRLTRDDRAAVD-----------------DALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170
....*....|...
gi 585044696 169 PTNFLDIKTLEAL 181
Cdd:NF040873 146 PTTGLDAESRERI 158
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
32-181 |
1.04e-09 |
|
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: 55.24 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLVKGSQK-LLTQVRFQIPYGKNIALVGANGVGKTTLLEAI-----YHQieG-IDCSPKVQMAYYRQLAYedMR 104
Cdd:cd03223 1 IELENLSLATPDGRvLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALaglwpWGS--GrIGMPEGEDLLFLPQRPY--LP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 105 DVSLLQ---YLMDEtdssesfsrailnnlglnealdrscnVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTLEAL 181
Cdd:cd03223 77 LGTLREqliYPWDD--------------------------VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRL 130
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
42-182 |
1.05e-09 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 57.48 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 42 GSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLE-----------AIYhqIEGIDcspkvqmayYRQLAYEDMRD-VSL- 108
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNlllrfydptsgRIL--IDGVD---------IRDLTLESLRRqIGVv 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 109 LQ--YLmdetdssesFSRAILNNLGL----------NEALDRSC--------------------NVLSGGERTKLSLAVL 156
Cdd:COG1132 420 PQdtFL---------FSGTIRENIRYgrpdatdeevEEAAKAAQahefiealpdgydtvvgergVNLSGGQRQRIAIARA 490
|
170 180 190
....*....|....*....|....*....|
gi 585044696 157 FSTKANMLILDEPTNFLDIKT----LEALE 182
Cdd:COG1132 491 LLKDPPILILDEATSALDTETealiQEALE 520
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
57-176 |
1.63e-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: 57.10 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 57 GKNIALVGANGVGKTTLLEAIYHQIE---GIDCSP-------------KVQmAYYRQLAYEDMRDVSLLQY--------- 111
Cdd:COG1245 99 GKVTGILGPNGIGKSTALKILSGELKpnlGDYDEEpswdevlkrfrgtELQ-DYFKKLANGEIKVAHKPQYvdlipkvfk 177
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 112 -----LMDETDSSESFsRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIK 176
Cdd:COG1245 178 gtvreLLEKVDERGKL-DELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIY 246
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
47-208 |
1.89e-09 |
|
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: 55.62 E-value: 1.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 47 LTQVRFQIPYGKNIALVGANGVGKTTLLEA---IYHQIEG---IDCSPKVQMA---------------YYRQLAY----E 101
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLlagIYPPDSGtvtVRGRVSSLLGlgggfnpeltgreniYLNGRLLglsrK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 102 DMRDVsllqylMDETdssESFSrailnnlGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPT-----NFLDiK 176
Cdd:cd03220 118 EIDEK------IDEI---IEFS-------ELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLavgdaAFQE-K 180
|
170 180 190
....*....|....*....|....*....|..
gi 585044696 177 TLEALEMFMNKyPGIILFTSHDTRFVKHVSDK 208
Cdd:cd03220 181 CQRRLRELLKQ-GKTVILVSHDPSSIKRLCDR 211
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
57-176 |
3.28e-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: 55.45 E-value: 3.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 57 GKNIALVGANGVGKTTLLEAIYHQIE---GIDCSP-------------KVQmAYYRQLAYEDMRDVSLLQY--------- 111
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKpnlGKFDDPpdwdeildefrgsELQ-NYFTKLLEGDVKVIVKPQYvdlipkavk 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 112 -----LMDETDSSESFSRaILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIK 176
Cdd:cd03236 105 gkvgeLLKKKDERGKLDE-LVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
50-208 |
3.71e-09 |
|
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: 55.50 E-value: 3.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 50 VRFQIPYGKNIALVGANGVGKTTLLEAIY-------HQIE-----------GIDCSP-KVQMAYYRQLA--YEDMRDVSL 108
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAgltrpdeGEIVlngrtlfdsrkGIFLPPeKRRIGYVFQEArlFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 109 LQYLMDETDSSESFSR--AILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKT----LEALE 182
Cdd:TIGR02142 96 LRYGMKRARPSERRISfeRVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRkyeiLPYLE 175
|
170 180
....*....|....*....|....*.
gi 585044696 183 MFMNKYPGIILFTSHDTRFVKHVSDK 208
Cdd:TIGR02142 176 RLHAEFGIPILYVSHSLQEVLRLADR 201
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
47-216 |
8.24e-09 |
|
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: 53.98 E-value: 8.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 47 LTQVRFQIPYGKNIALVGANGVGKTTLLEAIY-------------HQIEGID---CSPkVQMAYYRQ--LAYedmrdVSl 108
Cdd:COG4778 27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYgnylpdsgsilvrHDGGWVDlaqASP-REILALRRrtIGY-----VS- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 109 lQYL-----------------MDETDSSESFSRA--ILNNLGLNEAL-DRSCNVLSGGERTKLSLAVLFSTKANMLILDE 168
Cdd:COG4778 100 -QFLrviprvsaldvvaepllERGVDREEARARAreLLARLNLPERLwDLPPATFSGGEQQRVNIARGFIADPPLLLLDE 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 585044696 169 PTNFLDIKT----LEALEMFMNKYPGII-LFtsHDTRFVKHVSDKKWELTGQS 216
Cdd:COG4778 179 PTASLDAANravvVELIEEAKARGTAIIgIF--HDEEVREAVADRVVDVTPFS 229
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
61-207 |
1.70e-08 |
|
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: 52.61 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 61 ALVGANGVGKTTLLEAIYHQIEGIDCSPKVQMAYYRQLAYEDMRDVSLlqYLMDETDSSESF----SRAILNNL------ 130
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKYALTGELPPNSKGGAHDPKLIREGEVRAQV--KLAFENANGKKYtitrSLAILENVifchqg 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 131 GLNEALDRSCNVLSGGERTKLSLAV------LFSTKANMLILDEPTNFLD-----IKTLEALEMFMNKYPGIILFTSHDT 199
Cdd:cd03240 104 ESNWPLLDMRGRCSGGEKVLASLIIrlalaeTFGSNCGILALDEPTTNLDeenieESLAEIIEERKSQKNFQLIVITHDE 183
|
....*...
gi 585044696 200 RFVKHVSD 207
Cdd:cd03240 184 ELVDAADH 191
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
43-204 |
1.86e-08 |
|
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: 53.00 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 43 SQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYH---------QIEGIDCSpKVQMAYYRQ---------------- 97
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRfydvssgsiLIDGQDIR-EVTLDSLRRaigvvpqdtvlfndti 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 98 ---LAY-------EDMRDVSLLQYLMDETDSSESFSRAILNNLGLNealdrscnvLSGGERTKLSLAVLFSTKANMLILD 167
Cdd:cd03253 92 gynIRYgrpdatdEEVIEAAKAAQIHDKIMRFPDGYDTIVGERGLK---------LSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190
....*....|....*....|....*....|....*..
gi 585044696 168 EPTNFLDIKTLEALEMFMNKypgiiLFTSHDTRFVKH 204
Cdd:cd03253 163 EATSALDTHTEREIQAALRD-----VSKGRTTIVIAH 194
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
57-174 |
2.63e-08 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 53.51 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 57 GKNIALVGANGVGKTTLLEAIYHQIE-GIDCSPKV----------QM----AYYRQ--------LAYEDMRDVSLLQyLM 113
Cdd:TIGR00955 51 GELLAVMGSSGAGKTTLMNALAFRSPkGVKGSGSVllngmpidakEMraisAYVQQddlfiptlTVREHLMFQAHLR-MP 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 585044696 114 DETDSSESFSR--AILNNLGLNEALD------RSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLD 174
Cdd:TIGR00955 130 RRVTKKEKRERvdEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLD 198
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-208 |
2.74e-08 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 52.79 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 20 QNKIYDIHNNYPIIAQ-NLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYH---QIEGIDCSPKVQMAYY 95
Cdd:PRK14271 9 QSGAADVDAAAPAMAAvNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRmndKVSGYRYSGDVLLGGR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 96 RQLAYEDM----RDVSLL--------QYLMDETDSS------------ESFSRAILNNLGLNEAL-DRSCNV---LSGGE 147
Cdd:PRK14271 89 SIFNYRDVlefrRRVGMLfqrpnpfpMSIMDNVLAGvrahklvprkefRGVAQARLTEVGLWDAVkDRLSDSpfrLSGGQ 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 585044696 148 RTKLSLAVLFSTKANMLILDEPTNFLDIKTLEALEMFMNKYPG--IILFTSHDTRFVKHVSDK 208
Cdd:PRK14271 169 QQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADrlTVIIVTHNLAQAARISDR 231
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
43-174 |
3.06e-08 |
|
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: 53.18 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 43 SQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI---YHQIEGIDCSPKVQMAYY------RQLA-------------- 99
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIprfYEPDSGQILLDGHDLADYtlaslrRQVAlvsqdvvlfndtia 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 100 ----YEDMRDVSLLQ--------YLMDETDSSEsfsRAILNNLGLNEALdrscnvLSGGERTKLSLAVLFSTKANMLILD 167
Cdd:TIGR02203 424 nniaYGRTEQADRAEieralaaaYAQDFVDKLP---LGLDTPIGENGVL------LSGGQRQRLAIARALLKDAPILILD 494
|
....*..
gi 585044696 168 EPTNFLD 174
Cdd:TIGR02203 495 EATSALD 501
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
57-201 |
3.07e-08 |
|
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: 51.22 E-value: 3.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 57 GKNIALVGANGVGKTTLLEAIYHQIEgidcspkvqmayyrqlayEDMRDVSLLqylmdetdsSESFSRAILNNLGLNEAL 136
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELG------------------PPGGGVIYI---------DGEDILEEVLDQLLLIIV 54
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 585044696 137 DRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKT---------LEALEMFMNKYPGIILFTSHDTRF 201
Cdd:smart00382 55 GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQeallllleeLRLLLLLKSEKNLTVILTTNDEKD 128
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
35-208 |
3.11e-08 |
|
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: 52.12 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 35 QNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQ---------IEGID---CSPK------VQMAYYR 96
Cdd:cd03261 4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLlrpdsgevlIDGEDisgLSEAelyrlrRRMGMLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 97 QLA--YEDMrdvSLLQ----YLMDETDSSESFSRAI----LNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLIL 166
Cdd:cd03261 84 QSGalFDSL---TVFEnvafPLREHTRLSEEEIREIvlekLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 585044696 167 DEPTNFLDIKT---LEALEMFMNKYPGI-ILFTSHDTRFVKHVSDK 208
Cdd:cd03261 161 DEPTAGLDPIAsgvIDDLIRSLKKELGLtSIMVTHDLDTAFAIADR 206
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
41-187 |
3.62e-08 |
|
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: 51.48 E-value: 3.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 41 KGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQ-----IEG---IDCSPKVqMAYYRQLAYEDMRDVSllqyl 112
Cdd:cd03232 17 GGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRktagvITGeilINGRPLD-KNFQRSTGYVEQQDVH----- 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 585044696 113 mdetdssesfsraiLNNLGLNEALDRSCNV--LSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTLEALEMFMNK 187
Cdd:cd03232 91 --------------SPNLTVREALRFSALLrgLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKK 153
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
49-198 |
3.72e-08 |
|
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: 51.91 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 49 QVRFQIPyGKNIALVGANGVGKTTLL------EAIYH-QIE-----------GIDCSP-KVQMAY-YRQLA-YEDMRDVS 107
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLrciaglEKPDGgTIVlngtvlfdsrkKINLPPqQRKIGLvFQQYAlFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 108 LLQYLMDETDSSES--FSRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTLEALEMFM 185
Cdd:cd03297 95 NLAFGLKRKRNREDriSVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174
|
170
....*....|....*..
gi 585044696 186 NK----YPGIILFTSHD 198
Cdd:cd03297 175 KQikknLNIPVIFVTHD 191
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
32-204 |
3.75e-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: 52.83 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLVKGS-QKLLTQVRFQIPYGKNIALVGANGVGKTTL------LEAIYHQIEGIDcsPKVQMAYYRQLAYEDMR 104
Cdd:TIGR00954 452 IKFENIPLVTPNgDVLIESLSFEVPSGNNLLICGPNGCGKSSLfrilgeLWPVYGGRLTKP--AKGKLFYVPQRPYMTLG 529
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 105 DvsllqyLMDET---DSSESFSR---------AILNNLGLNEALDRS------CN---VLSGGERTKLSLAVLFSTKANM 163
Cdd:TIGR00954 530 T------LRDQIiypDSSEDMKRrglsdkdleQILDNVQLTHILEREggwsavQDwmdVLSGGEKQRIAMARLFYHKPQF 603
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 585044696 164 LILDEPTNFLDIKTLEALEMFMNKYpGIILFT-SHDTRFVKH 204
Cdd:TIGR00954 604 AILDECTSAVSVDVEGYMYRLCREF-GITLFSvSHRKSLWKY 644
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
44-206 |
4.52e-08 |
|
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: 51.82 E-value: 4.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 44 QKLLTQVRFQIPYGKNIALVGANGVGKTTLLE-----------AIYhqIEGIDcspkvqmayYRQLAYEDMR-------- 104
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKllaglykptsgSVL--LDGTD---------IRQLDPADLRrnigyvpq 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 105 DVSLL------QYLMDETDSSESFSRAILNNLGLNEALDRSCN-----------VLSGGERTKLSLAVLFSTKANMLILD 167
Cdd:cd03245 86 DVTLFygtlrdNITLGAPLADDERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 585044696 168 EPTNFLDIKTLEALEMFMNKYPG--IILFTSHDTRFVKHVS 206
Cdd:cd03245 166 EPTSAMDMNSEERLKERLRQLLGdkTLIIITHRPSLLDLVD 206
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
34-208 |
4.60e-08 |
|
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: 51.67 E-value: 4.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 34 AQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI---Y-------------------HQI--EGI----- 84
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLIsgfLrptsgsvlfdgeditglppHEIarLGIgrtfq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 85 -----------DCspkVQMAYYRQLAyedmRDVSLLQYLMDETDSSESfSRAILNNLGLNEALDRSCNVLSGGERTKLSL 153
Cdd:cd03219 83 iprlfpeltvlEN---VMVAAQARTG----SGLLLARARREEREARER-AEELLERVGLADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 585044696 154 AVLFSTKANMLILDEPT---NFLDIKTLEALEMFMNKYpGI-ILFTSHDTRFVKHVSDK 208
Cdd:cd03219 155 ARALATDPKLLLLDEPAaglNPEETEELAELIRELRER-GItVLLVEHDMDVVMSLADR 212
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
41-174 |
4.65e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.06 E-value: 4.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 41 KGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQIEGIDCSPKV---QMAYYRQLAYedMRDVSLLQYLMDETD 117
Cdd:PLN03232 627 KTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVirgSVAYVPQVSW--IFNATVRENILFGSD 704
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 585044696 118 -SSESFSRAI-----------LNNLGLNEALDRSCNVlSGGERTKLSLAVLFSTKANMLILDEPTNFLD 174
Cdd:PLN03232 705 fESERYWRAIdvtalqhdldlLPGRDLTEIGERGVNI-SGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
35-205 |
5.44e-08 |
|
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: 50.99 E-value: 5.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 35 QNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI-----YHQIEGidcspkvqmayyrQLAYEDmrdVSLL 109
Cdd:cd03217 4 KDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImghpkYEVTEG-------------EILFKG---EDIT 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 110 QYLMDEtdssesfsRAilnNLGL--------------NEALDRSCNV-LSGGERTKLSLAVLFSTKANMLILDEPTNFLD 174
Cdd:cd03217 68 DLPPEE--------RA---RLGIflafqyppeipgvkNADFLRYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136
|
170 180 190
....*....|....*....|....*....|....*
gi 585044696 175 IKTLEALEMFMNKY----PGIILFTsHDTRFVKHV 205
Cdd:cd03217 137 IDALRLVAEVINKLreegKSVLIIT-HYQRLLDYI 170
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
32-208 |
7.05e-08 |
|
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: 51.19 E-value: 7.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQ---------IEGIDCSPK-VQ---------- 91
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLerpdsgtilFGGEDATDVpVQernvgfvfqh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 92 MAYYRQLAYEDmrDVSL-LQYLMDETDSSESFSRAILNNL----GLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLIL 166
Cdd:cd03296 83 YALFRHMTVFD--NVAFgLRVKPRSERPPEAEIRAKVHELlklvQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 585044696 167 DEPTNFLDIKTLEALEMFMNKYPGII----LFTSHDTRFVKHVSDK 208
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELhvttVFVTHDQEEALEVADR 206
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
25-175 |
7.21e-08 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 51.33 E-value: 7.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 25 DIHNNYPIIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI-YHQ--IEG---IDCSPKVQM---AYY 95
Cdd:PRK10575 5 TNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLgRHQppSEGeilLDAQPLESWsskAFA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 96 RQLAY--------EDM--RD-VSLLQY-------LMDETDSsESFSRAIlNNLGLNEALDRSCNVLSGGERTKLSLAVLF 157
Cdd:PRK10575 85 RKVAYlpqqlpaaEGMtvRElVAIGRYpwhgalgRFGAADR-EKVEEAI-SLVGLKPLAHRLVDSLSGGERQRAWIAMLV 162
|
170
....*....|....*...
gi 585044696 158 STKANMLILDEPTNFLDI 175
Cdd:PRK10575 163 AQDSRCLLLDEPTSALDI 180
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
41-208 |
7.83e-08 |
|
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: 51.34 E-value: 7.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 41 KGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYH---------QIEGIDCS---PKVQMAYYR--QLAYED---- 102
Cdd:TIGR02769 21 KQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGlekpaqgtvSFRGQDLYqldRKQRRAFRRdvQLVFQDspsa 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 103 ------MRDV---SLLQYL-MDETDSSESFSrAILNNLGL-NEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTN 171
Cdd:TIGR02769 101 vnprmtVRQIigePLRHLTsLDESEQKARIA-ELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 585044696 172 FLDI----KTLEALEMFMNKYPGIILFTSHDTRFVKHVSDK 208
Cdd:TIGR02769 180 NLDMvlqaVILELLRKLQQAFGTAYLFITHDLRLVQSFCQR 220
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
47-185 |
9.06e-08 |
|
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: 51.08 E-value: 9.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 47 LTQVRFQIPYGKNIALVGANGVGKTTLLEAI---YH------QIEGIDC------SPKVQMAYYRQ------------LA 99
Cdd:cd03251 18 LRDISLDIPAGETVALVGPSGSGKSTLVNLIprfYDvdsgriLIDGHDVrdytlaSLRRQIGLVSQdvflfndtvaenIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 100 Y-------EDMRDVSLLQYLMDETDSSESFSRAILNNLGLNealdrscnvLSGGERTKLSLAVLFSTKANMLILDEPTNF 172
Cdd:cd03251 98 YgrpgatrEEVEEAARAANAHEFIMELPEGYDTVIGERGVK---------LSGGQRQRIAIARALLKDPPILILDEATSA 168
|
170
....*....|....*..
gi 585044696 173 LDIKT----LEALEMFM 185
Cdd:cd03251 169 LDTESerlvQAALERLM 185
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
52-208 |
1.17e-07 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 50.85 E-value: 1.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 52 FQIPYGKNIALVGANGVGKTTLLEAI---YHQIEG-IDCSPKV-----------------QMAYYRQLAY----EDMRDV 106
Cdd:COG1134 47 FEVERGESVGIIGRNGAGKSTLLKLIagiLEPTSGrVEVNGRVsallelgagfhpeltgrENIYLNGRLLglsrKEIDEK 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 107 sllqylMDETdssESFSrailnnlGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPT-----NFLDiKTLEAL 181
Cdd:COG1134 127 ------FDEI---VEFA-------ELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLavgdaAFQK-KCLARI 189
|
170 180
....*....|....*....|....*..
gi 585044696 182 EMFMNKyPGIILFTSHDTRFVKHVSDK 208
Cdd:COG1134 190 RELRES-GRTVIFVSHSMGAVRRLCDR 215
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
47-192 |
1.42e-07 |
|
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: 50.30 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 47 LTQVRFQIPYGKNIALVGANGVGKTTLLE-----------AIYhqIEGIDcspkvqmayYRQLAYEDMRdvSLLQYLMDE 115
Cdd:cd03254 19 LKDINFSIKPGETVAIVGPTGAGKTTLINllmrfydpqkgQIL--IDGID---------IRDISRKSLR--SMIGVVLQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 116 TdssESFSRAILNN--LGLNEALDRSCNV----------------------------LSGGERTKLSLAVLFSTKANMLI 165
Cdd:cd03254 86 T---FLFSGTIMENirLGRPNATDEEVIEaakeagahdfimklpngydtvlgenggnLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190
....*....|....*....|....*....|.
gi 585044696 166 LDEPTNFLDIKT----LEALEMFMNKYPGII 192
Cdd:cd03254 163 LDEATSNIDTETekliQEALEKLMKGRTSII 193
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
32-198 |
1.88e-07 |
|
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: 49.83 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI---YHQIEG---IDCSPKVQMAYYRqlayedmRD 105
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIaglERPDSGeilIDGRDVTGVPPER-------RN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 106 VSLL--QY-------------------LMDETDSSESfSRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANML 164
Cdd:cd03259 74 IGMVfqDYalfphltvaeniafglklrGVPKAEIRAR-VRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 585044696 165 ILDEPTNFLDIKTLEAL-----EMFMNKypGI-ILFTSHD 198
Cdd:cd03259 153 LLDEPLSALDAKLREELreelkELQREL--GItTIYVTHD 190
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
47-203 |
2.08e-07 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 49.66 E-value: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 47 LTQVRFQIPYGKNIALVGANGVGKTTLLeaiyHQIEGID--CSPKV-------------QMAYYRQLA-------YEDMR 104
Cdd:TIGR02211 21 LKGVSLSIGKGEIVAIVGSSGSGKSTLL----HLLGGLDnpTSGEVlfngqslsklssnERAKLRNKKlgfiyqfHHLLP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 105 DVSLLQYLM-------DETDSSESFSRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKT 177
Cdd:TIGR02211 97 DFTALENVAmplligkKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGNLDNNN 176
|
170 180 190
....*....|....*....|....*....|
gi 585044696 178 LEALEMFM---NKYPGI-ILFTSHDTRFVK 203
Cdd:TIGR02211 177 AKIIFDLMlelNRELNTsFLVVTHDLELAK 206
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
30-174 |
2.16e-07 |
|
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: 51.10 E-value: 2.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 30 YPIIAQN--LTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQIEGID--CSPKVQMAYYRQLAYedMRD 105
Cdd:TIGR00957 635 NSITVHNatFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEghVHMKGSVAYVPQQAW--IQN 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 106 VSLLQYLMDETDSSESFSRAILNNLGL------------NEALDRSCNvLSGGERTKLSLAVLFSTKANMLILDEPTNFL 173
Cdd:TIGR00957 713 DSLRENILFGKALNEKYYQQVLEACALlpdleilpsgdrTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
.
gi 585044696 174 D 174
Cdd:TIGR00957 792 D 792
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
62-212 |
2.24e-07 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 50.01 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 62 LVGANGVGKTTLLE-----------AIYHQIEGIDCSPKVQMAYYRQLA--YEDMRDvsllQYLMDETDSSESFSraiLN 128
Cdd:PRK13638 32 LVGANGCGKSTLFMnlsgllrpqkgAVLWQGKPLDYSKRGLLALRQQVAtvFQDPEQ----QIFYTDIDSDIAFS---LR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 129 NLGLNEA-----LDRSCNV-------------LSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTLEALEMFMNKYPG 190
Cdd:PRK13638 105 NLGVPEAeitrrVDEALTLvdaqhfrhqpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVA 184
|
170 180
....*....|....*....|....*
gi 585044696 191 I---ILFTSHDTRFVKHVSDKKWEL 212
Cdd:PRK13638 185 QgnhVIISSHDIDLIYEISDAVYVL 209
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
25-197 |
2.81e-07 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 50.49 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 25 DIHNNYPI-----IAQNLTlvkgsqklltqvrFQIPYGKNIALVGANGVGKTT---LLEAIYHQIEG---IDCSPKVQM- 92
Cdd:TIGR00958 483 DVSFSYPNrpdvpVLKGLT-------------FTLHPGEVVALVGPSGSGKSTvaaLLQNLYQPTGGqvlLDGVPLVQYd 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 93 --AYYRQLAYEDMRDV------------SLLQYLMDETDSS--ESFSRAILNNL--GLNEALDRSCNVLSGGERTKLSLA 154
Cdd:TIGR00958 550 hhYLHRQVALVGQEPVlfsgsvreniayGLTDTPDEEIMAAakAANAHDFIMEFpnGYDTEVGEKGSQLSGGQKQRIAIA 629
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 585044696 155 VLFSTKANMLILDEPTNFLDIKTLEALEMFMNKYPGIILFTSH 197
Cdd:TIGR00958 630 RALVRKPRVLILDEATSALDAECEQLLQESRSRASRTVLLIAH 672
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
32-200 |
2.81e-07 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 49.58 E-value: 2.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYH---------QIEGIDCS-------PKVQMAY- 94
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGlvrpdagkiLIDGQDIThlpmherARLGIGYl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 95 ------YRQLAYED-MRDVSLLQYLMDEtDSSESFSRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILD 167
Cdd:TIGR04406 82 pqeasiFRKLTVEEnIMAVLEIRKDLDR-AEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 585044696 168 E------PTNFLDIKTLealeMFMNKYPGI-ILFTSHDTR 200
Cdd:TIGR04406 161 EpfagvdPIAVGDIKKI----IKHLKERGIgVLITDHNVR 196
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
32-205 |
4.84e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.51 E-value: 4.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQIE----GIDCSPKVQMAYYRQ--LAYEDMR- 104
Cdd:PRK15064 2 LSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEpsagNVSLDPNERLGKLRQdqFAFEEFTv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 105 -DVSLLQYL-----------------MDETD-----------------SSESFSRAILnnLGLNEALDRSCNVLSG---G 146
Cdd:PRK15064 82 lDTVIMGHTelwevkqerdriyalpeMSEEDgmkvadlevkfaemdgyTAEARAGELL--LGVGIPEEQHYGLMSEvapG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 147 ERTKLSLA-VLFStKANMLILDEPTNFLDIKTLEALEMFMNKYPGIILFTSHDTRFVKHV 205
Cdd:PRK15064 160 WKLRVLLAqALFS-NPDILLLDEPTNNLDINTIRWLEDVLNERNSTMIIISHDRHFLNSV 218
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
42-177 |
5.03e-07 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 49.57 E-value: 5.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 42 GSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLeAIYHQ----------IEGIDCSpKVQMAYYRQLAYEDMRDVSLlqy 111
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI-NLLQRvfdpqsgrilIDGTDIR-TVTRASLRRNIAVVFQDAGL--- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 112 lmdetdssesFSRAILNNLG----------LNEALDRSC--------------------NVLSGGERTKLSLAVLFSTKA 161
Cdd:PRK13657 421 ----------FNRSIEDNIRvgrpdatdeeMRAAAERAQahdfierkpdgydtvvgergRQLSGGERQRLAIARALLKDP 490
|
170
....*....|....*.
gi 585044696 162 NMLILDEPTNFLDIKT 177
Cdd:PRK13657 491 PILILDEATSALDVET 506
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
42-207 |
5.20e-07 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 48.56 E-value: 5.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 42 GSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQI---------EGIDCSPKVQMAYYRQLAY---------EDM 103
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLIsptsgtllfEGEDISTLKPEIYRQQVSYcaqtptlfgDTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 104 RDVSLLQYLMDETDSSESFSRAILNNLGL-NEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTLEALE 182
Cdd:PRK10247 98 YDNLIFPWQIRNQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVN 177
|
170 180
....*....|....*....|....*....
gi 585044696 183 MFMNKY---PGI-ILFTSHDTRFVKHVSD 207
Cdd:PRK10247 178 EIIHRYvreQNIaVLWVTHDKDEINHADK 206
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
47-208 |
6.20e-07 |
|
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: 48.49 E-value: 6.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 47 LTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQI---------EGIDCSP----KVQMAY-------------YRQLAY 100
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIkpdsgkillNGKDITNlppeKRDISYvpqnyalfphmtvYKNIAY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 101 eDMRdvslLQYLMDETDSSESfsRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTLEA 180
Cdd:cd03299 95 -GLK----KRKVDKKEIERKV--LEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEK 167
|
170 180 190
....*....|....*....|....*....|..
gi 585044696 181 LEMFMNK----YPGIILFTSHDTRFVKHVSDK 208
Cdd:cd03299 168 LREELKKirkeFGVTVLHVTHDFEEAWALADK 199
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
37-207 |
6.97e-07 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 48.50 E-value: 6.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 37 LTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQIEGIDCSPKV-------------------------- 90
Cdd:PRK14246 16 LYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVdgkvlyfgkdifqidaiklrkevgmv 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 91 --------QMAYYRQLAY----EDMRDVSLLQYLMDETdssesfsraiLNNLGL----NEALDRSCNVLSGGERTKLSLA 154
Cdd:PRK14246 96 fqqpnpfpHLSIYDNIAYplksHGIKEKREIKKIVEEC----------LRKVGLwkevYDRLNSPASQLSGGQQQRLTIA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 585044696 155 VLFSTKANMLILDEPTNFLDIKTLEALEMFMN--KYPGIILFTSHDTRFVKHVSD 207
Cdd:PRK14246 166 RALALKPKVLLMDEPTSMIDIVNSQAIEKLITelKNEIAIVIVSHNPQQVARVAD 220
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
27-197 |
7.15e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 48.31 E-value: 7.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 27 HNNYPIIA-QNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLE---AIYHQIEG---IDCSPKVQMAYYRQLA 99
Cdd:PRK13543 6 HTAPPLLAaHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRvlaGLLHVESGqiqIDGKTATRGDRSRFMA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 100 Y--------EDMRDVSLLQYLMD----ETDSSESFSRAILNNLGLNEALDRScnvLSGGERTKLSLAVLFSTKANMLILD 167
Cdd:PRK13543 86 YlghlpglkADLSTLENLHFLCGlhgrRAKQMPGSALAIVGLAGYEDTLVRQ---LSAGQKKRLALARLWLSPAPLWLLD 162
|
170 180 190
....*....|....*....|....*....|...
gi 585044696 168 EPTNFLDIKTLEALEMFMNKY---PGIILFTSH 197
Cdd:PRK13543 163 EPYANLDLEGITLVNRMISAHlrgGGAALVTTH 195
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
50-170 |
8.84e-07 |
|
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: 47.81 E-value: 8.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 50 VRFQIPYGKNIALVGANGVGKTTLLEAIY----------------------HQI--EGIDCSPK-------------VQM 92
Cdd:cd03224 19 VSLTVPEGEIVALLGRNGAGKTTLLKTIMgllpprsgsirfdgrditglppHERarAGIGYVPEgrrifpeltveenLLL 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 585044696 93 AYYRqlayedmRDVSLLQYLMDETdsSESFSRailnnlgLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPT 170
Cdd:cd03224 99 GAYA-------RRRAKRKARLERV--YELFPR-------LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
47-186 |
1.07e-06 |
|
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: 47.85 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 47 LTQVRFQIPYGKNIALVGANGVGKTTLLEAIY--------------HQIEGIDCSPKVQMAYYRQLAYEDMRDVSLLQYL 112
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISglaqptsggvilegKQITEPGPDRMVVFQNYSLLPWLTVRENIALAVD 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 585044696 113 MDETDSSESFSRAILNN----LGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTLEAL-EMFMN 186
Cdd:TIGR01184 81 RVLPDLSKSERRAIVEEhialVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLqEELMQ 159
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
35-205 |
1.13e-06 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 47.64 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 35 QNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQ-----------IEGIDCS---------------- 87
Cdd:TIGR01978 4 KDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGHpsyevtsgtilFKGQDLLelepderaraglflaf 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 88 ------PKVQMAYYRQLAYEDMR------DVSLLQYlmdetdssESFSRAILNNLGLNEA-LDRSCNV-LSGGERTK--- 150
Cdd:TIGR01978 84 qypeeiPGVSNLEFLRSALNARRsargeePLDLLDF--------EKLLKEKLALLDMDEEfLNRSVNEgFSGGEKKRnei 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 585044696 151 LSLAVLfstKANMLILDEPTNFLDIKTL----EALEMFMNKYPGIILFTsHDTRFVKHV 205
Cdd:TIGR01978 156 LQMALL---EPKLAILDEIDSGLDIDALkivaEGINRLREPDRSFLIIT-HYQRLLNYI 210
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
29-202 |
1.15e-06 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 47.81 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 29 NYPIIAQNLTLV-KGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLL---EAIYH------QIEGIDCSPKVQMAYYRQ- 97
Cdd:PRK13647 2 DNIIEVEDLHFRyKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLlhlNGIYLpqrgrvKVMGREVNAENEKWVRSKv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 98 -LAYEDMRDVSLLQYLMDET-----------DSSESFSRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLI 165
Cdd:PRK13647 82 gLVFQDPDDQVFSSTVWDDVafgpvnmgldkDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 585044696 166 LDEPTNFLDIK----TLEALEMFMNKYPGIILFTsHDTRFV 202
Cdd:PRK13647 162 LDEPMAYLDPRgqetLMEILDRLHNQGKTVIVAT-HDVDLA 201
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
32-198 |
1.23e-06 |
|
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: 47.36 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLL------------EAIyhqIEGID--CSPK-------- 89
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIkmlttllkptsgRAT---VAGHDvvREPRevrrrigi 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 90 --VQMAYYRQL-AYEDMrdvsLLQYLMDETDSSESFSRA--ILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANML 164
Cdd:cd03265 78 vfQDLSVDDELtGWENL----YIHARLYGVPGAERRERIdeLLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 585044696 165 ILDEPTNFLDIKTLEALEMF---MNKYPGI-ILFTSHD 198
Cdd:cd03265 154 FLDEPTIGLDPQTRAHVWEYiekLKEEFGMtILLTTHY 191
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
37-181 |
1.70e-06 |
|
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: 46.55 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 37 LTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEaiyhqiEGIDCSPKVQMAYYRQLAYEDMR-DVSLLQYLMDe 115
Cdd:cd03238 1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVN------EGLYASGKARLISFLPKFSRNKLiFIDQLQFLID- 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 585044696 116 tdssesfsrailnnLGLNE-ALDRSCNVLSGGERTKLSLAV-LFSTKANML-ILDEPTNFLDIKTLEAL 181
Cdd:cd03238 74 --------------VGLGYlTLGQKLSTLSGGELQRVKLASeLFSEPPGTLfILDEPSTGLHQQDINQL 128
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
35-202 |
2.15e-06 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 47.03 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 35 QNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQIE----GIDCSPKVQMAYYRQLAYEDMR---DVS 107
Cdd:PRK09544 8 ENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVApdegVIKRNGKLRIGYVPQKLYLDTTlplTVN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 108 LLQYLMDETDSSEsfsraILNNLGLNEA---LDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTLEAL--- 181
Cdd:PRK09544 88 RFLRLRPGTKKED-----ILPALKRVQAghlIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALydl 162
|
170 180
....*....|....*....|..
gi 585044696 182 -EMFMNKYPGIILFTSHDTRFV 202
Cdd:PRK09544 163 iDQLRRELDCAVLMVSHDLHLV 184
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
29-203 |
2.58e-06 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 47.39 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 29 NYPIIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTT----LLEAIYHQIE-GIDCSP-----KVQMAYYR-- 96
Cdd:PRK15134 284 AFPIRKGILKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQGEiWFDGQPlhnlnRRQLLPVRhr 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 97 -QLAYEDMRD-----VSLLQYLMD---------ETDSSESFSRAILNNLGLN-EALDRSCNVLSGGERTKLSLAVLFSTK 160
Cdd:PRK15134 364 iQVVFQDPNSslnprLNVLQIIEEglrvhqptlSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILK 443
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 585044696 161 ANMLILDEPTNFLDiKTLEA-----LEMFMNKYPGIILFTSHDTRFVK 203
Cdd:PRK15134 444 PSLIILDEPTSSLD-KTVQAqilalLKSLQQKHQLAYLFISHDLHVVR 490
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
34-208 |
3.12e-06 |
|
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: 45.50 E-value: 3.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 34 AQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI---YHQIEGidcspkvqmayyrqlayedmrdvsllQ 110
Cdd:cd03216 3 LRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILsglYKPDSG--------------------------E 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 111 YLMDETDssesfsraiLNNLGLNEALDRSCNV---LSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTLEALEMFMN- 186
Cdd:cd03216 57 ILVDGKE---------VSFASPRDARRAGIAMvyqLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRr 127
|
170 180
....*....|....*....|....
gi 585044696 187 -KYPGI-ILFTSHDTRFVKHVSDK 208
Cdd:cd03216 128 lRAQGVaVIFISHRLDEVFEIADR 151
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
25-207 |
3.29e-06 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 46.88 E-value: 3.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 25 DIHNNYPIiAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTL---LEAIYH------QIEGIDCS-------- 87
Cdd:PRK11308 10 DLKKHYPV-KRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLarlLTMIETptggelYYQGQDLLkadpeaqk 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 88 ---PKVQMAYyrQLAYEDM---RDVS--LLQYLMDETDSSESFSR----AILNNLGLN-EALDRSCNVLSGGERTKLSLA 154
Cdd:PRK11308 89 llrQKIQIVF--QNPYGSLnprKKVGqiLEEPLLINTSLSAAERRekalAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 585044696 155 vlfstKANML-----ILDEPTNFLDIkTLEA--LEMFMN-------KYpgiiLFTSHDTRFVKHVSD 207
Cdd:PRK11308 167 -----RALMLdpdvvVADEPVSALDV-SVQAqvLNLMMDlqqelglSY----VFISHDLSVVEHIAD 223
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
42-174 |
3.43e-06 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 46.24 E-value: 3.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 42 GSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIyHQIEGIDC-----------SPKVQMAYYRQLAYEDMRDVSLLQ 110
Cdd:PRK09493 12 GPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCI-NKLEEITSgdlivdglkvnDPKVDERLIRQEAGMVFQQFYLFP 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 585044696 111 YL---------------MDETDSsESFSRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLD 174
Cdd:PRK09493 91 HLtalenvmfgplrvrgASKEEA-EKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
32-208 |
3.88e-06 |
|
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: 46.72 E-value: 3.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLL--------------EAIYH------------------ 79
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMhvlrgmdqyeptsgRIIYHvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 80 ------------QIEGIDCSPKVQMAYYRQLA---------YEDMRD-VSLLQYLMD-ETDSSESFSRAI--LNNLGLNE 134
Cdd:TIGR03269 81 pcpvcggtlepeEVDFWNLSDKLRRRIRKRIAimlqrtfalYGDDTVlDNVLEALEEiGYEGKEAVGRAVdlIEMVQLSH 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 585044696 135 ALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTL----EALEMFMNKYPGIILFTSHDTRFVKHVSDK 208
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAklvhNALEEAVKASGISMVLTSHWPEVIEDLSDK 238
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
35-177 |
5.78e-06 |
|
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: 45.64 E-value: 5.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 35 QNLTLV-KGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLE-----------AIYHQIEGI-DCSPKVQMAYYRQLAY- 100
Cdd:cd03256 4 ENLSKTyPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRclnglveptsgSVLIDGTDInKLKGKALRQLRRQIGMi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 101 -EDMRDV---SLLQYLMDETDSSESFSRAILNNLGLNE------ALDRS---------CNVLSGGERTKLSLAVLFSTKA 161
Cdd:cd03256 84 fQQFNLIerlSVLENVLSGRLGRRSTWRSLFGLFPKEEkqralaALERVglldkayqrADQLSGGQQQRVAIARALMQQP 163
|
170
....*....|....*.
gi 585044696 162 NMLILDEPTNFLDIKT 177
Cdd:cd03256 164 KLILADEPVASLDPAS 179
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
45-183 |
6.33e-06 |
|
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: 45.33 E-value: 6.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 45 KLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI------YHQIEGI---DCSPKVQMA--YYRQLAYEDMRDVSLLQYLM 113
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALanrtegNVSVEGDihyNGIPYKEFAekYPGEIIYVSEEDVHFPTLTV 100
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 114 DETdssESFSRAILNNlglnealdRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTleALEM 183
Cdd:cd03233 101 RET---LDFALRCKGN--------EFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST--ALEI 157
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-208 |
7.40e-06 |
|
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: 45.95 E-value: 7.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 1 MEHLEEVEKPQSYhEFNFPQNKIYDIHNNYpiiaqnLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIyhq 80
Cdd:TIGR03269 261 MEGVSEVEKECEV-EVGEPIIKVRNVSKRY------ISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKII--- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 81 iegIDCSPKVQMAYYRQLAYE--DMRDVSLL------QYL-MDETDSSESFSRAILNNL----GLN-------------- 133
Cdd:TIGR03269 331 ---AGVLEPTSGEVNVRVGDEwvDMTKPGPDgrgrakRYIgILHQEYDLYPHRTVLDNLteaiGLElpdelarmkavitl 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 134 -----------EALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLD-IKTLEALEMFMNKYPGI---ILFTSHD 198
Cdd:TIGR03269 408 kmvgfdeekaeEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDpITKVDVTHSILKAREEMeqtFIIVSHD 487
|
250
....*....|
gi 585044696 199 TRFVKHVSDK 208
Cdd:TIGR03269 488 MDFVLDVCDR 497
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
31-183 |
7.47e-06 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 45.44 E-value: 7.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 31 PIIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAiyhqIEGIDCSPKVQM-AYYRQL--AYEDMR--- 104
Cdd:PRK11247 12 PLLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRL----LAGLETPSAGELlAGTAPLaeAREDTRlmf 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 105 -DVSLLQYlmdetdssesfsRAILNNLGLN----------EAL------DRSCN---VLSGGERTKLSLAVLFSTKANML 164
Cdd:PRK11247 88 qDARLLPW------------KKVIDNVGLGlkgqwrdaalQALaavglaDRANEwpaALSGGQKQRVALARALIHRPGLL 155
|
170
....*....|....*....
gi 585044696 165 ILDEPTNFLDikTLEALEM 183
Cdd:PRK11247 156 LLDEPLGALD--ALTRIEM 172
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
42-206 |
8.15e-06 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 45.35 E-value: 8.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 42 GSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLE-----------AIYHQIEGI----DCSPKVQMAYYRQLAYEDMR-- 104
Cdd:PRK10619 16 GEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRcinflekpsegSIVVNGQTInlvrDKDGQLKVADKNQLRLLRTRlt 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 105 ----------DVSLLQYLMDET------DSSESFSRAI--LNNLGLNEALDRSCNV-LSGGERTKLSLAVLFSTKANMLI 165
Cdd:PRK10619 96 mvfqhfnlwsHMTVLENVMEAPiqvlglSKQEARERAVkyLAKVGIDERAQGKYPVhLSGGQQQRVSIARALAMEPEVLL 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 585044696 166 LDEPTNFLDIKTLEALEMFMNKYP---GIILFTSHDTRFVKHVS 206
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQLAeegKTMVVVTHEMGFARHVS 219
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
31-200 |
9.64e-06 |
|
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: 45.12 E-value: 9.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 31 PII-AQNLTL-VKGSQKLLT---QVRFQIPYGKNIALVGANGVGKTTLLeAIyhqIEGIDC--SPKVQMAYYR--QLAyE 101
Cdd:COG4181 7 PIIeLRGLTKtVGTGAGELTilkGISLEVEAGESVAIVGASGSGKSTLL-GL---LAGLDRptSGTVRLAGQDlfALD-E 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 102 DMR-------------------DVSLLQYLM---DETDSSESFSRA--ILNNLGLNEALDRSCNVLSGGERTKLSLAVLF 157
Cdd:COG4181 82 DARarlrarhvgfvfqsfqllpTLTALENVMlplELAGRRDARARAraLLERVGLGHRLDHYPAQLSGGEQQRVALARAF 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 585044696 158 STKANMLILDEPTNFLDIKTLEALE--MF-MNKYPGIILF-TSHDTR 200
Cdd:COG4181 162 ATEPAILFADEPTGNLDAATGEQIIdlLFeLNRERGTTLVlVTHDPA 208
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-197 |
9.70e-06 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 45.59 E-value: 9.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 25 DIHNNYPiiaqnltlvKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI---YHQIEGIDCSPKVQMAYYRQLAYE 101
Cdd:PRK11160 343 NVSFTYP---------DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLtraWDPQQGEILLNGQPIADYSEAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 102 DM---------------RDvSLLqyLMDETDSSESFSrAILNNLGL------NEALD-------RScnvLSGGERTKLSL 153
Cdd:PRK11160 414 QAisvvsqrvhlfsatlRD-NLL--LAAPNASDEALI-EVLQQVGLeklledDKGLNawlgeggRQ---LSGGEQRRLGI 486
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 585044696 154 AVLFSTKANMLILDEPTNFLDIKT----LEALEMFM-NKypgIILFTSH 197
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETerqiLELLAEHAqNK---TVLMITH 532
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
41-174 |
9.72e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.88 E-value: 9.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 41 KGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQI---EGIDCSPKVQMAYYRQLA------------------ 99
Cdd:PLN03130 627 KAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELpprSDASVVIRGTVAYVPQVSwifnatvrdnilfgspfd 706
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 585044696 100 ---YEDMRDVSLLQYLMDetdssesfsraILNNLGLNEALDRSCNVlSGGERTKLSLAVLFSTKANMLILDEPTNFLD 174
Cdd:PLN03130 707 perYERAIDVTALQHDLD-----------LLPGGDLTEIGERGVNI-SGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
42-218 |
1.26e-05 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 44.48 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 42 GSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYhqieGIDcSPKVQMAYY--RQLAYEDMRDVSLLQ--------- 110
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLIC----GIE-RPSAGKIWFsgHDITRLKNREVPFLRrqigmifqd 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 111 --YLMDET-------------DSSESFSR---AILNNLGLneaLDRSCNV---LSGGERTKLSLAVLFSTKANMLILDEP 169
Cdd:PRK10908 88 hhLLMDRTvydnvaipliiagASGDDIRRrvsAALDKVGL---LDKAKNFpiqLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 585044696 170 TNFLDIKTLEA-LEMF--MNKYPGIILFTSHDTRFVKHVSDKKWELTGQSLH 218
Cdd:PRK10908 165 TGNLDDALSEGiLRLFeeFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
47-177 |
1.26e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 44.87 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 47 LTQVRFQIPYGKNIALVGANGVGKTTLLEAIYH---------QIEGIDCSPKVQ---MAYYRQLAYED------MRDVSL 108
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGfvrlasgkiSILGQPTRQALQknlVAYVPQSEEVDwsfpvlVEDVVM 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 585044696 109 ------LQYLMDETDSSESFSRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKT 177
Cdd:PRK15056 103 mgryghMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
42-208 |
1.63e-05 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 44.69 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 42 GSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIY---HQ------IEGIDCSP------KV-----QMAYYRQLAYE 101
Cdd:PRK10851 13 GRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAgleHQtsghirFHGTDVSRlhardrKVgfvfqHYALFRHMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 102 DMRDVSLLQYLMDETDSSESFSR---AILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTL 178
Cdd:PRK10851 93 DNIAFGLTVLPRRERPNAAAIKAkvtQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQVR 172
|
170 180 190
....*....|....*....|....*....|....
gi 585044696 179 EALEMFMNKYPGIILFTS----HDTRFVKHVSDK 208
Cdd:PRK10851 173 KELRRWLRQLHEELKFTSvfvtHDQEEAMEVADR 206
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
45-177 |
1.65e-05 |
|
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: 43.94 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 45 KLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQIEGIDCSPKVQMAYYRQLAYEDMRDvSLLQYLMDETdsseSFSR 124
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRS-SLTIIPQDPT----LFSG 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 585044696 125 AILNNLG-LNEALDR----------SCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKT 177
Cdd:cd03369 97 TIRSNLDpFDEYSDEeiygalrvseGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
25-174 |
1.94e-05 |
|
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: 44.07 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 25 DIHNNYP-----IIAQNLTLVkgsqklltqvrfqIPYGKNIALVGANGVGKTT---LLEAIYHQIEG---IDcspkvqma 93
Cdd:cd03249 5 NVSFRYPsrpdvPILKGLSLT-------------IPPGKTVALVGSSGCGKSTvvsLLERFYDPTSGeilLD-------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 94 yyrqlaYEDMRDVSlLQYLMDETD--SSES--FSRAILNN--LGLNEALD-------RSCNV------------------ 142
Cdd:cd03249 64 ------GVDIRDLN-LRWLRSQIGlvSQEPvlFDGTIAENirYGKPDATDeeveeaaKKANIhdfimslpdgydtlvger 136
|
170 180 190
....*....|....*....|....*....|....*
gi 585044696 143 ---LSGGERTKLSLAVLFSTKANMLILDEPTNFLD 174
Cdd:cd03249 137 gsqLSGGQKQRIAIARALLRNPKILLLDEATSALD 171
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
47-182 |
2.04e-05 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 44.62 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 47 LTQVRFQIPYGKNIALVGANGVGKTT---LLEAIYH------QIEGID---------------CSPKVQM---------A 93
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTianLLTRFYDidegeiLLDGHDlrdytlaslrnqvalVSQNVHLfndtianniA 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 94 YYRQLAY--EDMRDVSLLQYLMDETDSSESfsrailnnlGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTN 171
Cdd:PRK11176 439 YARTEQYsrEQIEEAARMAYAMDFINKMDN---------GLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEATS 509
|
170
....*....|.
gi 585044696 172 FLDIKTLEALE 182
Cdd:PRK11176 510 ALDTESERAIQ 520
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
15-197 |
2.32e-05 |
|
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: 44.73 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 15 EFNFPQNKIYDIHNNYPIIAQNLTLVKG-SQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIY--------------H 79
Cdd:TIGR01193 457 EFINKKKRTELNNLNGDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVgffqarsgeillngF 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 80 QIEGIDCSPKVQ-MAYYRQLAYedMRDVSLLQYLM---------DETDSSESFS--RAILNN--LGLNEALDRSCNVLSG 145
Cdd:TIGR01193 537 SLKDIDRHTLRQfINYLPQEPY--IFSGSILENLLlgakenvsqDEIWAACEIAeiKDDIENmpLGYQTELSEEGSSISG 614
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 585044696 146 GERTKLSLAVLFSTKANMLILDEPTNFLDIKTLEA-LEMFMNKYPGIILFTSH 197
Cdd:TIGR01193 615 GQKQRIALARALLTDSKVLILDESTSNLDTITEKKiVNNLLNLQDKTIIFVAH 667
|
|
| RecF |
COG1195 |
Recombinational DNA repair ATPase RecF [Replication, recombination and repair]; |
47-78 |
2.55e-05 |
|
Recombinational DNA repair ATPase RecF [Replication, recombination and repair];
Pssm-ID: 440808 [Multi-domain] Cd Length: 352 Bit Score: 43.99 E-value: 2.55e-05
10 20 30
....*....|....*....|....*....|..
gi 585044696 47 LTQVRFQIPYGKNIaLVGANGVGKTTLLEAIY 78
Cdd:COG1195 13 YESLELEFSPGINV-LVGPNGQGKTNLLEAIY 43
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
137-198 |
2.84e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 44.28 E-value: 2.84e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 585044696 137 DRSCNVLSGGERTKLSLA------VLFSTKANMLILDEPTNFLD----IKTLEALEMFMNKYPGIILfTSHD 198
Cdd:PRK03918 783 ERPLTFLSGGERIALGLAfrlalsLYLAGNIPLLILDEPTPFLDeerrRKLVDIMERYLRKIPQVII-VSHD 853
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
125-197 |
3.13e-05 |
|
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: 44.62 E-value: 3.13e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 585044696 125 AILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTLEALEMFMNKYPG---IILFTSH 197
Cdd:TIGR01257 1044 AMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSgrtIIMSTHH 1119
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
32-176 |
3.26e-05 |
|
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: 43.40 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI-----------YhqIEGIDCS---PK---VQMA- 93
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIagleeptsgriY--IGGRDVTdlpPKdrdIAMVf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 94 -----YYRQLAYEDMRdVSLLQYLMDETDSSESFSRAIlNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDE 168
Cdd:cd03301 79 qnyalYPHMTVYDNIA-FGLKLRKVPKDEIDERVREVA-ELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
....*...
gi 585044696 169 PTNFLDIK 176
Cdd:cd03301 157 PLSNLDAK 164
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
35-215 |
3.75e-05 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 43.60 E-value: 3.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 35 QNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQI-----------EGI---------DCSPKVQMAY 94
Cdd:PRK11831 11 RGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIapdhgeilfdgENIpamsrsrlyTVRKRMSMLF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 95 YRQLAYEDMRDVSLLQY-LMDETDSSESFSRAI----LNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEP 169
Cdd:PRK11831 91 QSGALFTDMNVFDNVAYpLREHTQLPAPLLHSTvmmkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 585044696 170 TNFLDIKTLEALEMF---MNKYPGII-LFTSHDTRFVKHVSDKKWELTGQ 215
Cdd:PRK11831 171 FVGQDPITMGVLVKLiseLNSALGVTcVVVSHDVPEVLSIADHAYIVADK 220
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
47-77 |
5.82e-05 |
|
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: 42.66 E-value: 5.82e-05
10 20 30
....*....|....*....|....*....|.
gi 585044696 47 LTQVRFQIPYGKNIALVGANGVGKTTLLEAI 77
Cdd:COG0410 19 LHGVSLEVEEGEIVALLGRNGAGKTTLLKAI 49
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
34-177 |
5.93e-05 |
|
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: 42.03 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 34 AQNLTlVKGSqklLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQ---------IEGIDCSPK-VQMAYYRQLAY--E 101
Cdd:cd03215 7 VRGLS-VKGA---VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLrppasgeitLDGKPVTRRsPRDAIRAGIAYvpE 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 585044696 102 DMRDVSLLQylmdetdssesfSRAILNNLGLNealdrscNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKT 177
Cdd:cd03215 83 DRKREGLVL------------DLSVAENIALS-------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
42-174 |
6.48e-05 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 43.17 E-value: 6.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 42 GSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLeaiyhQIEGidCSPKVQMAYYR------------QLA---------- 99
Cdd:PRK10535 19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLM-----NILG--CLDKPTSGTYRvagqdvatldadALAqlrrehfgfi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 100 ---YEDMRDVSLLQ-------YLMDETDSSESFSRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEP 169
Cdd:PRK10535 92 fqrYHLLSHLTAAQnvevpavYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEP 171
|
....*
gi 585044696 170 TNFLD 174
Cdd:PRK10535 172 TGALD 176
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
47-184 |
6.68e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 42.70 E-value: 6.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 47 LTQVRFQIPYGKNIALVGANGVGKTTLLE---AIYHQIEG-IDCSPKVQMAYYRQLAYEDMRD-VSLL-QY----LMDET 116
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQhlnGLLQPTSGtVTIGERVITAGKKNKKLKPLRKkVGIVfQFpehqLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 117 ----------------DSSESFSRAILNNLGLNEA-LDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIK-TL 178
Cdd:PRK13634 103 vekdicfgpmnfgvseEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKgRK 182
|
....*.
gi 585044696 179 EALEMF 184
Cdd:PRK13634 183 EMMEMF 188
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
143-207 |
7.70e-05 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 43.16 E-value: 7.70e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 585044696 143 LSGGERTKLSLAVLFSTKANMLILDEPTNFLDIkTLEAL----------EMFMNkypgiILFTSHDTRFVKHVSD 207
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDV-SVQAQilqllrelqqELNMG-----LLFITHNLSIVRKLAD 225
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
25-208 |
7.84e-05 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 42.37 E-value: 7.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 25 DIHNNYPiiaqnltlvKGSQkLLTQVRFQIPYGKNIALVGANGVGKTTL---LEAIYHQIEG----------------ID 85
Cdd:PRK13639 6 DLKYSYP---------DGTE-ALKGINFKAEKGEMVALLGPNGAGKSTLflhFNGILKPTSGevlikgepikydkkslLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 86 CSPKVQMAYYR---QL-AYEDMRDVSL----LQYLMDETdssESFSRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLF 157
Cdd:PRK13639 76 VRKTVGIVFQNpddQLfAPTVEEDVAFgplnLGLSKEEV---EKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 585044696 158 STKANMLILDEPTNFLD----IKTLEALEMfMNKYPGIILFTSHDTRFVKHVSDK 208
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDpmgaSQIMKLLYD-LNKEGITIIISTHDVDLVPVYADK 206
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
47-208 |
9.14e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 42.85 E-value: 9.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 47 LTQVRFQIPYGKNIALVGANGVGKTTL---LEAIYH------QIEGIDCS---PKVQMAY-----YRQLAYEDmrDVSLL 109
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLmkvLSGIHEptkgtiTINNINYNkldHKLAAQLgigiiYQELSVID--ELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 110 QYL------------MDETDSSESFSRA--ILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDI 175
Cdd:PRK09700 99 ENLyigrhltkkvcgVNIIDWREMRVRAamMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTN 178
|
170 180 190
....*....|....*....|....*....|....*.
gi 585044696 176 KTLEALEMFMNKYPG---IILFTSHDTRFVKHVSDK 208
Cdd:PRK09700 179 KEVDYLFLIMNQLRKegtAIVYISHKLAEIRRICDR 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
53-174 |
1.30e-04 |
|
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: 41.71 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 53 QIPYGKNIALVGANGVGKTTLLEAIYH---------QIEGID--CSP----KVQMAY-----YRQLAYEDMRDVSLLQYL 112
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNLIAGfetpqsgrvLINGVDvtAAPpadrPVSMLFqennlFAHLTVEQNVGLGLSPGL 99
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 585044696 113 -MDETDSSESfsRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLD 174
Cdd:cd03298 100 kLTAEDRQAI--EVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALD 160
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
116-198 |
1.37e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 42.00 E-value: 1.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 116 TDSSESFSRA--ILNNLGLNEA-LDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLD-IKTLEALEMFMNKYPG- 190
Cdd:PRK13651 136 VSKEEAKKRAakYIELVGLDESyLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILEIFDNLNKQg 215
|
90
....*....|
gi 585044696 191 --IILFTsHD 198
Cdd:PRK13651 216 ktIILVT-HD 224
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
43-174 |
1.69e-04 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 41.54 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 43 SQKLLTQVRFQIPYGKNIALVGANGVGKTTL---------LEAIYHQIEGIDCSP--------KVQMAYYR---QLAYED 102
Cdd:PRK13635 19 ATYALKDVSFSVYEGEWVAIVGHNGSGKSTLakllnglllPEAGTITVGGMVLSEetvwdvrrQVGMVFQNpdnQFVGAT 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 585044696 103 MRD---VSLLQYLMDETDSSESFSRAiLNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLD 174
Cdd:PRK13635 99 VQDdvaFGLENIGVPREEMVERVDQA-LRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
29-207 |
1.83e-04 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 41.37 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 29 NYPIIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEA-----------------------IYH-QIEGI 84
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTfnrllelneearvegevrlfgrnIYSpDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 85 DCSPKVQMAY-----YRQLA-YEDMRDVSLLQYLMDETDSSESFSRAILNNLGL-NEALDRSCNV---LSGGERTKLSLA 154
Cdd:PRK14267 82 EVRREVGMVFqypnpFPHLTiYDNVAIGVKLNGLVKSKKELDERVEWALKKAALwDEVKDRLNDYpsnLSGGQRQRLVIA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 585044696 155 VLFSTKANMLILDEPTNFLD---IKTLEALEMFMNKYPGIILFTsHDTRFVKHVSD 207
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDpvgTAKIEELLFELKKEYTIVLVT-HSPAQAARVSD 216
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
29-195 |
1.89e-04 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 41.17 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 29 NYPIIA-QNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI-----YHQIEG---------IDCSPK---- 89
Cdd:CHL00131 4 NKPILEiKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghpaYKILEGdilfkgesiLDLEPEerah 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 90 ---------------VQMAYYRQLAYEDMRDvsllQYLMDETDSSESFS--RAILNNLGLNEA-LDRSCNV-LSGGERTK 150
Cdd:CHL00131 84 lgiflafqypieipgVSNADFLRLAYNSKRK----FQGLPELDPLEFLEiiNEKLKLVGMDPSfLSRNVNEgFSGGEKKR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 585044696 151 ---LSLAVLFSTKAnmlILDEPTNFLDIKTL----EALEMFMNKYPGIILFT 195
Cdd:CHL00131 160 neiLQMALLDSELA---ILDETDSGLDIDALkiiaEGINKLMTSENSIILIT 208
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
136-208 |
2.19e-04 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 41.76 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 136 LDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLD----------IKTLEAlEMFMnkypGIIlFTSHDTRFVKHV 205
Cdd:PRK10261 162 LSRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDvtiqaqilqlIKVLQK-EMSM----GVI-FITHDMGVVAEI 235
|
...
gi 585044696 206 SDK 208
Cdd:PRK10261 236 ADR 238
|
|
| recF |
PRK00064 |
recombination protein F; Reviewed |
57-78 |
2.43e-04 |
|
recombination protein F; Reviewed
Pssm-ID: 234608 [Multi-domain] Cd Length: 361 Bit Score: 41.30 E-value: 2.43e-04
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
43-184 |
2.67e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 40.87 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 43 SQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI-----------------------YHQIEGIDCSPKVQMAYYRQLA 99
Cdd:PRK13643 18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLngllqptegkvtvgdivvsstskQKEIKPVRKKVGVVFQFPESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 100 YED--MRDVSL-LQYLMDETDSSESFSRAILNNLGLN-EALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDI 175
Cdd:PRK13643 98 FEEtvLKDVAFgPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170
....*....|
gi 585044696 176 KT-LEALEMF 184
Cdd:PRK13643 178 KArIEMMQLF 187
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
134-208 |
2.86e-04 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 40.76 E-value: 2.86e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 585044696 134 EALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTLEA-LEMF--MNK-YPGIILFTSHDTRFVKHVSDK 208
Cdd:PRK13645 142 DYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDfINLFerLNKeYKKRIIMVTHNMDQVLRIADE 220
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
50-168 |
3.18e-04 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 41.11 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 50 VRFQIPYGKNIALVGANGVGKTT---LLEAIYHQIEG---IDCSP--KVQMAYYRQLAYEDMRDVSLLQYLMDE--TDSS 119
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTlamLLTGLYQPQSGeilLDGKPvtAEQPEDYRKLFSAVFTDFHLFDQLLGPegKPAN 421
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 585044696 120 ESFSRAILNNLGLNEALD----RSCNV-LSGGERTKLSLAVLFSTKANMLILDE 168
Cdd:PRK10522 422 PALVEKWLERLKMAHKLEledgRISNLkLSKGQKKRLALLLALAEERDILLLDE 475
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
42-182 |
3.64e-04 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 40.45 E-value: 3.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 42 GSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYH---------QIEGIDCS-PKVQMAYYRQ----LAYEDMRD-V 106
Cdd:PRK11248 12 GGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGfvpyqhgsiTLDGKPVEgPGAERGVVFQneglLPWRNVQDnV 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 585044696 107 SL-LQYLMDETDSSESFSRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTLEALE 182
Cdd:PRK11248 92 AFgLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQMQ 168
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
52-174 |
3.68e-04 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 40.34 E-value: 3.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 52 FQIPYGKNIALVGANGVGKTTLLEAIYH---------QIEGIDC--SPKVQmayyrqlayedmRDVSLL-------QYLM 113
Cdd:PRK10771 20 LTVERGERVAILGPSGAGKSTLLNLIAGfltpasgslTLNGQDHttTPPSR------------RPVSMLfqennlfSHLT 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 585044696 114 DE-------------TDSSESFSRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLD 174
Cdd:PRK10771 88 VAqniglglnpglklNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALD 161
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
127-176 |
4.08e-04 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 40.60 E-value: 4.08e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 585044696 127 LNNLGLNEA-LDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIK 176
Cdd:PRK13631 160 LNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPK 210
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
34-198 |
4.08e-04 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 40.48 E-value: 4.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 34 AQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYhQI----EG--------IDCSPKVQMAYY---RQL 98
Cdd:COG4152 4 LKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIIL-GIlapdSGevlwdgepLDPEDRRRIGYLpeeRGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 99 aYEDMRDVSLLQYL-----MDETDSSESfSRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFL 173
Cdd:COG4152 83 -YPKMKVGEQLVYLarlkgLSKAEAKRR-ADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGL 160
|
170 180 190
....*....|....*....|....*....|.
gi 585044696 174 DIktlEALEMFMN-----KYPG-IILFTSHD 198
Cdd:COG4152 161 DP---VNVELLKDvirelAAKGtTVIFSSHQ 188
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
46-205 |
5.36e-04 |
|
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: 39.76 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 46 LLTQVRFQIPYGKNIALVGANGVGKTTLLEAI---YHQIEGIDCSPKvQMAYYRQLAY---EDMRDVSLLQYLMDEtdss 119
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALlgeLEKLSGSVSVPG-SIAYVSQEPWiqnGTIRENILFGKPFDE---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 120 ESFSRAI--------LNNL-----------GLNealdrscnvLSGGERTKLSLA-VLFStKANMLILDEPTNFLDIKTLE 179
Cdd:cd03250 95 ERYEKVIkacalepdLEILpdgdlteigekGIN---------LSGGQKQRISLArAVYS-DADIYLLDDPLSAVDAHVGR 164
|
170 180 190
....*....|....*....|....*....|...
gi 585044696 180 AL-------EMFMNKypGIILFTsHDTRFVKHV 205
Cdd:cd03250 165 HIfencilgLLLNNK--TRILVT-HQLQLLPHA 194
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
60-181 |
5.71e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 39.61 E-value: 5.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 60 IALVGANGVGKTTLLEAIYH---------------------------------------------QIEGIDCSPKVQMAY 94
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIRYalygkarsrsklrsdlinvgseeasvelefehggkryrierrqgeFAEFLEAKPSERKEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 95 YRQL----AYEDMRDV-----SLLQYLMDETDSSESFSRAILNNLGLNEALDRscnvLSGGERTKLSLAVLFStkanmLI 165
Cdd:COG0419 106 LKRLlgleIYEELKERlkeleEALESALEELAELQKLKQEILAQLSGLDPIET----LSGGERLRLALADLLS-----LI 176
|
170
....*....|....*.
gi 585044696 166 LDepTNFLDIKTLEAL 181
Cdd:COG0419 177 LD--FGSLDEERLERL 190
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
57-197 |
5.76e-04 |
|
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: 40.77 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 57 GKNIALVGANGVGKTTLLEAIYHQIEGIDCSPKV--------------QMAYYRQL-AYEDMRDVSLLQYLMDE-----T 116
Cdd:TIGR01257 1965 GECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVagksiltnisdvhqNMGYCPQFdAIDDLLTGREHLYLYARlrgvpA 2044
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 117 DSSESFSRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIktlEALEMFMNKYPGII---- 192
Cdd:TIGR01257 2045 EEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP---QARRMLWNTIVSIIregr 2121
|
....*..
gi 585044696 193 --LFTSH 197
Cdd:TIGR01257 2122 avVLTSH 2128
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
49-175 |
6.31e-04 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 39.86 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 49 QVRFQIPyGKNI-ALVGANGVGKTTLLEAI---------YHQIEG---IDCSPKVQMA-YYRQLAY--EDMRdvsL---- 108
Cdd:PRK11144 16 TVNLTLP-AQGItAIFGRSGAGKTSLINAIsgltrpqkgRIVLNGrvlFDAEKGICLPpEKRRIGYvfQDAR---Lfphy 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 585044696 109 -----LQYLMDETDSSEsFSRaILNNLGLNEALDRSCNVLSGGE--RTKLSLAVLfsTKANMLILDEPTNFLDI 175
Cdd:PRK11144 92 kvrgnLRYGMAKSMVAQ-FDK-IVALLGIEPLLDRYPGSLSGGEkqRVAIGRALL--TAPELLLMDEPLASLDL 161
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
32-177 |
8.38e-04 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 39.30 E-value: 8.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLV----KGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI---YHQIEG-IDCSPKVQMAYYRQLAY--- 100
Cdd:COG1116 8 LELRGVSKRfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIaglEKPTSGeVLVDGKPVTGPGPDRGVvfq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 101 EDmrdvSLLQYL-----------MDETDSSESFSRA--ILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILD 167
Cdd:COG1116 88 EP----ALLPWLtvldnvalgleLRGVPKAERRERAreLLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMD 163
|
170
....*....|..
gi 585044696 168 EPtnF--LDIKT 177
Cdd:COG1116 164 EP--FgaLDALT 173
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
32-169 |
8.55e-04 |
|
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: 39.06 E-value: 8.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTL------LE-----AIYhqIEGIDCSpKVQMaYYRQ--- 97
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTfymivgLVkpdsgKIL--LDGQDIT-KLPM-HKRArlg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 98 ---LAYED--MRDVSLLQYLM-------DETDSSESFSRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLI 165
Cdd:cd03218 77 igyLPQEAsiFRKLTVEENILavleirgLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
....
gi 585044696 166 LDEP 169
Cdd:cd03218 157 LDEP 160
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
42-170 |
9.15e-04 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 39.09 E-value: 9.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 42 GSQKLLTQVRFQIPYGKNIALVGANGVGKTTLL-------EAIYHQI-----------------EGIDCSPKVQMAYYRQ 97
Cdd:PRK11614 16 GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLgtlcgdpRATSGRIvfdgkditdwqtakimrEAVAIVPEGRRVFSRM 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 585044696 98 LAYEDMrdvSLLQYLMDETDSSESFSRAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPT 170
Cdd:PRK11614 96 TVEENL---AMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPS 165
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
74-202 |
9.23e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 39.64 E-value: 9.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 74 LEAIYHQIEGIDcspkvqmAYYRQLAYE-DMRDVSLLQYLMDETDS----SESFSRAILN---NLGL----NEALDRScn 141
Cdd:PRK02224 710 LEALYDEAEELE-------SMYGDLRAElRQRNVETLERMLNETFDlvyqNDAYSHIELDgeyELTVyqkdGEPLEPE-- 780
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 585044696 142 VLSGGERT--KLSL--------AVLFSTKANM--LILDEPTNFLD----IKTLEALEMFMNKYPGIILFTSHDTRFV 202
Cdd:PRK02224 781 QLSGGERAlfNLSLrcaiyrllAEGIEGDAPLppLILDEPTVFLDsghvSQLVDLVESMRRLGVEQIVVVSHDDELV 857
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
43-174 |
9.69e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 39.76 E-value: 9.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 43 SQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQIEgidcspkVQ---------MAYYRQLAY---EDMRDVSLlq 110
Cdd:PTZ00243 672 PKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFE-------ISegrvwaersIAYVPQQAWimnATVRGNIL-- 742
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 585044696 111 yLMDETDSSE-------SFSRAILNNL--GL-NEALDRSCNvLSGGERTKLSLAVLFSTKANMLILDEPTNFLD 174
Cdd:PTZ00243 743 -FFDEEDAARladavrvSQLEADLAQLggGLeTEIGEKGVN-LSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
34-208 |
1.15e-03 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 39.30 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 34 AQNLTLVKGsqklltqVRFQIPYGKNIALVGANGVGKTTLLEAIYHQIEGIDCSPKVQMAYYRQLAYEDMRDV------- 106
Cdd:PRK15079 31 PKTLKAVDG-------VTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdiqmi 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 107 ------SL-------------LQYLMDETDSSESFSR--AILNNLGLNEAL-DRSCNVLSGGERTKLSLAVLFSTKANML 164
Cdd:PRK15079 104 fqdplaSLnprmtigeiiaepLRTYHPKLSRQEVKDRvkAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLI 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 585044696 165 ILDEPTNFLD-------IKTLEALEMFMnkypGIIL-FTSHDTRFVKHVSDK 208
Cdd:PRK15079 184 ICDEPVSALDvsiqaqvVNLLQQLQREM----GLSLiFIAHDLAVVKHISDR 231
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
47-198 |
1.20e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 39.01 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 47 LTQVRFQIPYGKNIALVGANGVGKTT---LLEAIYHQIEGIDCSPKVQMAYYRQLAYEDMRD-VSLL------QYLMDET 116
Cdd:PRK13640 23 LNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTAKTVWDIREkVGIVfqnpdnQFVGATV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 117 DSSESFS---------------RAILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLD----IKT 177
Cdd:PRK13640 103 GDDVAFGlenravprpemikivRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDpagkEQI 182
|
170 180
....*....|....*....|.
gi 585044696 178 LEALEMFMNKYPGIILFTSHD 198
Cdd:PRK13640 183 LKLIRKLKKKNNLTVISITHD 203
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
50-198 |
1.29e-03 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 38.91 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 50 VRFQIPYGKNIALVGANGVGKTT---LLEAIYHQIEGI----DCSP-KVQMAYYR----------QLAYedmrDVSLLqy 111
Cdd:COG4586 41 ISFTIEPGEIVGFIGPNGAGKSTtikMLTGILVPTSGEvrvlGYVPfKRRKEFARrigvvfgqrsQLWW----DLPAI-- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 112 lmdetdssESFS--RAI-----------LNN----LGLNEALDRSCNVLSGGERTK--LSLAVLFSTKanMLILDEPTNF 172
Cdd:COG4586 115 --------DSFRllKAIyripdaeykkrLDElvelLDLGELLDTPVRQLSLGQRMRceLAAALLHRPK--ILFLDEPTIG 184
|
170 180 190
....*....|....*....|....*....|
gi 585044696 173 LDIKTLEALEMF---MNKYPGI-ILFTSHD 198
Cdd:COG4586 185 LDVVSKEAIREFlkeYNRERGTtILLTSHD 214
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
60-186 |
1.90e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 38.23 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 60 IALVGANGVGKTTLLEAIYHQIEgidcsPKVQMAYyrqLAYEDMRDVSLLQYLMDETD-SSESFSRAILNNLgLNEALDR 138
Cdd:COG3267 46 VVLTGEVGTGKTTLLRRLLERLP-----DDVKVAY---IPNPQLSPAELLRAIADELGlEPKGASKADLLRQ-LQEFLLE 116
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 585044696 139 SCnvlSGGERTklslavlfstkanMLILDEPTNfLDIKTLEALEMFMN 186
Cdd:COG3267 117 LA---AAGRRV-------------VLIIDEAQN-LPPETLEELRLLSN 147
|
|
| COG1106 |
COG1106 |
ATPase/GTPase, AAA15 family [General function prediction only]; |
35-78 |
1.92e-03 |
|
ATPase/GTPase, AAA15 family [General function prediction only];
Pssm-ID: 440723 [Multi-domain] Cd Length: 330 Bit Score: 38.49 E-value: 1.92e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 585044696 35 QNLTLVKGSQKLLtqvrfqipygKNIALVGANGVGKTTLLEAIY 78
Cdd:COG1106 17 LTLSMVASGLRLL----------RVNLIYGANASGKSNLLEALY 50
|
|
| EF-G_bact |
cd04170 |
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). ... |
59-77 |
1.93e-03 |
|
Elongation factor G (EF-G) family; Translocation is mediated by EF-G (also called translocase). The structure of EF-G closely resembles that of the complex between EF-Tu and tRNA. This is an example of molecular mimicry; a protein domain evolved so that it mimics the shape of a tRNA molecule. EF-G in the GTP form binds to the ribosome, primarily through the interaction of its EF-Tu-like domain with the 50S subunit. The binding of EF-G to the ribosome in this manner stimulates the GTPase activity of EF-G. On GTP hydrolysis, EF-G undergoes a conformational change that forces its arm deeper into the A site on the 30S subunit. To accommodate this domain, the peptidyl-tRNA in the A site moves to the P site, carrying the mRNA and the deacylated tRNA with it. The ribosome may be prepared for these rearrangements by the initial binding of EF-G as well. The dissociation of EF-G leaves the ribosome ready to accept the next aminoacyl-tRNA into the A site. This group contains only bacterial members.
Pssm-ID: 206733 [Multi-domain] Cd Length: 268 Bit Score: 38.34 E-value: 1.93e-03
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
143-215 |
2.30e-03 |
|
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: 37.55 E-value: 2.30e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 585044696 143 LSGGERTKLSLAVLFSTKANMLILDEPTNFLDIK----TLEALEMFMNKYPGIILFTSHDTRFVKHVSDKKWELTGQ 215
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEqrlnAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
143-208 |
2.32e-03 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 38.35 E-value: 2.32e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 585044696 143 LSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTleALEMF-----MNKYPGI-ILFTSHDTRFVKHVSDK 208
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEPTNAMESTT--QAQIFrllarLNQLQGTsILLISHDLESISQWADT 228
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
35-77 |
2.71e-03 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 38.16 E-value: 2.71e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 585044696 35 QNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAI 77
Cdd:COG3842 9 ENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMI 51
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
117-177 |
2.83e-03 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 38.18 E-value: 2.83e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 585044696 117 DSSESFSRA----ILNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKT 177
Cdd:NF000106 115 DLSRKDARAradeLLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRT 179
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
34-175 |
3.76e-03 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 37.50 E-value: 3.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 34 AQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQI-------------------EGIDCSPKVQMAY 94
Cdd:PRK13547 4 ADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgarvtgdvtlngEPLAAIDAPRLAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 95 YR-------QLAYE-DMRDVSLLQYLMDETDSSESFSR------AILNNLGLNEALDRSCNVLSGGERTKLS----LAVL 156
Cdd:PRK13547 84 LRavlpqaaQPAFAfSAREIVLLGRYPHARRAGALTHRdgeiawQALALAGATALVGRDVTTLSGGELARVQfarvLAQL 163
|
170 180
....*....|....*....|....
gi 585044696 157 FSTKANM-----LILDEPTNFLDI 175
Cdd:PRK13547 164 WPPHDAAqppryLLLDEPTAALDL 187
|
|
| FusA |
COG0480 |
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; ... |
58-77 |
3.79e-03 |
|
Translation elongation factor EF-G, a GTPase [Translation, ribosomal structure and biogenesis]; Translation elongation factor EF-G, a GTPase is part of the Pathway/BioSystem: Translation factors
Pssm-ID: 440248 [Multi-domain] Cd Length: 693 Bit Score: 37.72 E-value: 3.79e-03
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
119-208 |
3.83e-03 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 37.28 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 119 SESFSRAI--LNNLGLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPT---NFLDIKTLEALEMFMNKYPGI-I 192
Cdd:PRK11300 128 SEALDRAAtwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAaglNPKETKELDELIAELRNEHNVtV 207
|
90
....*....|....*.
gi 585044696 193 LFTSHDTRFVKHVSDK 208
Cdd:PRK11300 208 LLIEHDMKLVMGISDR 223
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
35-74 |
3.99e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 37.80 E-value: 3.99e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 585044696 35 QNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTTLL 74
Cdd:NF033858 5 EGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLL 44
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
61-198 |
4.13e-03 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 37.25 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 61 ALVGANGVGKTTLLEAI----YHQIEGidcSPKVQMAYYRQLAYEDMRDVSL------LQYL------MDETDssesFSR 124
Cdd:cd03279 32 LICGPTGAGKSTILDAItyalYGKTPR---YGRQENLRSVFAPGEDTAEVSFtfqlggKKYRversrgLDYDQ----FTR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 125 AILNNLG-LNEALDRSCNVLSGGERTKLSLAVLF--------STKANM--LILDEPTNFLDIKTLEALEMFMNKYPG--- 190
Cdd:cd03279 105 IVLLPQGeFDRFLARPVSTLSGGETFLASLSLALalsevlqnRGGARLeaLFIDEGFGTLDPEALEAVATALELIRTenr 184
|
....*...
gi 585044696 191 IILFTSHD 198
Cdd:cd03279 185 MVGVISHV 192
|
|
| VirB11 |
TIGR02788 |
P-type DNA transfer ATPase VirB11; The VirB11 protein is found in the vir locus of ... |
51-81 |
4.22e-03 |
|
P-type DNA transfer ATPase VirB11; The VirB11 protein is found in the vir locus of Agrobacterium Ti plasmids where it is involved in the type IV secretion system for DNA transfer. VirB11 is believed to be an ATPase. VirB11 is a homolog of the P-like conjugation system TrbB protein and the Flp pilus sytem protein TadA.
Pssm-ID: 274301 Cd Length: 308 Bit Score: 37.33 E-value: 4.22e-03
10 20 30
....*....|....*....|....*....|.
gi 585044696 51 RFQIPYGKNIALVGANGVGKTTLLEAIYHQI 81
Cdd:TIGR02788 138 RLAIASRKNIIISGGTGSGKTTFLKSLVDEI 168
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
136-196 |
4.74e-03 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 37.68 E-value: 4.74e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 585044696 136 LDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTLEALEMFMNKYPG----IILFTS 196
Cdd:PRK10762 389 MEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAeglsIILVSS 453
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
61-79 |
4.80e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 37.37 E-value: 4.80e-03
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
114-174 |
4.81e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 37.57 E-value: 4.81e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 585044696 114 DETDSSESFSRAILNNlGLNEALDRscnvLSGGERTKLSLAV------LFSTKANMLILDEPTNFLD 174
Cdd:PRK01156 778 DDIDVDQDFNITVSRG-GMVEGIDS----LSGGEKTAVAFALrvavaqFLNNDKSLLIMDEPTAFLD 839
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
119-176 |
6.53e-03 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 36.65 E-value: 6.53e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 585044696 119 SESFSRAILNNLGLNEAL-DRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIK 176
Cdd:PRK13649 121 AEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
32-170 |
7.31e-03 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 37.03 E-value: 7.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 32 IIAQNLTLVKGSQKLLTQVRFQIPYGKNIALVGANGVGKTT-------LLEAIyhqiEG--------IDCSPkvqMAYYR 96
Cdd:NF033858 267 IEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTtmkmltgLLPAS----EGeawlfgqpVDAGD---IATRR 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 97 QLAYedmrdvsllqylMdetdsSESFS-----------------------------RAILNNLGLNEALDRSCNVLSGGE 147
Cdd:NF033858 340 RVGY------------M-----SQAFSlygeltvrqnlelharlfhlpaaeiaarvAEMLERFDLADVADALPDSLPLGI 402
|
170 180
....*....|....*....|...
gi 585044696 148 RTKLSLAVLFSTKANMLILDEPT 170
Cdd:NF033858 403 RQRLSLAVAVIHKPELLILDEPT 425
|
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
53-82 |
7.33e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 35.97 E-value: 7.33e-03
10 20 30
....*....|....*....|....*....|
gi 585044696 53 QIPYGKNIALVGANGVGKTTLLEAIYHQIE 82
Cdd:cd00009 15 ELPPPKNLLLYGPPGTGKTTLARAIANELF 44
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
46-182 |
8.03e-03 |
|
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: 36.43 E-value: 8.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 46 LLTQVRFQIPYGKNIALVGANGVGKTTLLEAIYHQ---------IEGIDCSpKVQMAYYRQLAYEDMRDVSL----LQYL 112
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMvdifdgkivIDGIDIS-KLPLHTLRSRLSIILQDPILfsgsIRFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 113 MDE----TDSS--ESFSRAILNNL------GLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDIKTLEA 180
Cdd:cd03288 115 LDPeckcTDDRlwEALEIAQLKNMvkslpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENI 194
|
..
gi 585044696 181 LE 182
Cdd:cd03288 195 LQ 196
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
51-77 |
8.30e-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: 36.52 E-value: 8.30e-03
10 20
....*....|....*....|....*...
gi 585044696 51 RFQIPYGKNI-ALVGANGVGKTTLLEAI 77
Cdd:COG3593 16 DLSIELSDDLtVLVGENNSGKSSILEAL 43
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
64-203 |
8.44e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 36.00 E-value: 8.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 585044696 64 GANGVGKTTLLEAI-----------YHQIEGIDCSPKVQMAYY-RQLAYE-DMRDVSLLQYLMDETDSSESFSRAIlNNL 130
Cdd:PRK13541 33 GANGCGKSSLLRMIagimqpssgniYYKNCNINNIAKPYCTYIgHNLGLKlEMTVFENLKFWSEIYNSAETLYAAI-HYF 111
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 585044696 131 GLNEALDRSCNVLSGGERTKLSLAVLFSTKANMLILDEPTNFLDI---KTLEALEMFMNKYPGIILFTSHDTRFVK 203
Cdd:PRK13541 112 KLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKenrDLLNNLIVMKANSGGIVLLSSHLESSIK 187
|
|
| |
