|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
261-498 |
4.29e-144 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 412.85 E-value: 4.29e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfIKAGKRDdapvIRQGIRR 340
Cdd:COG1126 4 IENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGED-LTDSKKD----INKLRRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 IGMVFQNFNLFPHRTILDNVILAPRYHGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIM 420
Cdd:COG1126 79 VGMVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2084914118 421 LFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSE-GDPRVRRFIG 498
Cdd:COG1126 159 LFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENpQHERTRAFLS 237
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
261-476 |
8.51e-121 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 352.60 E-value: 8.51e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfIKAGKRDdapvIRQGIRR 340
Cdd:cd03262 3 IKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLK-LTDDKKN----INELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 IGMVFQNFNLFPHRTILDNVILAPRY-HGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDI 419
Cdd:cd03262 78 VGMVFQQFNLFPHLTVLENITLAPIKvKGM-SKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKV 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 420 MLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHV 476
Cdd:cd03262 157 MLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
256-497 |
7.02e-112 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 331.77 E-value: 7.02e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 256 PDALLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGN--DFIKAGKRDDAPV 333
Cdd:COG4598 6 PPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEeiRLKPDRDGELVPA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 334 IRQGIRRI----GMVFQNFNLFPHRTILDNVILAPRY-HGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVA 408
Cdd:COG4598 86 DRRQLQRIrtrlGMVFQSFNLWSHMTVLENVIEAPVHvLGR-PKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 409 IARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI--- 485
Cdd:COG4598 165 IARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVfgn 244
|
250
....*....|...
gi 2084914118 486 -RSEgdpRVRRFI 497
Cdd:COG4598 245 pKSE---RLRQFL 254
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
261-497 |
6.26e-100 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 300.47 E-value: 6.26e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfIKAGKRDDApVIRQgirR 340
Cdd:PRK09493 4 FKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLK-VNDPKVDER-LIRQ---E 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 IGMVFQNFNLFPHRTILDNVILAPRYHGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIM 420
Cdd:PRK09493 79 AGMVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 421 LFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPAS-IRSEGDPRVRRFI 497
Cdd:PRK09493 159 LFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVlIKNPPSQRLQEFL 236
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
258-497 |
4.41e-87 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 268.16 E-value: 4.41e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 258 ALLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLfGNDFIKAGK--RDDAPVIR 335
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRV-GDITIDTARslSQQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 336 QGIRRIGMVFQNFNLFPHRTILDNVILAPRYHGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAM 415
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 416 EPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSE-GDPRVR 494
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADpQQPRTR 241
|
...
gi 2084914118 495 RFI 497
Cdd:PRK11264 242 QFL 244
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
261-497 |
9.08e-87 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 266.85 E-value: 9.08e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDAPvIRqgiRR 340
Cdd:COG1127 8 VRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYE-LR---RR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 IGMVFQNFNLFPHRTILDNVILAPRYHGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIM 420
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 421 LFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSEGDPRVRRFI 497
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDDPWVRQFL 241
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
258-498 |
5.59e-85 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 266.19 E-value: 5.59e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 258 ALLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDF--IKAGKRDdapvir 335
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVtgLPPEKRN------ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 336 qgirrIGMVFQNFNLFPHRTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAM 415
Cdd:COG3842 79 -----VGMVFQDYALFPHLTVAENVAFGLRMRGV-PKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 416 EPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSE-GDPRV 493
Cdd:COG3842 153 EPRVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERpATRFV 232
|
....*
gi 2084914118 494 RRFIG 498
Cdd:COG3842 233 ADFIG 237
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
259-476 |
9.36e-84 |
|
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: 258.19 E-value: 9.36e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGN----HEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDAPVI 334
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 335 RqgiRRIGMVFQNFNLFPHRTILDNVILAPRYHGLAdSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALA 414
Cdd:cd03255 81 R---RHIGFVFQSFNLLPDLTALENVELPLLLAGVP-KKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 415 MEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFAlSISDRIVFMENGHV 476
Cdd:cd03255 157 NDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
262-497 |
1.14e-81 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 253.98 E-value: 1.14e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 262 RDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRD------DAPVIR 335
Cdd:TIGR03005 4 SDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRNgplvpaDEKHLR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 336 QGIRRIGMVFQNFNLFPHRTILDNVILAP-RYHGLAdSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALA 414
Cdd:TIGR03005 84 QMRNKIGMVFQSFNLFPHKTVLDNVTEAPvLVLGMA-RAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARALA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 415 MEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI-RSEGDPR 492
Cdd:TIGR03005 163 MRPKVMLFDEVTSALDPELVGEVLNVIRRLASEhDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIfRQPKEER 242
|
....*
gi 2084914118 493 VRRFI 497
Cdd:TIGR03005 243 TREFL 247
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
261-477 |
1.37e-81 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 256.93 E-value: 1.37e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRY----GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDdapvIRQ 336
Cdd:COG1135 4 LENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERE----LRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 337 GIRRIGMVFQNFNLFPHRTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAME 416
Cdd:COG1135 80 ARRKIGMIFQHFNLLSSRTVAENVALPLEIAGV-PKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084914118 417 PDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:COG1135 159 PKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIV 220
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
256-479 |
1.75e-81 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 252.66 E-value: 1.75e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 256 PDALLLRDIHKRYGN----HEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfIKAGKRDDA 331
Cdd:COG1136 2 SPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQD-ISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 332 PVIRQgiRRIGMVFQNFNLFPHRTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIAR 411
Cdd:COG1136 81 ARLRR--RHIGFVFQFFNLLPELTALENVALPLLLAGV-SRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2084914118 412 ALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFAlSISDRIVFMENGHVVTD 479
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELA-ARADRVIRLRDGRIVSD 225
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
261-496 |
1.09e-78 |
|
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: 245.87 E-value: 1.09e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDAPvIRqgiRR 340
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYR-LR---RR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 IGMVFQNFNLFPHRTILDNVILAPRYHGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIM 420
Cdd:cd03261 79 MGMLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 421 LFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSEGDPRVRRF 496
Cdd:cd03261 159 LYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDDPLVRQF 235
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
261-477 |
1.95e-78 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 245.31 E-value: 1.95e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFiKAGKRDDAPVIRQGIRR 340
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHF-DFSKTPSDKAIRELRRN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 IGMVFQNFNLFPHRTILDNVILAP-RYHGLADsAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDI 419
Cdd:PRK11124 84 VGMVFQQYNLWPHLTVQQNLIEAPcRVLGLSK-DQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 420 MLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIV 220
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
253-505 |
2.30e-78 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 245.77 E-value: 2.30e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 253 PGQPDALLLRDIHKRY----GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLfgndfikagkr 328
Cdd:COG1116 2 SAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLV----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 329 DDAPVIRQGiRRIGMVFQNFNLFPHRTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVA 408
Cdd:COG1116 71 DGKPVTGPG-PDRGVVFQEPALLPWLTVLDNVALGLELRGV-PKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 409 IARALAMEPDIMLFDEPTSALDP----ELVGEVLNVirdLAREGMTMLIVTHEMDFALSISDRIVFMENGhvvtdasPAS 484
Cdd:COG1116 149 IARALANDPEVLLMDEPFGALDAltreRLQDELLRL---WQETGKTVLFVTHDVDEAVFLADRVVVLSAR-------PGR 218
|
250 260 270
....*....|....*....|....*....|..
gi 2084914118 485 IRSE---GDPRVR--------RFIGLEQEVTA 505
Cdd:COG1116 219 IVEEidvDLPRPRdrelrtspEFAALRAEILD 250
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
258-483 |
4.01e-78 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 244.97 E-value: 4.01e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 258 ALLLRDIHKRY-GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDdapvIRQ 336
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRA----LRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 337 GIRRIGMVFQNFNLFPHRTILDNViLAPR--YHGLADS------AELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVA 408
Cdd:COG3638 78 LRRRIGMIFQQFNLVPRLSVLTNV-LAGRlgRTSTWRSllglfpPEDRERALEALERVGLADKAYQRADQLSGGQQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2084914118 409 IARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPA 483
Cdd:COG3638 157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPA 232
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
261-477 |
1.45e-77 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 243.00 E-value: 1.45e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFiKAGKRDDAPVIRQGIRR 340
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQF-DFSQKPSEKAIRLLRQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 IGMVFQNFNLFPHRTILDNVILAP-RYHGLAdSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDI 419
Cdd:COG4161 84 VGMVFQQYNLWPHLTVMENLIEAPcKVLGLS-KEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 420 MLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRII 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
261-483 |
6.77e-77 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 240.72 E-value: 6.77e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGN-HEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAgKRDDAPVIRqgiR 339
Cdd:COG2884 4 FENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRL-KRREIPYLR---R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 340 RIGMVFQNFNLFPHRTILDNVILAPRYHGlADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDI 419
Cdd:COG2884 80 RIGVVFQDFRLLPDRTVYENVALPLRVTG-KSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084914118 420 MLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPA 483
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARG 222
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
259-477 |
9.55e-77 |
|
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: 240.11 E-value: 9.55e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIkagkrdDAPVIRqgi 338
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT------GVPPER--- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRIGMVFQNFNLFPHRTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPD 418
Cdd:cd03259 72 RNIGMVFQDYALFPHLTVAENIAFGLKLRGV-PKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 419 IMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:cd03259 151 LLLLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
261-490 |
1.01e-76 |
|
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: 240.31 E-value: 1.01e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRY-GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDdapvIRqgiR 339
Cdd:COG1122 3 LENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRE----LR---R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 340 RIGMVFQN-FN-LFpHRTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEP 417
Cdd:COG1122 76 KVGLVFQNpDDqLF-APTVEEDVAFGPENLGL-PREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 418 DIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSEGD 490
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
259-497 |
1.34e-76 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 241.41 E-value: 1.34e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRD------DAP 332
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvaDKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 333 VIRQGIRRIGMVFQNFNLFPHRTILDNVILAP-RYHGLAdSAELRRKGHGLLDRVGLLAHAH-KYPHQLSGGQQQRVAIA 410
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPiQVLGLS-KQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 411 RALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI-RSEG 489
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLfGNPQ 244
|
....*...
gi 2084914118 490 DPRVRRFI 497
Cdd:PRK10619 245 SPRLQQFL 252
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
203-485 |
1.89e-76 |
|
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: 249.05 E-value: 1.89e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 203 VLIVTLFGWLLQWAERHLDLsRKNARTLDDTQAQALRQPAS--------ASKKRNEPVPGQPDALL-LRDIHKRY----- 268
Cdd:COG1123 197 LLITHDLGVVAEIADRVVVM-DDGRIVEDGPPEEILAAPQAlaavprlgAARGRAAPAAAAAEPLLeVRNLSKRYpvrgk 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 269 GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDdapvIRQGIRRIGMVFQNF 348
Cdd:COG1123 276 GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRS----LRELRRRVQMVFQDP 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 349 N--LFPHRTILDNVILAPRYHGLADSAELRRKGHGLLDRVGLLA-HAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEP 425
Cdd:COG1123 352 YssLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPdLADRYPHELSGGQRQRVAIARALALEPKLLILDEP 431
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084914118 426 TSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI 485
Cdd:COG1123 432 TSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
261-477 |
6.37e-75 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 235.94 E-value: 6.37e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNH----EVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDdapvIRQ 336
Cdd:cd03258 4 LKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKE----LRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 337 GIRRIGMVFQNFNLFPHRTILDNVILAPRYHGLADsAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAME 416
Cdd:cd03258 80 ARRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPK-AEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084914118 417 PDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:cd03258 159 PKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
262-485 |
3.01e-74 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 234.88 E-value: 3.01e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 262 RDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSL-ESID----RGEIVLFGNDfIKAGKRDDApVIRq 336
Cdd:TIGR00972 5 ENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMnDLVPgvriEGKVLFDGQD-IYDKKIDVV-ELR- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 337 giRRIGMVFQNFNLFPhRTILDNVILAPRYHGLADSAELRR------KGHGLLDRVGllAHAHKYPHQLSGGQQQRVAIA 410
Cdd:TIGR00972 82 --RRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELDEiveeslKKAALWDEVK--DRLHDSALGLSGGQQQRLCIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084914118 411 RALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLaREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI 485
Cdd:TIGR00972 157 RALAVEPEVLLLDEPTSALDPIATGKIEELIQEL-KKKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQI 230
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
259-477 |
3.92e-74 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 233.52 E-value: 3.92e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGN----HEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGndfikagkrddAPVI 334
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG-----------EPVT 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 335 RQGiRRIGMVFQNFNLFPHRTILDNVILAPRYHGLADsAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALA 414
Cdd:cd03293 70 GPG-PDRGYVFQQDALLPWLTVLDNVALGLELQGVPK-AEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALA 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2084914118 415 MEPDIMLFDEPTSALDP----ELVGEVLNVIRdlaREGMTMLIVTHEMDFALSISDRIVFMEN--GHVV 477
Cdd:cd03293 148 VDPDVLLLDEPFSALDAltreQLQEELLDIWR---ETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIV 213
|
|
| HisM |
COG0765 |
ABC-type amino acid transport system, permease component [Amino acid transport and metabolism]; ... |
1-224 |
6.76e-74 |
|
ABC-type amino acid transport system, permease component [Amino acid transport and metabolism];
Pssm-ID: 440528 [Multi-domain] Cd Length: 218 Bit Score: 232.66 E-value: 6.76e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 1 MAFDWAYFFSlfSVSAFWKACLTVVQLSTLSWSIGLVLGFLLASAKLSGHAWLRMPASFYIWLFRSIPLLVLLVFVYN-L 79
Cdd:COG0765 1 MFFDFSVLLD--YLPLLLEGLLVTLLLTVLAIVLGLVLGLLLALARLSPNPVLRWLATAYVEFFRGTPLLVQLFFIYFgL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 80 PQLfpvtGSVLSqPFYSGLIALVLTETAYMAEIHRGGLLSVLKGQREAAKALGIRGVGAQRLVIIPQAIRISLPTLTNEY 159
Cdd:COG0765 79 PLL----GIDLS-PFVAAVIALTLNSAAYLAEIVRAGIQSVPKGQWEAARALGLSRWQTMRRIILPQALRIILPPLGNEF 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084914118 160 VTIVKLTSLVSVISLNELLLVGQRLYAQNFLVLETLAAVAIYYVLIVTLFGWLLQWAERHLDLSR 224
Cdd:COG0765 154 ISLLKDTSLVSVIGVPELTRAAQQIASRTFRPFEVYLVAALIYLVLTLPLSLLARRLERRLARGR 218
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
261-488 |
8.80e-73 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 230.34 E-value: 8.80e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFikagkRDDAPVIRqgiRR 340
Cdd:COG1131 3 VRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV-----ARDPAEVR---RR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 IGMVFQNFNLFPHRTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIM 420
Cdd:COG1131 75 IGYVPQEPALYPDLTVRENLRFFARLYGL-PRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 421 LFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSE 488
Cdd:COG1131 154 ILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
261-488 |
4.78e-70 |
|
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: 223.60 E-value: 4.78e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGN-HEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDdapvIRQGIR 339
Cdd:cd03256 3 VENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKA----LRQLRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 340 RIGMVFQNFNLFPHRTILDNViLAPR--YH-------GLADSAElRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIA 410
Cdd:cd03256 79 QIGMIFQQFNLIERLSVLENV-LSGRlgRRstwrslfGLFPKEE-KQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2084914118 411 RALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSE 488
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDE 235
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
259-475 |
1.08e-69 |
|
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: 220.52 E-value: 1.08e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFikAGKRDDAPVIRqgi 338
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDL--TDLEDELPPLR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRIGMVFQNFNLFPHRTILDNVILApryhgladsaelrrkghglldrvgllahahkyphqLSGGQQQRVAIARALAMEPD 418
Cdd:cd03229 76 RRIGMVFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 419 IMLFDEPTSALDPELVGEVLNVIRDL-AREGMTMLIVTHEMDFALSISDRIVFMENGH 475
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
261-498 |
1.28e-69 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 224.97 E-value: 1.28e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGN-HEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFikagKRDDAPVIRqgiR 339
Cdd:COG1125 4 FENVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDI----RDLDPVELR---R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 340 RIGMVFQNFNLFPHRTILDNVILAPRYHGlADSAELRRKGHGLLDRVGLLA--HAHKYPHQLSGGQQQRVAIARALAMEP 417
Cdd:COG1125 77 RIGYVIQQIGLFPHMTVAENIATVPRLLG-WDKERIRARVDELLELVGLDPeeYRDRYPHELSGGQQQRVGVARALAADP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 418 DIMLFDEPTSALDP----ELVGEVLNVIRDLareGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI-RSEGDPR 492
Cdd:COG1125 156 PILLMDEPFGALDPitreQLQDELLRLQREL---GKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEIlANPANDF 232
|
....*.
gi 2084914118 493 VRRFIG 498
Cdd:COG1125 233 VADFVG 238
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
259-498 |
1.57e-69 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 225.80 E-value: 1.57e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGND-FIKAGKRDdapvirqg 337
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlFTNLPPRE-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 338 iRRIGMVFQNFNLFPHRTILDNVILAPRyHGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEP 417
Cdd:COG1118 75 -RRVGFVFQHYALFPHMTVAENIAFGLR-VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 418 DIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI-RSEGDPRVRR 495
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRRLHDElGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVyDRPATPFVAR 232
|
...
gi 2084914118 496 FIG 498
Cdd:COG1118 233 FLG 235
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
261-498 |
2.23e-68 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 219.03 E-value: 2.23e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIkagkrdDAPVIRqgiRR 340
Cdd:cd03300 3 LENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT------NLPPHK---RP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 IGMVFQNFNLFPHRTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIM 420
Cdd:cd03300 74 VNTVFQNYALFPHLTVFENIAFGLRLKKL-PKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 421 LFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSEGDPR-VRRFIG 498
Cdd:cd03300 153 LLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRfVADFIG 232
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
258-498 |
8.07e-68 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 221.49 E-value: 8.07e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 258 ALLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDF--IKAGKRDdapvir 335
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtdLPPKDRN------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 336 qgirrIGMVFQNFNLFPHRTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAM 415
Cdd:COG3839 77 -----IAMVFQSYALYPHMTVYENIAFPLKLRKV-PKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 416 EPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSegDPR-- 492
Cdd:COG3839 151 EPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRlGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYD--RPAnl 228
|
....*..
gi 2084914118 493 -VRRFIG 498
Cdd:COG3839 229 fVAGFIG 235
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
261-475 |
1.74e-67 |
|
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: 215.79 E-value: 1.74e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHE--VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFikagkrdDAPVIRQGI 338
Cdd:cd03225 2 LKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDL-------TKLSLKELR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRIGMVFQNFNL-FPHRTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEP 417
Cdd:cd03225 75 RKVGLVFQNPDDqFFGPTVEEEVAFGLENLGL-PEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 418 DIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGH 475
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
266-485 |
2.08e-67 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 216.78 E-value: 2.08e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 266 KRYGN-HEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDdapvIRQGIRRIGMV 344
Cdd:TIGR02315 9 KVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKK----LRKLRRRIGMI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 345 FQNFNLFPHRTILDNViLAPR--YH-------GLADSAElRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAM 415
Cdd:TIGR02315 85 FQHYNLIERLTVLENV-LHGRlgYKptwrsllGRFSEED-KERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQ 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084914118 416 EPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI 485
Cdd:TIGR02315 163 QPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
261-485 |
2.39e-67 |
|
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: 216.28 E-value: 2.39e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESI-----DRGEIVLFGNDfikAGKRDDAPV-I 334
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKD---IYDLDVDVLeL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 335 RqgiRRIGMVFQNFNLFPhRTILDNVILAPRYHGLADSAELRRKGHGLLDRVGL--LAHAHKYPHQLSGGQQQRVAIARA 412
Cdd:cd03260 80 R---RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 413 LAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREgMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI 485
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
259-498 |
8.42e-67 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 219.14 E-value: 8.42e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGND--FIKAGKRDdapvirq 336
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDitRLPPQKRD------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 337 girrIGMVFQNFNLFPHRTILDNVIlapryHGL----ADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARA 412
Cdd:TIGR03265 78 ----YGIVFQSYALFPNLTVADNIA-----YGLknrgMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 413 LAMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI-RSEGD 490
Cdd:TIGR03265 149 LATSPGLLLLDEPLSALDARVREHLRTEIRQLQRRlGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIyRHPAT 228
|
....*...
gi 2084914118 491 PRVRRFIG 498
Cdd:TIGR03265 229 PFVADFVG 236
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
249-477 |
1.63e-66 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 214.90 E-value: 1.63e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 249 NEPVPGQPDALLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSL-ESID----RGEIVLFGNDfI 323
Cdd:COG1117 2 TAPASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMnDLIPgarvEGEILLDGED-I 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 324 kAGKRDDAPVIRqgiRRIGMVFQNFNLFPHrTILDNVILAPRYHGLADSAELRRKGHGLLDRVGL-------LahaHKYP 396
Cdd:COG1117 81 -YDPDVDVVELR---RRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALwdevkdrL---KKSA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 397 HQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDP-------ELvgevlnvIRDLAREgMTMLIVTHEMDFALSISDRIV 469
Cdd:COG1117 153 LGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPistakieEL-------ILELKKD-YTIVIVTHNMQQAARVSDYTA 224
|
....*...
gi 2084914118 470 FMENGHVV 477
Cdd:COG1117 225 FFYLGELV 232
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
261-477 |
4.25e-66 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 216.98 E-value: 4.25e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRY----GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDdapvIRQ 336
Cdd:PRK11153 4 LKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKE----LRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 337 GIRRIGMVFQNFNLFPHRTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAME 416
Cdd:PRK11153 80 ARRQIGMIFQHFNLLSSRTVFDNVALPLELAGT-PKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084914118 417 PDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
261-477 |
4.25e-66 |
|
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: 212.75 E-value: 4.25e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGN----HEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRddapviRQ 336
Cdd:cd03257 4 VKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRR------LR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 337 GIRR--IGMVFQN--FNLFPHRTILDNVILAPRYHG-LADSAELRRKGHGLLDRVGLLA-HAHKYPHQLSGGQQQRVAIA 410
Cdd:cd03257 78 KIRRkeIQMVFQDpmSSLNPRMTIGEQIAEPLRIHGkLSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 411 RALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
258-487 |
7.97e-66 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 212.74 E-value: 7.97e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 258 ALLLRDIHKRYG----NHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDApv 333
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 334 irqgiRRIGMVFQN----FNlfPHRTILDNVILAPRYHGLADSAELRRKghgLLDRVGL-LAHAHKYPHQLSGGQQQRVA 408
Cdd:COG1124 79 -----RRVQMVFQDpyasLH--PRHTVDRILAEPLRIHGLPDREERIAE---LLEQVGLpPSFLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 409 IARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRS 487
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
256-495 |
2.00e-65 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 212.21 E-value: 2.00e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 256 PDALL-LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFikAGKRDDApVI 334
Cdd:COG0411 1 SDPLLeVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI--TGLPPHR-IA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 335 RQGIRRIgmvFQNFNLFPHRTILDNVILAPRYHG--------------LADSAELRRKGHGLLDRVGLLAHAHKYPHQLS 400
Cdd:COG0411 78 RLGIART---FQNPRLFPELTVLENVLVAAHARLgrgllaallrlpraRREEREARERAEELLERVGLADRADEPAGNLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 401 GGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTD 479
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAE 234
|
250
....*....|....*.
gi 2084914118 480 ASPASIRSegDPRVRR 495
Cdd:COG0411 235 GTPAEVRA--DPRVIE 248
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
259-493 |
5.29e-65 |
|
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: 210.37 E-value: 5.29e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFikAGKRDDApVIRQGI 338
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDI--TGLPPHE-IARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRigmVFQNFNLFPHRTILDNVILAPRYHG---------LADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAI 409
Cdd:cd03219 78 GR---TFQIPRLFPELTVLENVMVAAQARTgsglllaraRREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 410 ARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSeg 489
Cdd:cd03219 155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN-- 232
|
....
gi 2084914118 490 DPRV 493
Cdd:cd03219 233 NPRV 236
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
262-497 |
5.69e-63 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 206.34 E-value: 5.69e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 262 RDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDAPVIRqgiRRI 341
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRR---KKI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 342 GMVFQNFNLFPHRTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIML 421
Cdd:cd03294 105 SMVFQSFALLPHRTVLENVAFGLEVQGV-PRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILL 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 422 FDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI-RSEGDPRVRRFI 497
Cdd:cd03294 184 MDEAFSALDPLIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEIlTNPANDYVREFF 261
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
263-497 |
1.95e-62 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 208.80 E-value: 1.95e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 263 DIHKRYGnHEV-LKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDdapvIRQgIRR- 340
Cdd:COG4175 32 EILEKTG-QTVgVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKLSKKE----LRE-LRRk 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 -IGMVFQNFNLFPHRTILDNVILapryhGL----ADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAM 415
Cdd:COG4175 106 kMSMVFQHFALLPHRTVLENVAF-----GLeiqgVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALAT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 416 EPDIMLFDEPTSALDP----ELVGEVLNVIRDLARegmTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI-RSEGD 490
Cdd:COG4175 181 DPDILLMDEAFSALDPlirrEMQDELLELQAKLKK---TIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEIlTNPAN 257
|
....*..
gi 2084914118 491 PRVRRFI 497
Cdd:COG4175 258 DYVADFV 264
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
258-498 |
3.39e-62 |
|
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: 203.34 E-value: 3.39e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 258 ALLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDdapvirqg 337
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 338 iRRIGMVFQNFNLFPHRTILDNVILAPRYHGLA---DSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALA 414
Cdd:cd03296 74 -RNVGFVFQHYALFRHMTVFDNVAFGLRVKPRSerpPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 415 MEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI-RSEGDPR 492
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVyDHPASPF 232
|
....*.
gi 2084914118 493 VRRFIG 498
Cdd:cd03296 233 VYSFLG 238
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
261-502 |
5.20e-62 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 202.92 E-value: 5.20e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGN-HEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFikagkRDDAPV-IRqgi 338
Cdd:cd03295 3 FENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDI-----REQDPVeLR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRIGMVFQNFNLFPHRTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGL--LAHAHKYPHQLSGGQQQRVAIARALAME 416
Cdd:cd03295 75 RKIGYVIQQIGLFPHMTVEENIALVPKLLKW-PKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 417 PDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI-RSEGDPRVR 494
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIlRSPANDFVA 233
|
....*...
gi 2084914118 495 RFIGLEQE 502
Cdd:cd03295 234 EFVGADRL 241
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
245-498 |
4.23e-61 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 204.80 E-value: 4.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 245 SKKRNEPVPGQPDALLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDF-- 322
Cdd:PRK09452 1 SKKLNKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIth 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 323 IKAGKRDdapvirqgirrIGMVFQNFNLFPHRTILDNVILAPRYHGLAdSAELRRKGHGLLDRVGLLAHAHKYPHQLSGG 402
Cdd:PRK09452 81 VPAENRH-----------VNTVFQSYALFPHMTVFENVAFGLRMQKTP-AAEITPRVMEALRMVQLEEFAQRKPHQLSGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 403 QQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDAS 481
Cdd:PRK09452 149 QQQRVAIARAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGT 228
|
250 260
....*....|....*....|
gi 2084914118 482 PASIRSEgdPR---VRRFIG 498
Cdd:PRK09452 229 PREIYEE--PKnlfVARFIG 246
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
261-490 |
6.62e-61 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 200.73 E-value: 6.62e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHE--VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDapvIRQgi 338
Cdd:TIGR04520 3 VENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENLWE---IRK-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 rRIGMVFQN-FNLFPHRTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEP 417
Cdd:TIGR04520 78 -KVGMVFQNpDNQFVGATVEDDVAFGLENLGV-PREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084914118 418 DIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSiSDRIVFMENGHVVTDASPASIRSEGD 490
Cdd:TIGR04520 156 DIIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQVE 228
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
261-477 |
8.87e-60 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 199.51 E-value: 8.87e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRY----GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLES---IDRGEIVLFGNDFIKAGKRDdapv 333
Cdd:COG0444 4 VRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKE---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 334 iRQGIR--RIGMVFQN----FNlfPHRTILDNVILAPRYHGLADSAELRRKGHGLLDRVGL---LAHAHKYPHQLSGGQQ 404
Cdd:COG0444 80 -LRKIRgrEIQMIFQDpmtsLN--PVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMR 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084914118 405 QRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
266-498 |
1.12e-59 |
|
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 200.85 E-value: 1.12e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 266 KRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDAPVIRqgiRRIGMVF 345
Cdd:TIGR01186 1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKQSPVELREVRR---KKIGMVF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 346 QNFNLFPHRTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEP 425
Cdd:TIGR01186 78 QQFALFPHMTILQNTSLGPELLGW-PEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084914118 426 TSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI-RSEGDPRVRRFIG 498
Cdd:TIGR01186 157 FSALDPLIRDSMQDELKKLQATlQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEIlRNPANEYVEEFIG 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
258-484 |
1.72e-58 |
|
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: 193.42 E-value: 1.72e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 258 ALLLRDIHKRYGNHE----VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfIKAGKRDDAPV 333
Cdd:COG4181 8 IIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQD-LFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 334 IRQgiRRIGMVFQNFNLFPHRTILDNVIL-APryhgLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARA 412
Cdd:COG4181 87 LRA--RHVGFVFQSFQLLPTLTALENVMLpLE----LAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 413 LAMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSiSDRIVFMENGHVVTDASPAS 484
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAATA 232
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
258-485 |
2.59e-58 |
|
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: 193.34 E-value: 2.59e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 258 ALLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfIKAGKRddapviRQG 337
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRD-LASLSR------REL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 338 IRRIGMVFQNFNLFPHRTILDNVIL--APrYHGL--ADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARAL 413
Cdd:COG1120 74 ARRIAYVPQEPPAPFGLTVRELVALgrYP-HLGLfgRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 414 AMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI 485
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
259-498 |
3.84e-57 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 189.58 E-value: 3.84e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHevLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKA--GKRddaPVirq 336
Cdd:COG3840 2 LRLDDLTYRYGDF--PLRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALppAER---PV--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 337 girriGMVFQNFNLFPHRTILDNVILAPRyHGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAME 416
Cdd:COG3840 74 -----SMLFQENNLFPHLTVAQNIGLGLR-PGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 417 PDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI-RSEGDPRVR 494
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALlDGEPPPALA 227
|
....
gi 2084914118 495 RFIG 498
Cdd:COG3840 228 AYLG 231
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
258-485 |
4.26e-57 |
|
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: 197.82 E-value: 4.26e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 258 ALLLRDIHKRY--GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSL---ESIDRGEIVLFGNDFIKAGKRDDAp 332
Cdd:COG1123 4 LLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSEALRG- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 333 virqgiRRIGMVFQNF--NLFPHrTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIA 410
Cdd:COG1123 83 ------RRIGMVFQDPmtQLNPV-TVGDQIAEALENLGL-SRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2084914118 411 RALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI 485
Cdd:COG1123 155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
259-477 |
8.85e-57 |
|
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: 188.23 E-value: 8.85e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDdapvirqgi 338
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRIGMVFQNFNLFPHRTILDNVILAPRYHGlADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPD 418
Cdd:cd03301 72 RDIAMVFQNYALYPHMTVYDNIAFGLKLRK-VPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 419 IMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| ArtM |
COG4160 |
ABC-type arginine/histidine transport system, permease component [Amino acid transport and ... |
3-220 |
2.09e-56 |
|
ABC-type arginine/histidine transport system, permease component [Amino acid transport and metabolism];
Pssm-ID: 443325 [Multi-domain] Cd Length: 229 Bit Score: 187.61 E-value: 2.09e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 3 FDWAYFFSlfSVSAFWKACLTVVQLSTLSWSIGLVLGFLLASAKLSGHAWLRMPASFYIWLFRSIPLLVLLVFVYN-LPQ 81
Cdd:COG4160 1 MDLDLLFE--YLPLLLSGLPLTLQLLALSLLLGFLLAVPLALARASGNRLLRWPARGYIYVFRGTPLLVQLFLIYYgLGQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 82 LFPVTGSVL----SQPFYSGLIALVLTETAYMAEIHRGGLLSVLKGQREAAKALGIRGVGAQRLVIIPQAIRISLPTLTN 157
Cdd:COG4160 79 FEWVRESWLwpllRDPWFCALLALTLNTAAYTAEIFRGAIRAVPKGEIEAARALGMSRWQTFRRIILPSALRRALPAYSN 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 158 EYVTIVKLTSLVSVISLNELLLVGQRLYAQNFLVLETLAAVAIYYVLIVTLFGWLLQWAERHL 220
Cdd:COG4160 159 EVILMLKATALASTITVMDLTGVARRIYSRTYDPFEPFLIAALIYLVITFLLTRLFRLLERRL 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
258-488 |
2.71e-56 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 187.99 E-value: 2.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 258 ALLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfikagkrddapvIRQG 337
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP------------PRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 338 IRRIGMVFQNFNL---FPhRTILDnVILAPRYHGLA----DSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIA 410
Cdd:COG1121 74 RRRIGYVPQRAEVdwdFP-ITVRD-VVLMGRYGRRGlfrrPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 411 RALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMeNGHVVTDASPASIRSE 488
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTP 228
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
261-471 |
4.67e-56 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 185.90 E-value: 4.67e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDAPVIRQgirR 340
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRRE---K 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 IGMVFQNFNLFPHRTILDNVILAPRYHGLADSaELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIM 420
Cdd:TIGR03608 78 LGYLFQNFALIENETVEENLDLGLKYKKLSKK-EKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2084914118 421 LFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFAlSISDRIVFM 471
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVA-KQADRVIEL 206
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
261-476 |
1.91e-55 |
|
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: 182.98 E-value: 1.91e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRddapvIRqgiRR 340
Cdd:cd03230 3 VRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE-----VK---RR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 IGMVFQNFNLFPHRTILDNVilapryhgladsaelrrkghglldrvgllahahkyphQLSGGQQQRVAIARALAMEPDIM 420
Cdd:cd03230 75 IGYLPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2084914118 421 LFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHV 476
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
261-488 |
2.27e-55 |
|
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: 185.45 E-value: 2.27e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfikagKRDDAPVIRqgiRR 340
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED-----VRKEPREAR---RQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 IGMVFQNFNLFPHRTILDNVILAPRYHGLADSaELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIM 420
Cdd:COG4555 76 IGVLPDERGLYDRLTVRENIRYFAELYGLFDE-ELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 421 LFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSE 488
Cdd:COG4555 155 LLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
259-476 |
5.20e-54 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 180.78 E-value: 5.20e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFikagKRDDAPVIRqgi 338
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL----SAMPPPEWR--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRIGMVFQNFNLFPHrTILDNVILAPRYHGLADSAElrrKGHGLLDRVGLLAHAHKYP-HQLSGGQQQRVAIARALAMEP 417
Cdd:COG4619 74 RQVAYVPQEPALWGG-TVRDNLPFPFQLRERKFDRE---RALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 418 DIMLFDEPTSALDPELVGEVLNVIRDL-AREGMTMLIVTHEMDFALSISDRIVFMENGHV 476
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
259-488 |
8.25e-54 |
|
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: 180.71 E-value: 8.25e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFikAGKRDDApVIRQGI 338
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDI--TGLPPHE-RARAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 rriGMVFQNFNLFPHRTILDNVILApryhgladsAELRRKGHG--LLDRV-----GLLAHAHKYPHQLSGGQQQRVAIAR 411
Cdd:cd03224 78 ---GYVPEGRRIFPELTVEENLLLG---------AYARRRAKRkaRLERVyelfpRLKERRKQLAGTLSGGEQQMLAIAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 412 ALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSE 488
Cdd:cd03224 146 ALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
264-498 |
1.24e-53 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 184.52 E-value: 1.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 264 IHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDdapvirqgiRRIGM 343
Cdd:PRK10851 8 IKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD---------RKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 344 VFQNFNLFPHRTILDNVILA----PRyHGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDI 419
Cdd:PRK10851 79 VFQHYALFRHMTVFDNIAFGltvlPR-RERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 420 MLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSEGDPR-VRRFI 497
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRfVLEFM 237
|
.
gi 2084914118 498 G 498
Cdd:PRK10851 238 G 238
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
253-477 |
2.50e-53 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 183.01 E-value: 2.50e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 253 PGQPDALL-LRDIHKRY--------GNHEVLK---GIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGN 320
Cdd:COG4608 1 AAMAEPLLeVRDLKKHFpvrgglfgRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 321 DFIKAGKRDDAPViRqgiRRIGMVFQN----FNlfPHRTILDNVILAPRYHGLADSAELRRKGHGLLDRVGLLA-HAHKY 395
Cdd:COG4608 81 DITGLSGRELRPL-R---RRMQMVFQDpyasLN--PRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPeHADRY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 396 PHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEmdfaLS----ISDRIVF 470
Cdd:COG4608 155 PHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHD----LSvvrhISDRVAV 230
|
....*..
gi 2084914118 471 MENGHVV 477
Cdd:COG4608 231 MYLGKIV 237
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
271-490 |
3.85e-53 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 180.73 E-value: 3.85e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 271 HEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfIKAGKRDDAPVIRqgiRRIGMVFQnfnl 350
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRD-ITAKKKKKLKDLR---KKVGLVFQ---- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 351 FPH-----RTILDNVILAPRYHGLADsAELRRKGHGLLDRVGL-LAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDE 424
Cdd:TIGR04521 90 FPEhqlfeETVYKDIAFGPKNLGLSE-EEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDE 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 425 PTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSEGD 490
Cdd:TIGR04521 169 PTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
261-474 |
1.70e-52 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 177.06 E-value: 1.70e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRY-GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAgKRDDAPVIRqgiR 339
Cdd:TIGR02673 4 FHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRL-RGRQLPLLR---R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 340 RIGMVFQNFNLFPHRTILDNVILAPRYHGlADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDI 419
Cdd:TIGR02673 80 RIGVVFQDFRLLPDRTVYENVALPLEVRG-KKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2084914118 420 MLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENG 474
Cdd:TIGR02673 159 LLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
257-496 |
5.11e-51 |
|
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: 173.63 E-value: 5.11e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 257 DALL-LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAgkrddAP--V 333
Cdd:COG0410 1 MPMLeVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGL-----PPhrI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 334 IRQGIrriGMVFQNFNLFPHRTILDNVILAPRYHGLadsaelRRKGHGLLDRVG-----LLAHAHKYPHQLSGGQQQRVA 408
Cdd:COG0410 76 ARLGI---GYVPEGRRIFPSLTVEENLLLGAYARRD------RAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 409 IARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSe 488
Cdd:COG0410 147 IGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA- 225
|
....*...
gi 2084914118 489 gDPRVRRF 496
Cdd:COG0410 226 -DPEVREA 232
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
267-477 |
1.61e-50 |
|
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: 171.56 E-value: 1.61e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 267 RYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfikagkrddapvIRQGIRRIGMVFQ 346
Cdd:cd03235 8 SYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP------------LEKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 347 NFNL---FPhRTILDNVILAPRYHGLAD---SAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIM 420
Cdd:cd03235 76 RRSIdrdFP-ISVRDVVLMGLYGHKGLFrrlSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 421 LFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMeNGHVV 477
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL-NRTVV 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
256-485 |
3.85e-50 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 178.67 E-value: 3.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 256 PDALL-LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDdapVI 334
Cdd:COG1129 1 AEPLLeMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD---AQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 335 RQGIrriGMVFQNFNLFPHRTILDNVILA--PRYHGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARA 412
Cdd:COG1129 78 AAGI---AIIHQELNLVPNLSVAENIFLGrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 413 LAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI 485
Cdd:COG1129 155 LSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
261-477 |
4.52e-50 |
|
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: 169.15 E-value: 4.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDApvirqgiRR 340
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA-------RK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 IGMVFQnfnlfphrtildnvilapryhgladsaelrrkghgLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIM 420
Cdd:cd03214 75 IAYVPQ-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPIL 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 421 LFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:cd03214 120 LLDEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
289-498 |
6.59e-50 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 173.83 E-value: 6.59e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 289 IIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAgkrddAPVIRQgirrIGMVFQNFNLFPHRTILDNVILAPRYHG 368
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNV-----PPHLRH----INMVFQSYALFPHMTVEENVAFGLKMRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 369 LaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE- 447
Cdd:TIGR01187 72 V-PRAEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQl 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2084914118 448 GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSEGDPR-VRRFIG 498
Cdd:TIGR01187 151 GITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLfVARFIG 202
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
255-482 |
1.61e-49 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 173.37 E-value: 1.61e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 255 QPDALLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGkrddapvI 334
Cdd:PRK11432 3 QKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS-------I 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 335 RQgiRRIGMVFQNFNLFPHRTILDNVILAPRYHGLAdSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALA 414
Cdd:PRK11432 76 QQ--RDICMVFQSYALFPHMSLGENVGYGLKMLGVP-KEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2084914118 415 MEPDIMLFDEPTSALDPELVGEVLNVIRDL-AREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASP 482
Cdd:PRK11432 153 LKPKVLLFDEPLSNLDANLRRSMREKIRELqQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSP 221
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
260-477 |
2.28e-49 |
|
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: 168.63 E-value: 2.28e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 260 LLRDIHKRYGNHEvLKgIDLVVkPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDAPVIRqgiR 339
Cdd:cd03297 2 LCVDIEKRLPDFT-LK-IDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQ---R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 340 RIGMVFQNFNLFPHRTILDNVILAPRYHglaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDI 419
Cdd:cd03297 76 KIGLVFQQYALFPHLNVRENLAFGLKRK---RNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPEL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2084914118 420 MLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:cd03297 153 LLLDEPFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
263-501 |
1.36e-48 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 171.05 E-value: 1.36e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 263 DIHKRYGNHEVlkGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDAPVIRqgiRRIG 342
Cdd:COG4148 6 DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPHR---RRIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 343 MVFQNFNLFPHRTILDNVilapRYhGLADSAELRRKGHglLDRV----GLLAHAHKYPHQLSGGQQQRVAIARALAMEPD 418
Cdd:COG4148 81 YVFQEARLFPHLSVRGNL----LY-GRKRAPRAERRIS--FDEVvellGIGHLLDRRPATLSGGERQRVAIGRALLSSPR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 419 IMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSegDPRVRRFI 497
Cdd:COG4148 154 LLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS--RPDLLPLA 231
|
....
gi 2084914118 498 GLEQ 501
Cdd:COG4148 232 GGEE 235
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
273-475 |
2.70e-48 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 166.05 E-value: 2.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 273 VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDdapviRQGIRR--IGMVFQNFNL 350
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLSYSQ-----KIILRRelIGYIFQSFNL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 351 FPHRTILDNVILAPRYHGLADSAELRRKGHgLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALD 430
Cdd:NF038007 95 IPHLSIFDNVALPLKYRGVAKKERIERVNQ-VLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2084914118 431 PELVGEVLNVIRDLAREGMTMLIVTHEmDFALSISDRIVFMENGH 475
Cdd:NF038007 174 SKNARAVLQQLKYINQKGTTIIMVTHS-DEASTYGNRIINMKDGK 217
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
261-475 |
6.31e-48 |
|
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: 162.80 E-value: 6.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGkrddapvIRQGIRR 340
Cdd:cd00267 2 IENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP-------LEELRRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 IGMVFQnfnlfphrtildnvilapryhgladsaelrrkghglldrvgllahahkyphqLSGGQQQRVAIARALAMEPDIM 420
Cdd:cd00267 75 IGYVPQ----------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2084914118 421 LFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGH 475
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| PhnT |
TIGR03258 |
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ... |
267-498 |
7.38e-48 |
|
2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.
Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 169.40 E-value: 7.38e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 267 RYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESID--RGEIVLFGNDFIKAgkrddaPVIRQGIrriGMV 344
Cdd:TIGR03258 14 AYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAglTGRIAIADRDLTHA------PPHKRGL---ALL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 345 FQNFNLFPHRTILDNVILAPRYHGLAdSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDE 424
Cdd:TIGR03258 85 FQNYALFPHLKVEDNVAFGLRAQKMP-KADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 425 PTSALDPELVGEVLNVIRDLARE--GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI-RSEGDPRVRRFIG 498
Cdd:TIGR03258 164 PLSALDANIRANMREEIAALHEElpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALyDAPADGFAAEFLG 240
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
261-500 |
8.35e-48 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 166.73 E-value: 8.35e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHE--VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNdfikagKRDDAPV--IRq 336
Cdd:PRK13635 8 VEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM------VLSEETVwdVR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 337 giRRIGMVFQN-FNLFPHRTILDNVILAPRYHGLADSaELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAM 415
Cdd:PRK13635 81 --RQVGMVFQNpDNQFVGATVQDDVAFGLENIGVPRE-EMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 416 EPDIMLFDEPTSALDPELVGEVLNVIRDLAREGM-TMLIVTHEMDFALSiSDRIVFMENGHVVTDASPASIRSEGDPRVR 494
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSGHMLQE 236
|
....*.
gi 2084914118 495 rfIGLE 500
Cdd:PRK13635 237 --IGLD 240
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
273-485 |
2.42e-47 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 166.41 E-value: 2.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 273 VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGND--FIKAGKRDDAPVIRQGI------------ 338
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDekNKKKTKEKEKVLEKLVIqktrfkkikkik 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 ---RRIGMVFQ--NFNLFpHRTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGL-LAHAHKYPHQLSGGQQQRVAIARA 412
Cdd:PRK13651 102 eirRRVGVVFQfaEYQLF-EQTIEKDIIFGPVSMGV-SKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 413 LAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI 485
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDI 252
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
259-500 |
6.68e-47 |
|
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: 162.89 E-value: 6.68e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEvLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIkagkrdDAPVIRqgi 338
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDIT------NLPPEK--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRIGMVFQNFNLFPHRTILDNVILAPRyHGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPD 418
Cdd:cd03299 71 RDISYVPQNYALFPHMTVYKNIAYGLK-KRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 419 IMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSEGDP-RVRRF 496
Cdd:cd03299 150 ILLLDEPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNeFVAEF 229
|
....
gi 2084914118 497 IGLE 500
Cdd:cd03299 230 LGFN 233
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
254-483 |
1.04e-46 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 169.44 E-value: 1.04e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 254 GQPDALLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDdApv 333
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRD-A-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 334 IRQGIrriGMVFQNFNLFPHRTILDNVILA--PRYHGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIAR 411
Cdd:COG3845 78 IALGI---GMVHQHFMLVPNLTVAENIVLGlePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILK 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084914118 412 ALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPA 483
Cdd:COG3845 155 ALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTA 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
263-477 |
6.70e-46 |
|
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: 159.34 E-value: 6.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 263 DIHKRYG-NHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIvLFGNDFIKAGKRddapvirqgIRRI 341
Cdd:cd03226 4 NISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSI-LLNGKPIKAKER---------RKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 342 GMVFQN--FNLFpHRTILDNVILapryhGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDI 419
Cdd:cd03226 74 GYVMQDvdYQLF-TDSVREELLL-----GLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 420 MLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
262-490 |
6.85e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 161.40 E-value: 6.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 262 RDIHKRYGN-HEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfIKAGKRDDAPViRQgirR 340
Cdd:PRK13639 5 RDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEP-IKYDKKSLLEV-RK---T 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 IGMVFQNFN--LFPhRTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPD 418
Cdd:PRK13639 80 VGIVFQNPDdqLFA-PTVEEDVAFGPLNLGL-SKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084914118 419 IMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSEGD 490
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
261-475 |
7.56e-46 |
|
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: 157.93 E-value: 7.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGN--HEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfIKAGKRDDapvIRqgi 338
Cdd:cd03228 3 FKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVD-LRDLDLES---LR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRIGMVFQNFNLFpHRTILDNVilapryhgladsaelrrkghglldrvgllahahkyphqLSGGQQQRVAIARALAMEPD 418
Cdd:cd03228 76 KNIAYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 419 IMLFDEPTSALDPELVGEVLNVIRDLaREGMTMLIVTHEMDfALSISDRIVFMENGH 475
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
261-476 |
2.19e-45 |
|
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: 158.34 E-value: 2.19e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEV-LKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAgKRDDAPVIRqgiR 339
Cdd:cd03292 3 FINVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDL-RGRAIPYLR---R 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 340 RIGMVFQNFNLFPHRTILDNVILAPRYHGlADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDI 419
Cdd:cd03292 79 KIGVVFQDFRLLPDRNVYENVAFALEVTG-VPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 420 MLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHV 476
Cdd:cd03292 158 LIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
261-479 |
2.50e-45 |
|
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: 158.04 E-value: 2.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGnhEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDdapvirqgiRR 340
Cdd:cd03298 3 LDKIRFSYG--EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD---------RP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 IGMVFQNFNLFPHRTILDNVILApRYHGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIM 420
Cdd:cd03298 72 VSMLFQENNLFAHLTVEQNVGLG-LSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 421 LFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTD 479
Cdd:cd03298 151 LLDEPFAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
259-477 |
3.79e-45 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 158.79 E-value: 3.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESID-----RGEIVLFGNDFIkaGKRDDAPV 333
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIY--SPRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 334 IRqgiRRIGMVFQNFNLFPHrTILDNVILAPRYHGLADSAELRR------KGHGLLDRVGllAHAHKYPHQLSGGQQQRV 407
Cdd:PRK14239 84 LR---KEIGMVFQQPNPFPM-SIYENVVYGLRLKGIKDKQVLDEavekslKGASIWDEVK--DRLHDSALGLSGGQQQRV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 408 AIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLaREGMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGL-KDDYTMLLVTRSMQQASRISDRTGFFLDGDLI 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
258-492 |
1.07e-44 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 159.12 E-value: 1.07e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 258 ALLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGndfikagkrddAPVIRQG 337
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG-----------EPLDPED 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 338 IRRIGMVFQNFNLFPHRTILDNVI-LApRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAME 416
Cdd:COG4152 70 RRRIGYLPEERGLYPKMKVGEQLVyLA-RLKGL-SKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHD 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2084914118 417 PDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSEGDPR 492
Cdd:COG4152 148 PELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRN 223
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
253-503 |
1.98e-44 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 157.15 E-value: 1.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 253 PGQPdaLLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIvLFGNdfikagkrddAP 332
Cdd:PRK11247 9 QGTP--LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGT----------AP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 333 V--IRQGIRrigMVFQNFNLFPHRTILDNVilapryhGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIA 410
Cdd:PRK11247 76 LaeAREDTR---LMFQDARLLPWKKVIDNV-------GLGLKGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 411 RALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRseg 489
Cdd:PRK11247 146 RALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDLTVDLPR--- 222
|
250
....*....|....*..
gi 2084914118 490 dPRVR---RFIGLEQEV 503
Cdd:PRK11247 223 -PRRRgsaRLAELEAEV 238
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
261-477 |
5.56e-44 |
|
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: 152.58 E-value: 5.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDapvIRQGIrr 340
Cdd:cd03216 3 LRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDA---RRAGI-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 iGMVfqnfnlfphrtildnvilapryhgladsaelrrkghglldrvgllahahkypHQLSGGQQQRVAIARALAMEPDIM 420
Cdd:cd03216 78 -AMV----------------------------------------------------YQLSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 421 LFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
263-482 |
7.98e-44 |
|
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: 154.06 E-value: 7.98e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 263 DIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKagkrdDAPVIRqgiRRIG 342
Cdd:cd03265 5 NLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-----EPREVR---RRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 343 MVFQNFNLFPHRTILDNVILAPRYHGLAdSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLF 422
Cdd:cd03265 77 IVFQDLSVDDELTGWENLYIHARLYGVP-GAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084914118 423 DEPTSALDPELVGEVLNVIRDL-AREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASP 482
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTP 216
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
261-480 |
2.03e-43 |
|
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: 152.76 E-value: 2.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKrddapvirqGIRR 340
Cdd:cd03268 3 TNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE---------ALRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 IGMVFQNFNLFPHRTILDNVILAPRYHGLADSAELRrkghgLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIM 420
Cdd:cd03268 74 IGALIEAPGFYPNLTARENLRLLARLLGIRKKRIDE-----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 421 LFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDA 480
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
258-505 |
3.70e-43 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 153.86 E-value: 3.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 258 ALLLRDIHKRYGN----HEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLfgndfikagkrDDAPV 333
Cdd:COG4525 3 MLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITL-----------DGVPV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 334 IRQGIRRiGMVFQNFNLFPHRTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARAL 413
Cdd:COG4525 72 TGPGADR-GVVFQKDALLPWLNVLDNVAFGLRLRGV-PKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 414 AMEPDIMLFDEPTSALDP---ELVGEVLnvIRDLAREGMTMLIVTHEMDFALSISDRIVFMEN--GHVVTDASP------ 482
Cdd:COG4525 150 AADPRFLLMDEPFGALDAltrEQMQELL--LDVWQRTGKGVFLITHSVEEALFLATRLVVMSPgpGRIVERLELdfsrrf 227
|
250 260
....*....|....*....|....*..
gi 2084914118 483 ---ASIRS-EGDPrvrRFIGLEQEVTA 505
Cdd:COG4525 228 lagEDARAiKSDP---AFIALREELLD 251
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
264-488 |
6.47e-43 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 153.24 E-value: 6.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 264 IHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDR---GEIVLFGNDFIKAGK--RDdapvIRQGI 338
Cdd:PRK09984 10 LAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREGRlaRD----IRKSR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRIGMVFQNFNLFPHRTILDNVILA-----PRYHGLADSAELRRKGHGL--LDRVGLLAHAHKYPHQLSGGQQQRVAIAR 411
Cdd:PRK09984 86 ANTGYIFQQFNLVNRLSVLENVLIGalgstPFWRTCFSWFTREQKQRALqaLTRVGMVHFAHQRVSTLSGGQQQRVAIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 412 ALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAR-EGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSE 488
Cdd:PRK09984 166 ALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNE 243
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
269-477 |
1.03e-42 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 159.08 E-value: 1.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 269 GNHEVLKGIDLVVKPGEVISIIGPSGSGKT----SLIRTINSLESIDRGEIVLFGNDFIKAGKRDdapviRQGIR--RIG 342
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERE-----LRRIRgnRIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 343 MVFQ------NfnlfPHRTILDNVILAPRYHGLADSAELRRKGHGLLDRVGLLAHAHK---YPHQLSGGQQQRVAIARAL 413
Cdd:COG4172 96 MIFQepmtslN----PLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRldaYPHQLSGGQRQRVMIAMAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 414 AMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHemDFAL--SISDRIVFMENGHVV 477
Cdd:COG4172 172 ANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITH--DLGVvrRFADRVAVMRQGEIV 236
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
244-477 |
1.33e-42 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 158.69 E-value: 1.33e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 244 ASKKRNEPVPGQPDA---LLLRDIHKRY-----------GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLES 309
Cdd:COG4172 258 AAEPRGDPRPVPPDApplLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 310 iDRGEIVLFGNDFIKAGKRDDAPViRqgiRRIGMVFQN----FNlfPHRTILDnvILAP--RYHGLA-DSAELRRKGHGL 382
Cdd:COG4172 338 -SEGEIRFDGQDLDGLSRRALRPL-R---RRMQVVFQDpfgsLS--PRMTVGQ--IIAEglRVHGPGlSAAERRARVAEA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 383 LDRVGLL-AHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDF 460
Cdd:COG4172 409 LEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAV 488
|
250
....*....|....*..
gi 2084914118 461 ALSISDRIVFMENGHVV 477
Cdd:COG4172 489 VRALAHRVMVMKDGKVV 505
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
274-474 |
1.69e-42 |
|
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: 151.08 E-value: 1.69e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 274 LKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNdfikagkrddaPVIRQGIRRIgMVFQNFNLFPH 353
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK-----------QITEPGPDRM-VVFQNYSLLPW 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 354 RTILDNVILA-PRYHGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDP- 431
Cdd:TIGR01184 69 LTVRENIALAvDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDAl 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2084914118 432 ---ELVGEVLNVIRDlarEGMTMLIVTHEMDFALSISDRIVFMENG 474
Cdd:TIGR01184 149 trgNLQEELMQIWEE---HRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
278-487 |
1.88e-42 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 150.89 E-value: 1.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 278 DLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAgkrddaPVIRqgiRRIGMVFQNFNLFPHRTIL 357
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTT------PPSR---RPVSMLFQENNLFSHLTVA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 358 DNVIL--APryhGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVG 435
Cdd:PRK10771 90 QNIGLglNP---GLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQ 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 436 EVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRS 487
Cdd:PRK10771 167 EMLTLVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
258-477 |
1.91e-42 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 151.53 E-value: 1.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 258 ALLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESID-----RGEIVLFGNDfIKAGKRDDAP 332
Cdd:PRK14267 4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRN-IYSPDVDPIE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 333 VIRqgirRIGMVFQNFNLFPHRTILDNVILAPRYHGLADS-AELRRKGHGLLDRVGLLAHA----HKYPHQLSGGQQQRV 407
Cdd:PRK14267 83 VRR----EVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSkKELDERVEWALKKAALWDEVkdrlNDYPSNLSGGQRQRL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 408 AIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREgMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLI 227
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
205-483 |
2.35e-42 |
|
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: 160.38 E-value: 2.35e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 205 IVTLFGWLLQWAERHLDLSRknartLDDTQAQALRQPASASKKRNEPVPGqpdALLLRDIHKRYGNHE--VLKGIDLVVK 282
Cdd:COG2274 428 VAQLIGLLQRFQDAKIALER-----LDDILDLPPEREEGRSKLSLPRLKG---DIELENVSFRYPGDSppVLDNISLTIK 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 283 PGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFikagkRD-DAPVIRqgiRRIGMVFQNFNLFpHRTILDNVI 361
Cdd:COG2274 500 PGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDL-----RQiDPASLR---RQIGVVLQDVFLF-SGTIRENIT 570
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 362 LApryHGLADSAELRRkghgLLDRVGLLAHAHKYPH-----------QLSGGQQQRVAIARALAMEPDIMLFDEPTSALD 430
Cdd:COG2274 571 LG---DPDATDEEIIE----AARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLRNPRILILDEATSALD 643
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 431 PELVGEVLNVIRDLAReGMTMLIVTHEMDfALSISDRIVFMENGHVVTDASPA 483
Cdd:COG2274 644 AETEAIILENLRRLLK-GRTVIIIAHRLS-TIRLADRIIVLDKGRIVEDGTHE 694
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
274-427 |
3.66e-42 |
|
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: 147.41 E-value: 3.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 274 LKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFikagKRDDAPVIRqgiRRIGMVFQNFNLFPH 353
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDL----TDDERKSLR---KEIGYVFQDPQLFPR 73
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 354 RTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGLLA----HAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTS 427
Cdd:pfam00005 74 LTVRENLRLGLLLKGL-SKREKDARAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
274-485 |
4.82e-42 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 154.81 E-value: 4.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 274 LKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDAPVIRqgiRRIGMVFQNFNLFPH 353
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRR---KKIAMVFQSFALMPH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 354 RTILDNVILAPRYHGLAdSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPEL 433
Cdd:PRK10070 121 MTVLDNTAFGMELAGIN-AEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 434 VGEVLNVIRDL-AREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI 485
Cdd:PRK10070 200 RTEMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
264-477 |
1.15e-41 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 148.48 E-value: 1.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 264 IHKRY-GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfIKAGKRDDAPVIRqgiRRIG 342
Cdd:PRK10908 7 VSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHD-ITRLKNREVPFLR---RQIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 343 MVFQNFNLFPHRTILDNVILaPRYHGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLF 422
Cdd:PRK10908 83 MIFQDHHLLMDRTVYDNVAI-PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2084914118 423 DEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
261-497 |
1.24e-41 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 149.92 E-value: 1.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIvLFGNDFIKAGKRDDAPVIRqgiRR 340
Cdd:PRK11831 10 MRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEI-LFDGENIPAMSRSRLYTVR---KR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 IGMVFQNFNLFPHRTILDNVILAPRYHGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIM 420
Cdd:PRK11831 86 MSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 421 LFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSEGDPRVRRFI 497
Cdd:PRK11831 166 MFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRVRQFL 243
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
237-498 |
1.82e-41 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 152.68 E-value: 1.82e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 237 ALRQPASASKKRNEPVpgqpdaLLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIV 316
Cdd:PRK11607 4 AIPRPQAKTRKALTPL------LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 317 LFGNDFikagkrDDAPVIRqgiRRIGMVFQNFNLFPHRTILDNVILAPRYHGLAdSAELRRKGHGLLDRVGLLAHAHKYP 396
Cdd:PRK11607 78 LDGVDL------SHVPPYQ---RPINMMFQSYALFPHMTVEQNIAFGLKQDKLP-KAEIASRVNEMLGLVHMQEFAKRKP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 397 HQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEV-LNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGH 475
Cdd:PRK11607 148 HQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGK 227
|
250 260
....*....|....*....|....
gi 2084914118 476 VVTDASPASIRSEGDPRVR-RFIG 498
Cdd:PRK11607 228 FVQIGEPEEIYEHPTTRYSaEFIG 251
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
259-457 |
5.03e-41 |
|
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: 146.08 E-value: 5.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfikagKRDDAPVIRqgi 338
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEP-----IRDAREDYR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRIGMVFQNFNLFPHRTILDNVILAPRYHGLADSAELRRKghgLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPD 418
Cdd:COG4133 75 RRLAYLGHADGLKPELTVRENLRFWAALYGLRADREAIDE---ALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 2084914118 419 IMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHE 457
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
263-490 |
6.14e-41 |
|
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: 150.65 E-value: 6.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 263 DIHKRYGNHEVlkGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDAPVIRqgiRRIG 342
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEK---RRIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 343 MVFQNFNLFPHRTILDNVilapRYhGL--ADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIM 420
Cdd:TIGR02142 79 YVFQEARLFPHLSVRGNL----RY-GMkrARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084914118 421 LFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSEGD 490
Cdd:TIGR02142 154 LMDEPLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
266-495 |
6.26e-41 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 149.08 E-value: 6.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 266 KRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKagkrdDAPVIRqgiRRIGMVF 345
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVR-----EPRKVR---RSIGIVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 346 QNFNLFPHRTILDNVILAPRYHGLADSaELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEP 425
Cdd:TIGR01188 73 QYASVDEDLTGRENLEMMGRLYGLPKD-EAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEP 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 426 TSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSEGDPRVRR 495
Cdd:TIGR01188 152 TTGLDPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLGKDTLE 221
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
259-495 |
6.45e-41 |
|
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: 146.92 E-value: 6.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAgkrddaPVIRQGI 338
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL------PMHKRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRIGMVFQNFNLFPHRTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPD 418
Cdd:cd03218 75 LGIGYLPQEASIFRKLTVEENILAVLEIRGL-SKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 419 IMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSegDPRVRR 495
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAA--NELVRK 228
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
259-477 |
1.44e-40 |
|
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: 145.12 E-value: 1.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNdfikagkrddaPVIRQGI 338
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK-----------PLDIAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRIGMVFQNFNLFPHRTILDNVILAPRYHGLADSaELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPD 418
Cdd:cd03269 70 NRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKE-EARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2084914118 419 IMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:cd03269 149 LLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAV 207
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
270-505 |
1.58e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 147.19 E-value: 1.58e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 270 NHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDdapvIRqgiRRIGMVFQN-F 348
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWD----IR---HKIGMVFQNpD 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 349 NLFPHRTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSA 428
Cdd:PRK13650 92 NQFVGATVEDDVAFGLENKGI-PHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSM 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 429 LDPELVGEVLNVIRDLARE-GMTMLIVTHEMDfALSISDRIVFMENGHVVTDASPASIRSEGDPRVRrfIGLEQEVTA 505
Cdd:PRK13650 171 LDPEGRLELIKTIKGIRDDyQMTVISITHDLD-EVALSDRVLVMKNGQVESTSTPRELFSRGNDLLQ--LGLDIPFTT 245
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
259-486 |
2.52e-40 |
|
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: 144.96 E-value: 2.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHE--VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfikagKRDDAPVIRQ 336
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYS-----IRTDRKAARQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 337 girRIGMVFQNFNLFPHRTILDNVILAPRYHGLADSaELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAME 416
Cdd:cd03263 76 ---SLGYCPQFDALFDELTVREHLRFYARLKGLPKS-EIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 417 PDIMLFDEPTSALDPELVGEVLNVIRDLaREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIR 486
Cdd:cd03263 152 PSVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQELK 220
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
216-496 |
3.51e-40 |
|
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: 152.61 E-value: 3.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 216 AERHLDLSRKNARTLDDTQAQAlrqPASASKKRNEPVPGQPDaLLLRDIHKRY--GNHEVLKGIDLVVKPGEVISIIGPS 293
Cdd:COG4987 295 AAQHLGRVRAAARRLNELLDAP---PAVTEPAEPAPAPGGPS-LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPS 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 294 GSGKTSLIRTINSLESIDRGEIVLFGNDFikagKRDDAPVIRqgiRRIGMVFQNFNLFpHRTILDNVILA-PRyhglADS 372
Cdd:COG4987 371 GSGKSTLLALLLRFLDPQSGSITLGGVDL----RDLDEDDLR---RRIAVVPQRPHLF-DTTLRENLRLArPD----ATD 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 373 AELRRkghgLLDRVGLLAHAHKYPH-----------QLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVI 441
Cdd:COG4987 439 EELWA----ALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADL 514
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2084914118 442 RDLAReGMTMLIVTHEMDfALSISDRIVFMENGHVVTDASPASIRsEGDPRVRRF 496
Cdd:COG4987 515 LEALA-GRTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEELL-AQNGRYRQL 566
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
274-490 |
4.39e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 146.35 E-value: 4.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 274 LKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLfgNDFIKAGKRDDAPVIRqgiRRIGMVFQ--NFNLF 351
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIII--DGVDITDKKVKLSDIR---KKVGLVFQypEYQLF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 352 pHRTILDNVILAPRYHGLADSaELRRKGHGLLDRVGL--LAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSAL 429
Cdd:PRK13637 98 -EETIEKDIAFGPINLGLSEE-EIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084914118 430 DPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSEGD 490
Cdd:PRK13637 176 DPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVE 237
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
270-488 |
4.92e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 146.00 E-value: 4.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 270 NHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDapvIRQgirRIGMVFQNfn 349
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWD---IRN---KAGMVFQN-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 350 lfPHRTIL-----DNVILAPRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDE 424
Cdd:PRK13633 94 --PDNQIVativeEDVAFGPENLGI-PPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084914118 425 PTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSiSDRIVFMENGHVVTDASPASIRSE 488
Cdd:PRK13633 171 PTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
259-477 |
5.77e-40 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 145.06 E-value: 5.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSL-----ESIDRGEIVLFGNDFIKAgkrdDAPV 333
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKM----DVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 334 IRqgiRRIGMVFQNFNLFPHRTILDNVILAPRYHGLADS-AELRRKGHGLLDRVGLLAHAHKY----PHQLSGGQQQRVA 408
Cdd:PRK14247 80 LR---RRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSkKELQERVRWALEKAQLWDEVKDRldapAGKLSGGQQQRLC 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2084914118 409 IARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREgMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIV 224
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
259-497 |
6.43e-40 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 144.20 E-value: 6.43e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDApviRQGI 338
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERA---RAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 rriGMVFQNFNLFPHRTILDNVILapryhGLAdsaELRRKGHGLLDRV-----GLLAHAHKYPHQLSGGQQQRVAIARAL 413
Cdd:TIGR03410 78 ---AYVPQGREIFPRLTVEENLLT-----GLA---ALPRRSRKIPDEIyelfpVLKEMLGRRGGDLSGGQQQQLAIARAL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 414 AMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIrseGDPR 492
Cdd:TIGR03410 147 VTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL---DEDK 223
|
....*
gi 2084914118 493 VRRFI 497
Cdd:TIGR03410 224 VRRYL 228
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
240-488 |
7.31e-40 |
|
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: 151.11 E-value: 7.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 240 QPASASKKRNEPVPGQPdALLLRDIHKRY-----GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGE 314
Cdd:TIGR03269 262 EGVSEVEKECEVEVGEP-IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 315 I-VLFGNDFIKAGKRddAPVIR-QGIRRIGMVFQNFNLFPHRTILDNVILAPryhGLADSAEL-RRKGHGLLDRVGLLAH 391
Cdd:TIGR03269 341 VnVRVGDEWVDMTKP--GPDGRgRAKRYIGILHQEYDLYPHRTVLDNLTEAI---GLELPDELaRMKAVITLKMVGFDEE 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 392 A-----HKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDlAREGM--TMLIVTHEMDFALSI 464
Cdd:TIGR03269 416 KaeeilDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILK-AREEMeqTFIIVSHDMDFVLDV 494
|
250 260
....*....|....*....|....
gi 2084914118 465 SDRIVFMENGHVVTDASPASIRSE 488
Cdd:TIGR03269 495 CDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
258-476 |
9.47e-40 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 147.30 E-value: 9.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 258 ALLLRDIHKRY-GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDdapvirq 336
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 337 giRRIGMVFQNFNLFPHRTILDNVILAPRYHGLADSAELRRKGH--------GLLDRvgllahahkYPHQLSGGQQQRVA 408
Cdd:PRK11650 76 --RDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEaarilelePLLDR---------KPRELSGGQRQRVA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2084914118 409 IARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHV 476
Cdd:PRK11650 145 MGRAIVREPAVFLFDEPLSNLDAKLRVQMRLEIQRLHRRlKTTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
238-489 |
2.89e-39 |
|
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: 149.91 E-value: 2.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 238 LRQPASASKKRNEPVP-GQPDALLLRDIHKRY-GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEI 315
Cdd:COG4988 315 LDAPEPAAPAGTAPLPaAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSI 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 316 VLFGNDFikagKRDDAPVIRqgiRRIGMVFQNFNLFpHRTILDNVILApryHGLADSAELRRkghgLLDRVGLLAHAHKY 395
Cdd:COG4988 395 LINGVDL----SDLDPASWR---RQIAWVPQNPYLF-AGTIRENLRLG---RPDASDEELEA----ALEAAGLDEFVAAL 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 396 PH-----------QLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAReGMTMLIVTHEMDfALSI 464
Cdd:COG4988 460 PDgldtplgeggrGLSGGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK-GRTVILITHRLA-LLAQ 537
|
250 260
....*....|....*....|....*
gi 2084914118 465 SDRIVFMENGHVVTDASPASIRSEG 489
Cdd:COG4988 538 ADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
165-477 |
3.72e-39 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 149.93 E-value: 3.72e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 165 LTSLVSVISLNELLLVGQRLYAQNFLVLETLAAVAIYyvliVTLFGWLLQWAERHLDLSRKNARTLDDTQAQALRQPASA 244
Cdd:COG1132 250 LMELLGNLGLALVLLVGGLLVLSGSLTVGDLVAFILY----LLRLFGPLRQLANVLNQLQRALASAERIFELLDEPPEIP 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 245 SKKRNEPVPGQPDALLLRDIHKRY-GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfI 323
Cdd:COG1132 326 DPPGAVPLPPVRGEIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVD-I 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 324 KAGKRDDapvIRqgiRRIGMVFQNFNLFpHRTILDNVILA-PRyhglADSAELRR--KghglldrvglLAHAH----KYP 396
Cdd:COG1132 405 RDLTLES---LR---RQIGVVPQDTFLF-SGTIRENIRYGrPD----ATDEEVEEaaK----------AAQAHefieALP 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 397 H-----------QLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLaREGMTMLIVTHEmdfaLS-- 463
Cdd:COG1132 464 DgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERL-MKGRTTIVIAHR----LSti 538
|
330
....*....|....*
gi 2084914118 464 -ISDRIVFMENGHVV 477
Cdd:COG1132 539 rNADRILVLDDGRIV 553
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
259-493 |
3.93e-39 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 142.82 E-value: 3.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFikAGKRDdapvirQGI 338
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI--EGLPG------HQI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRIGMV--FQNFNLFPHRTILDNVILAPRYH-------GLADSAELRR-------KGHGLLDRVGLLAHAHKYPHQLSGG 402
Cdd:PRK11300 78 ARMGVVrtFQHVRLFREMTVIENLLVAQHQQlktglfsGLLKTPAFRRaesealdRAATWLERVGLLEHANRQAGNLAYG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 403 QQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDAS 481
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
|
250
....*....|..
gi 2084914118 482 PASIRSegDPRV 493
Cdd:PRK11300 238 PEEIRN--NPDV 247
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
272-461 |
4.60e-39 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 140.64 E-value: 4.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 272 EVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfIKAGKRDdapvIRQGIRRIGMVFQNFN-- 349
Cdd:TIGR01166 6 EVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEP-LDYSRKG----LLERRQRVGLVFQDPDdq 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 350 LFpHRTILDNVILAPRYHGLADsAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSAL 429
Cdd:TIGR01166 81 LF-AADVDQDVAFGPLNLGLSE-AEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGL 158
|
170 180 190
....*....|....*....|....*....|..
gi 2084914118 430 DPELVGEVLNVIRDLAREGMTMLIVTHEMDFA 461
Cdd:TIGR01166 159 DPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
261-476 |
4.78e-39 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 145.56 E-value: 4.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIvlfgndFIKAGKRDDAPVIRQGIrr 340
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDL------FIGEKRMNDVPPAERGV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 iGMVFQNFNLFPHRTILDNVILAPRYHGlADSAELRRK----------GHgLLDRvgllahahkYPHQLSGGQQQRVAIA 410
Cdd:PRK11000 78 -GMVFQSYALYPHLSVAENMSFGLKLAG-AKKEEINQRvnqvaevlqlAH-LLDR---------KPKALSGGQRQRVAIG 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 411 RALAMEPDIMLFDEPTSALDPEL-VGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHV 476
Cdd:PRK11000 146 RTLVAEPSVFLLDEPLSNLDAALrVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
261-493 |
5.30e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 142.95 E-value: 5.30e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRY--GNHeVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDdapvIRQgi 338
Cdd:PRK13647 7 VEDLHFRYkdGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW----VRS-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 rRIGMVFQNFN--LFPhRTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAME 416
Cdd:PRK13647 80 -KVGLVFQDPDdqVFS-STVWDDVAFGPVNMGL-DKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 417 PDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVtdaspasirSEGDPRV 493
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVL---------AEGDKSL 224
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
274-490 |
9.99e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 142.85 E-value: 9.99e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 274 LKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLfGNDFIKAGKRD-DAPVIRQgirRIGMVFQnfnlFP 352
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITAGKKNkKLKPLRK---KVGIVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 353 -HR----TILDNVILAPRYHGLADsAELRRKGHGLLDRVGLLAHA-HKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPT 426
Cdd:PRK13634 95 eHQlfeeTVEKDICFGPMNFGVSE-EDAKQKAREMIELVGLPEELlARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084914118 427 SALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSEGD 490
Cdd:PRK13634 174 AGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
274-499 |
5.98e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 140.12 E-value: 5.98e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 274 LKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRddapvirQGIRRI-GMVFQNFNL-F 351
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKL-------QGIRKLvGIVFQNPETqF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 352 PHRTILDNVILAPRYHGLAdSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDP 431
Cdd:PRK13644 91 VGRTVEEDLAFGPENLCLP-PIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 432 ELVGEVLNVIRDLAREGMTMLIVTHEMDfALSISDRIVFMENGHVVTDASPASIRSegDPRVrRFIGL 499
Cdd:PRK13644 170 DSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLS--DVSL-QTLGL 233
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
259-479 |
6.54e-38 |
|
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: 138.27 E-value: 6.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHE----VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGkrddapvi 334
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 335 RQGIRRIGMVFQNFNLFPHRTILDNVILAPRYHGLAdSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALA 414
Cdd:cd03266 74 AEARRRLGFVSDSTGLYDRLTARENLEYFAGLYGLK-GDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084914118 415 MEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTD 479
Cdd:cd03266 153 HDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
258-483 |
6.62e-38 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 139.52 E-value: 6.62e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 258 ALLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfikagKRDDAPviRQG 337
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRP-----LADWSP--AEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 338 IRRIGMVFQNFNL-FPHRtiLDNVILAPRYHGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALA-- 414
Cdd:PRK13548 75 ARRRAVLPQHSSLsFPFT--VEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAql 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084914118 415 ----MEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPA 483
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPA 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
258-489 |
2.96e-37 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 145.25 E-value: 2.96e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 258 ALL-LRDIHKRYGNHE----VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfIKAGKRDDAP 332
Cdd:PRK10535 3 ALLeLKDIRRSYPSGEeqveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQD-VATLDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 333 VIRQgiRRIGMVFQNFNLFPHRTILDNVILAPRYHGLADSAELRRkGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARA 412
Cdd:PRK10535 82 QLRR--EHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLR-AQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARA 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 413 LAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSiSDRIVFMENGHVVTDaSPASIRSEG 489
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRN-PPAQEKVNV 233
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
261-485 |
3.78e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 137.81 E-value: 3.78e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHE--VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFikagKRDDAPVIRqgi 338
Cdd:PRK13632 10 VENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI----SKENLKEIR--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRIGMVFQN-FNLFPHRTILDNVILapryhGLA----DSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARAL 413
Cdd:PRK13632 83 KKIGIIFQNpDNQFIGATVEDDIAF-----GLEnkkvPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 414 AMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLI-VTHEMDFALsISDRIVFMENGHVVTDASPASI 485
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLIsITHDMDEAI-LADKVIVFSEGKLIAQGKPKEI 229
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
259-477 |
1.06e-36 |
|
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: 134.63 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGeVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAgkrddapviRQGI 338
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQ---------PQKL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RR-IGMVFQNFNLFPHRTILDNVILAPRYHGLADSaELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEP 417
Cdd:cd03264 71 RRrIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSK-EVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 418 DIMLFDEPTSALDPELVGEVLNVIRDLArEGMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLLSELG-EDRIVILSTHIVEDVESLCNQVAVLNKGKLV 208
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
267-476 |
2.69e-36 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 133.83 E-value: 2.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 267 RYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAgkrddAPVIRQgirrIGMVFQ 346
Cdd:TIGR01277 7 RYEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGL-----APYQRP----VSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 347 NFNLFPHRTILDNVILAPRyHGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPT 426
Cdd:TIGR01277 78 ENNLFAHLTVRQNIGLGLH-PGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPF 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2084914118 427 SALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHV 476
Cdd:TIGR01277 157 SALDPLLREEMLALVKQLCSErQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
256-479 |
4.17e-36 |
|
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: 134.44 E-value: 4.17e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 256 PDALLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRG-EIVLFGNDFIKAGKRDdapvI 334
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWE----L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 335 RqgiRRIGMV---FQNFnlFPHRTILDNVILAPRYH--GLAD--SAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRV 407
Cdd:COG1119 77 R---KRIGLVspaLQLR--FPRDETVLDVVLSGFFDsiGLYRepTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRV 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 408 AIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREG-MTMLIVTHEMDFALSISDRIVFMENGHVVTD 479
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAA 224
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
262-484 |
6.39e-36 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 134.09 E-value: 6.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 262 RDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDApvirqgiRRI 341
Cdd:COG4559 5 ENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELA-------RRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 342 GMVFQNFNL-FPHrTILDnVILAPRYHGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALA------ 414
Cdd:COG4559 78 AVLPQHSSLaFPF-TVEE-VVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepv 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084914118 415 -MEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPAS 484
Cdd:COG4559 156 dGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
275-477 |
7.60e-36 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 135.99 E-value: 7.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 275 KGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDdapvIRQGIRRIGMVFQN--FNLFP 352
Cdd:PRK15079 38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDE----WRAVRSDIQMIFQDplASLNP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 353 HRTILDnVILAP--RYHGLADSAELRRKGHGLLDRVGLLAHA-HKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSAL 429
Cdd:PRK15079 114 RMTIGE-IIAEPlrTYHPKLSRQEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2084914118 430 DPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 241
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
273-485 |
7.97e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 134.02 E-value: 7.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 273 VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDR------GEIVLFGNDFIkagkRDDAPVIRqgiRRIGMVFQ 346
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDskikvdGKVLYFGKDIF----QIDAIKLR---KEVGMVFQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 347 NFNLFPHRTILDNVILAPRYHGLADSAELRRKGHGLLDRVGLLAHAHKY----PHQLSGGQQQRVAIARALAMEPDIMLF 422
Cdd:PRK14246 98 QPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRlnspASQLSGGQQQRLTIARALALKPKVLLM 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 423 DEPTSALDPELVGEVLNVIRDLAREgMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI 485
Cdd:PRK14246 178 DEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
259-496 |
8.80e-36 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 133.23 E-value: 8.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGND------FIKAgkrddap 332
Cdd:COG1137 4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDithlpmHKRA------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 333 viRQGIrriGMVFQNFNLFPHRTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARA 412
Cdd:COG1137 77 --RLGI---GYLPQEASIFRKLTVEDNILAVLELRKL-SKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 413 LAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSegDPR 492
Cdd:COG1137 151 LATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILN--NPL 228
|
....
gi 2084914118 493 VRRF 496
Cdd:COG1137 229 VRKV 232
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
263-478 |
3.63e-35 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 134.62 E-value: 3.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 263 DIHKRYGNHevlkgiDLVVK---PGEVIS-IIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDAPVIRqgi 338
Cdd:PRK11144 5 NFKQQLGDL------CLTVNltlPAQGITaIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRIGMVFQNFNLFPHRTILDNVilapRYhGLADSaelrRKGHgLLDRVGLLAHAH---KYPHQLSGGQQQRVAIARALAM 415
Cdd:PRK11144 76 RRIGYVFQDARLFPHYKVRGNL----RY-GMAKS----MVAQ-FDKIVALLGIEPlldRYPGSLSGGEKQRVAIGRALLT 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084914118 416 EPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVT 478
Cdd:PRK11144 146 APELLLMDEPLASLDLPRKRELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKA 209
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
253-488 |
4.51e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 133.01 E-value: 4.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 253 PGQPDALLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAgkrddAP 332
Cdd:PRK13537 2 PMSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR-----AR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 333 VIRQgirRIGMVFQNFNLFPHRTILDNVILAPRYHGLAdSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARA 412
Cdd:PRK13537 77 HARQ---RVGVVPQFDNLDPDFTVRENLLVFGRYFGLS-AAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 413 LAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASP-ASIRSE 488
Cdd:PRK13537 153 LVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPhALIESE 229
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
274-492 |
5.27e-35 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 133.55 E-value: 5.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 274 LKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDapviRQGIRRIGMVFQN--FNLF 351
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQ----KLLRQKIQIVFQNpyGSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 352 PHRTILDnvILA-PryhgLA-----DSAELRRKGHGLLDRVGLLA-HAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDE 424
Cdd:PRK11308 107 PRKKVGQ--ILEeP----LLintslSAAERREKALAMMAKVGLRPeHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADE 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2084914118 425 PTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSegDPR 492
Cdd:PRK11308 181 PVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFN--NPR 247
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
259-473 |
1.32e-34 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 129.14 E-value: 1.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESID---RGEIVLFGNDfikagkRDDAPVIR 335
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRR------LTALPAEQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 336 qgiRRIGMVFQNFNLFPHRTILDNVI--LAPRYHGladsAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARAL 413
Cdd:COG4136 76 ---RRIGILFQDDLLFPHLSVGENLAfaLPPTIGR----AQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084914118 414 AMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISdRIVFMEN 473
Cdd:COG4136 149 LAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQrGIPALLVTHDEEDAPAAG-RVLDLGN 208
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
262-470 |
1.76e-34 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 130.29 E-value: 1.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 262 RDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESI-----DRGEIVLFGNDFIkaGKRDDAPVIRq 336
Cdd:PRK14243 14 ENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLY--APDVDPVEVR- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 337 giRRIGMVFQNFNLFPhRTILDNVILAPRYHGL-ADSAELRRKG---HGLLDRV-------GLlahahkyphQLSGGQQQ 405
Cdd:PRK14243 91 --RRIGMVFQKPNPFP-KSIYDNIAYGARINGYkGDMDELVERSlrqAALWDEVkdklkqsGL---------SLSGGQQQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084914118 406 RVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLaREGMTMLIVTHEMDFALSISDRIVF 470
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSDMTAF 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
256-488 |
2.63e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 130.35 E-value: 2.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 256 PDALL-LRDIHKRYGN-HEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIvLFGN---DFIKAGKRDd 330
Cdd:PRK13636 2 EDYILkVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRI-LFDGkpiDYSRKGLMK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 331 apvIRQGIrriGMVFQ--NFNLFPhRTILDNVILAPRYHGLADSaELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVA 408
Cdd:PRK13636 80 ---LRESV---GMVFQdpDNQLFS-ASVYQDVSFGAVNLKLPED-EVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 409 IARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRS 487
Cdd:PRK13636 152 IAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
|
.
gi 2084914118 488 E 488
Cdd:PRK13636 232 E 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
262-490 |
3.32e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 129.92 E-value: 3.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 262 RDIHKRY-GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGkrddapvIRQGIRR 340
Cdd:PRK13652 7 RDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEN-------IREVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 IGMVFQNFN--LFPhRTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPD 418
Cdd:PRK13652 80 VGLVFQNPDdqIFS-PTVEQDIAFGPINLGL-DEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 419 IMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSEGD 490
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPD 230
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
259-476 |
9.94e-34 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 127.24 E-value: 9.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRY--GN--HEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDAPVi 334
Cdd:PRK11629 6 LQCDNLCKRYqeGSvqTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 335 RQgiRRIGMVFQNFNLFPHRTILDNVILaPRYHGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALA 414
Cdd:PRK11629 85 RN--QKLGFIYQFHHLLPDFTALENVAM-PLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2084914118 415 MEPDIMLFDEPTSALDP-------ELVGEvLNVirdlaREGMTMLIVTHEMDFALSISdRIVFMENGHV 476
Cdd:PRK11629 162 NNPRLVLADEPTGNLDArnadsifQLLGE-LNR-----LQGTAFLVVTHDLQLAKRMS-RQLEMRDGRL 223
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
273-476 |
1.13e-33 |
|
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: 125.62 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 273 VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfIKAGKRDDApvIRQGI-------RRIGmvf 345
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKP-VTRRSPRDA--IRAGIayvpedrKREG--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 346 qnfnLFPHRTILDNVILapryhgladsaelrrkghglldrvgllahahkyPHQLSGGQQQRVAIARALAMEPDIMLFDEP 425
Cdd:cd03215 89 ----LVLDLSVAENIAL---------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2084914118 426 TSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHV 476
Cdd:cd03215 132 TRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
273-485 |
1.37e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 129.59 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 273 VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLfgNDFIKAGKRDDAPVIRQGI-----------RRI 341
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV--GDIYIGDKKNNHELITNPYskkiknfkelrRRV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 342 GMVFQ--NFNLFPHrTILDNVILAPRYHGLADSaELRRKGHGLLDRVGL-LAHAHKYPHQLSGGQQQRVAIARALAMEPD 418
Cdd:PRK13631 119 SMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKS-EAKKLAKFYLNKMGLdDSYLERSPFGLSGGQKRRVAIAGILAIQPE 196
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 419 IMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI 485
Cdd:PRK13631 197 ILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEI 263
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
261-485 |
1.45e-33 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 127.51 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDApvirqgiRR 340
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA-------KR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 IGMVFQNfNLFPHR-TILDNVILA--PrYHGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEP 417
Cdd:COG4604 77 LAILRQE-NHINSRlTVRELVAFGrfP-YSKGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDT 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2084914118 418 DIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI 485
Cdd:COG4604 155 DYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
250-477 |
1.87e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 132.45 E-value: 1.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 250 EPVPGQPdALLLRDIHKRygnhEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfIKAGKRD 329
Cdd:COG1129 249 AAAPGEV-VLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKP-VRIRSPR 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 330 DApvIRQGI-------RRIGmvfqnfnLFPHRTILDNVILA--PRY--HGLADSAELRRKGHGLLDRVGLlahahKYPH- 397
Cdd:COG1129 323 DA--IRAGIayvpedrKGEG-------LVLDLSIRENITLAslDRLsrGGLLDRRRERALAEEYIKRLRI-----KTPSp 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 398 -----QLSGGQQQRVAIARALAMEPDIMLFDEPTSALDpelVG---EVLNVIRDLAREGMTMLIVTHEMDFALSISDRIV 469
Cdd:COG1129 389 eqpvgNLSGGNQQKVVLAKWLATDPKVLILDEPTRGID---VGakaEIYRLIRELAAEGKAVIVISSELPELLGLSDRIL 465
|
....*...
gi 2084914118 470 FMENGHVV 477
Cdd:COG1129 466 VMREGRIV 473
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
269-461 |
2.54e-33 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 126.05 E-value: 2.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 269 GNHE--VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDAPVIRQgirRIGMVFQ 346
Cdd:PRK10584 19 GEHElsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAK---HVGFVFQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 347 NFNLFPHRTILDNVILAPRYHGLADSaELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPT 426
Cdd:PRK10584 96 SFMLIPTLNALENVELPALLRGESSR-QSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPT 174
|
170 180 190
....*....|....*....|....*....|....*.
gi 2084914118 427 SALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFA 461
Cdd:PRK10584 175 GNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLA 210
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
274-496 |
3.89e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 127.17 E-value: 3.89e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 274 LKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDAPVIRQgirRIGMVFQnfnlFPH 353
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRK---KVGLVFQ----FPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 354 -----RTILDNVILAPRYHGLADSaELRRKGHGLLDRVGLLAHA-HKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTS 427
Cdd:PRK13649 96 sqlfeETVLKDVAFGPQNFGVSQE-EAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 428 ALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSE---------GDPRVRRF 496
Cdd:PRK13649 175 GLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDvdfleekqlGVPKITKF 252
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
258-474 |
5.05e-33 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 125.97 E-value: 5.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 258 ALLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLfgndfikAGKRDDAPvirqG 337
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITL-------DGKPVEGP----G 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 338 IRRiGMVFQNFNLFPHRTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEP 417
Cdd:PRK11248 70 AER-GVVFQNEGLLPWRNVQDNVAFGLQLAGV-EKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 418 DIMLFDEPTSALDP---ELVGEVLnvIRDLAREGMTMLIVTHEMDFALSISDRIVFMENG 474
Cdd:PRK11248 148 QLLLLDEPFGALDAftrEQMQTLL--LKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
261-479 |
5.15e-33 |
|
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: 125.01 E-value: 5.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHE--VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFikagKRDDAPVIRqgi 338
Cdd:cd03245 5 FRNVSFSYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDI----RQLDPADLR--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRIGMVFQNFNLFpHRTILDNVILApryHGLADSAELRRkghgLLDRVGLLAHAHKYPH-----------QLSGGQQQRV 407
Cdd:cd03245 78 RNIGYVPQDVTLF-YGTLRDNITLG---APLADDERILR----AAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084914118 408 AIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAReGMTMLIVTHEMDFaLSISDRIVFMENGHVVTD 479
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPSL-LDLVDRIIVMDSGRIVAD 219
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
268-480 |
6.21e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 126.36 E-value: 6.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 268 YGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLEsiDRGEIVLFGNDFIKAGK-----RDdapvIRQGIRRIG 342
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMN--DKVSGYRYSGDVLLGGRsifnyRD----VLEFRRRVG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 343 MVFQNFNLFPhRTILDNVILAPRYHGLADSAELRRKGHGLLDRVGLLAHAHK----YPHQLSGGQQQRVAIARALAMEPD 418
Cdd:PRK14271 105 MLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDrlsdSPFRLSGGQQQLLCLARTLAVNPE 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084914118 419 IMLFDEPTSALDPELVGEVLNVIRDLArEGMTMLIVTHEMDFALSISDRIVFMENGHVVTDA 480
Cdd:PRK14271 184 VLLLDEPTSALDPTTTEKIEEFIRSLA-DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEG 244
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
277-490 |
6.39e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 126.77 E-value: 6.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 277 IDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDAPVIRqgiRRIGMVFQnfnlFPH--- 353
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVR---KKVGVVFQ----FPEsql 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 354 --RTILDNVILAPRYHGLADSaELRRKGHGLLDRVGLLAHA-HKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALD 430
Cdd:PRK13643 98 feETVLKDVAFGPQNFGIPKE-KAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 431 PELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSEGD 490
Cdd:PRK13643 177 PKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVD 236
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
275-490 |
7.79e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 126.48 E-value: 7.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 275 KGIDLV---VKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDAPVIRqgiRRIGMVFQnfnlF 351
Cdd:PRK13641 21 KGLDNIsfeLEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLR---KKVSLVFQ----F 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 352 PH-----RTILDNVILAPRYHGLADSaELRRKGHGLLDRVGLLAH-AHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEP 425
Cdd:PRK13641 94 PEaqlfeNTVLKDVEFGPKNFGFSED-EAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084914118 426 TSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSEGD 490
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
258-477 |
7.95e-33 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 125.72 E-value: 7.95e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 258 ALL-LRDIHKRYGNH---------EVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNdfiKAGK 327
Cdd:COG4167 3 ALLeVRNLSKTFKYRtglfrrqqfEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGH---KLEY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 328 RDdapvIRQGIRRIGMVFQNFN--LFPHRTI---LDnvilAP-RYHGLADSAELRRKGHGLLDRVGLLA-HAHKYPHQLS 400
Cdd:COG4167 80 GD----YKYRCKHIRMIFQDPNtsLNPRLNIgqiLE----EPlRLNTDLTAEEREERIFATLRLVGLLPeHANFYPHMLS 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 401 GGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDL-AREGMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:COG4167 152 SGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELqEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVV 229
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
259-481 |
8.97e-33 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 125.58 E-value: 8.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGN-----HEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGND--FIKAGKRdda 331
Cdd:COG1101 2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDvtKLPEYKR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 332 pvirqgIRRIGMVFQNFNL--FPHRTILDNVILAPR---YHGL------ADSAELRRK----GHGLLDR----VGLLaha 392
Cdd:COG1101 79 ------AKYIGRVFQDPMMgtAPSMTIEENLALAYRrgkRRGLrrgltkKRRELFRELlatlGLGLENRldtkVGLL--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 393 hkyphqlSGGQQQrvaiARALAM----EPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDR 467
Cdd:COG1101 150 -------SGGQRQ----ALSLLMatltKPKLLLLDEHTAALDPKTAALVLELTEKIVEEnNLTTLMVTHNMEQALDYGNR 218
|
250
....*....|....
gi 2084914118 468 IVFMENGHVVTDAS 481
Cdd:COG1101 219 LIMMHEGRIILDVS 232
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
271-482 |
9.64e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 126.05 E-value: 9.64e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 271 HEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLfgNDFIKAGKRDDApVIRQGIRRIGMVFQnfnl 350
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTV--DDITITHKTKDK-YIRPVRKRIGMVFQ---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 351 FPHRTIL-DNV----ILAPRYHGLaDSAELRRKGHGLLDRVGLLAHA-HKYPHQLSGGQQQRVAIARALAMEPDIMLFDE 424
Cdd:PRK13646 93 FPESQLFeDTVereiIFGPKNFKM-NLDEVKNYAHRLLMDLGFSRDVmSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2084914118 425 PTSALDPELVGEVLNVIRDLA-REGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASP 482
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSP 230
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
221-492 |
2.09e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 126.87 E-value: 2.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 221 DLSRKNARTLDDTQ--AQALRQPASASKKRNEPVPGQPD-ALLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGK 297
Cdd:PRK13536 1 LLTRAVAEEAPRRLelSPIERKHQGISEAKASIPGSMSTvAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 298 TSLIRTINSLESIDRGEIVLFGndfikagkrddAPV---IRQGIRRIGMVFQNFNLFPHRTILDNVILAPRYHGLAdSAE 374
Cdd:PRK13536 81 STIARMILGMTSPDAGKITVLG-----------VPVparARLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMS-TRE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 375 LRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIV 454
Cdd:PRK13536 149 IEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLT 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2084914118 455 THEMDFALSISDRIVFMENGHVVTDASPASIRSE-----------GDPR 492
Cdd:PRK13536 229 THFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEhigcqvieiygGDPH 277
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
261-477 |
2.21e-32 |
|
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: 123.80 E-value: 2.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRY---GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFikagkRDDApvIRQG 337
Cdd:cd03249 3 FKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI-----RDLN--LRWL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 338 IRRIGMVFQNFNLFPhRTILDNVILAPRYhglADSAELrrkghgllDRVGLLAHAHKY----PH-----------QLSGG 402
Cdd:cd03249 76 RSQIGLVSQEPVLFD-GTIAENIRYGKPD---ATDEEV--------EEAAKKANIHDFimslPDgydtlvgergsQLSGG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084914118 403 QQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIrDLAREGMTMLIVTHEMDfALSISDRIVFMENGHVV 477
Cdd:cd03249 144 QKQRIAIARALLRNPKILLLDEATSALDAESEKLVQEAL-DRAMKGRTTIVIAHRLS-TIRNADLIAVLQNGQVV 216
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
240-477 |
2.26e-32 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 130.75 E-value: 2.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 240 QPASASKKRNEPVPGQPdALLLRDIHKRYG---------NHEV--LKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLE 308
Cdd:PRK10261 296 AKQEPPIEQDTVVDGEP-ILQVRNLVTRFPlrsgllnrvTREVhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLV 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 309 SIDRGEIVLFGN--DFIKAGKRddapvirQGIRR-IGMVFQN--FNLFPHRTILDNVILAPRYHGLADSAELRRKGHGLL 383
Cdd:PRK10261 375 ESQGGEIIFNGQriDTLSPGKL-------QALRRdIQFIFQDpyASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLL 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 384 DRVGLLA-HAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFA 461
Cdd:PRK10261 448 ERVGLLPeHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVV 527
|
250
....*....|....*.
gi 2084914118 462 LSISDRIVFMENGHVV 477
Cdd:PRK10261 528 ERISHRVAVMYLGQIV 543
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
259-480 |
2.40e-32 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 124.80 E-value: 2.40e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNH---------EVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfIKAGKRD 329
Cdd:PRK10419 4 LNVSGLSHHYAHGglsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEP-LAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 330 DAPVIRqgiRRIGMVFQN----FNlfPHRTILDnVILAPRYHGLA-DSAELRRKGHGLLDRVGL-LAHAHKYPHQLSGGQ 403
Cdd:PRK10419 83 QRKAFR---RDIQMVFQDsisaVN--PRKTVRE-IIREPLRHLLSlDKAERLARASEMLRAVDLdDSVLDKRPPQLSGGQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 404 QQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDL-AREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDA 480
Cdd:PRK10419 157 LQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQ 234
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
259-474 |
5.35e-32 |
|
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: 122.54 E-value: 5.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHE-------VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTI--NSLesIDRGEI-VLFGNDFI---KA 325
Cdd:COG4778 5 LEVENLSKTFTLHLqggkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIygNYL--PDSGSIlVRHDGGWVdlaQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 326 GKRDdapVIRqgIRR--IGMVFQNFNLFPHRTILDNVILAPRYHGlADSAELRRKGHGLLDRVGL---LAHAhkYPHQLS 400
Cdd:COG4778 83 SPRE---ILA--LRRrtIGYVSQFLRVIPRVSALDVVAEPLLERG-VDREEARARARELLARLNLperLWDL--PPATFS 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084914118 401 GGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENG 474
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
274-500 |
1.73e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 122.51 E-value: 1.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 274 LKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLfgndfikAGKRDDAPVIRQGIRRIGMVFQN-FNLFP 352
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKI-------DGELLTAENVWNLRRKIGMVFQNpDNQFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 353 HRTILDNVILAPRYHGLADSAELRRKGHGLLdRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPE 432
Cdd:PRK13642 96 GATVEDDVAFGMENQGIPREEMIKRVDEALL-AVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPT 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2084914118 433 LVGEVLNVIRDLA-REGMTMLIVTHEMDFALSiSDRIVFMENGHVVTDASPASIRSEGDPRVRrfIGLE 500
Cdd:PRK13642 175 GRQEIMRVIHEIKeKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEDMVE--IGLD 240
|
|
| PRK15100 |
PRK15100 |
cystine ABC transporter permease; |
19-208 |
2.24e-31 |
|
cystine ABC transporter permease;
Pssm-ID: 185055 [Multi-domain] Cd Length: 220 Bit Score: 120.62 E-value: 2.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 19 KACLTVVQLSTLSWSIGLVLGFLLASAKLSGHAWLRMPASFYIWLFRSIPLLV-LLVFVYNLPQLfpvtgSVLSQPFYSG 97
Cdd:PRK15100 17 KGAGYTLQLSIGGMFFGLLLGFILALMRLSPIWPVRWLARFYVSIFRGTPLIAqLFMIYYGLPQF-----GIELDPIPAA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 98 LIALVLTETAYMAEIHRGGLLSVLKGQREAAKALGIRGVGAQRLVIIPQAIRISLPTLTNEYVTIVKLTSLVSVISLNEL 177
Cdd:PRK15100 92 MIGLSLNTAAYAAETLRAAISSIDKGQWEAAASIGMTRWQTLRRAILPQAARTALPPLSNSFISLVKDTSLAATIQVPEL 171
|
170 180 190
....*....|....*....|....*....|..
gi 2084914118 178 LLVGQRLYAQNFLVLET-LAAVAIYYVLIVTL 208
Cdd:PRK15100 172 FRQAQLITSRTLEVFTMyLAASLIYWIMATVL 203
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
261-481 |
3.08e-31 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 120.67 E-value: 3.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYG--NHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAgkrdDAPVIRqgi 338
Cdd:cd03252 3 FEHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA----DPAWLR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRIGMVFQNFNLFpHRTILDNVilapryhGLADSAELRRKghglLDRVGLLAHAHKYPHQ---------------LSGGQ 403
Cdd:cd03252 76 RQVGVVLQENVLF-NRSIRDNI-------ALADPGMSMER----VIEAAKLAGAHDFISElpegydtivgeqgagLSGGQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 404 QQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLArEGMTMLIVTHEMDfALSISDRIVFMENGHVVTDAS 481
Cdd:cd03252 144 RQRIAIARALIHNPRILIFDEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGS 219
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
261-479 |
3.60e-31 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 127.67 E-value: 3.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGN--HEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFikagKRDDAPVIRqgi 338
Cdd:TIGR03375 466 FRNVSFAYPGqeTPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDI----RQIDPADLR--- 538
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRIGMVFQNFNLFpHRTILDNVILAPRYhglADSAELRRkghgLLDRVGLLA----HAHKYPHQ-------LSGGQQQRV 407
Cdd:TIGR03375 539 RNIGYVPQDPRLF-YGTLRDNIALGAPY---ADDEEILR----AAELAGVTEfvrrHPDGLDMQigergrsLSGGQRQAV 610
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084914118 408 AIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLArEGMTMLIVTHEMDFaLSISDRIVFMENGHVVTD 479
Cdd:TIGR03375 611 ALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTSL-LDLVDRIIVMDNGRIVAD 680
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
261-502 |
3.81e-31 |
|
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: 126.46 E-value: 3.81e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESI--DRGEIV---------------------- 316
Cdd:TIGR03269 3 VKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYepTSGRIIyhvalcekcgyverpskvgepc 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 317 --------LFGNDFIKAgkrdDAPVIRQGIRRIGMVFQ-NFNLFPHRTILDNVILAPRYHGLADSAELRRKGHgLLDRVG 387
Cdd:TIGR03269 83 pvcggtlePEEVDFWNL----SDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVD-LIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 388 LlahAHKYPH---QLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALS 463
Cdd:TIGR03269 158 L---SHRITHiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSHWPEVIED 234
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2084914118 464 ISDRIVFMENGHVVTDASPASIRS---EGDPRVRRFIGLEQE 502
Cdd:TIGR03269 235 LSDKAIWLENGEIKEEGTPDEVVAvfmEGVSEVEKECEVEVG 276
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
190-456 |
7.08e-31 |
|
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: 125.55 E-value: 7.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 190 LVLETLAAVAIYYVLIVtlfgwllqwAERHLDLSRKNARTLDDTQAQALRQPAsASKKRNEPVPGQPDALLLRDIHKRY- 268
Cdd:TIGR02868 276 LVLLPLAAFEAFAALPA---------AAQQLTRVRAAAERIVEVLDAAGPVAE-GSAPAAGAVGLGKPTLELRDLSAGYp 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 269 GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDApvirqgiRRIGMVFQNF 348
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVR-------RRVSVCAQDA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 349 NLFpHRTILDNVILApryHGLADSAELRRkghgLLDRVGLLAHAHKYPH-----------QLSGGQQQRVAIARALAMEP 417
Cdd:TIGR02868 419 HLF-DTTVRENLRLA---RPDATDEELWA----ALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADA 490
|
250 260 270
....*....|....*....|....*....|....*....
gi 2084914118 418 DIMLFDEPTSALDPELVGEVLNVIRDlAREGMTMLIVTH 456
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
274-487 |
7.39e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 121.27 E-value: 7.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 274 LKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLfGNDFIKAGKRDDAPVIRqgIRR-IGMVFQ--NFNL 350
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIV-GDYAIPANLKKIKEVKR--LRKeIGLVFQfpEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 351 FpHRTILDNVILAPRYHGlADSAELRRKGHGLLDRVGL-LAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSAL 429
Cdd:PRK13645 104 F-QETIEKDIAFGPVNLG-ENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2084914118 430 DPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRS 487
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
|
|
| glnP |
PRK09494 |
glutamine ABC transporter permease protein; Reviewed |
1-220 |
1.37e-30 |
|
glutamine ABC transporter permease protein; Reviewed
Pssm-ID: 181907 [Multi-domain] Cd Length: 219 Bit Score: 118.23 E-value: 1.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 1 MAFDWAYFFSlfSVSAFWKACLTVVQLSTLSWSIGLVLGFLLASAKLSGHAWLRMPASFYIWLFRSIPLLVLLVFVY-NL 79
Cdd:PRK09494 1 MQFDWSAIWP--AIPLLLEGAKMTLWISVLGLAGGLVIGLLAGFARAYGGWIANHIALVFIELIRGTPIVVQVMFIYfAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 80 PQLFPvtgSVLSQPFYSGLIALVLTETAYMAEIHRGGLLSVLKGQREAAKALGIRGVGAQRLVIIPQAIRISLPTLTNEY 159
Cdd:PRK09494 79 PMAFN---DLRIDPFTAAVVTIMINSGAYIAEITRGAVLSIHKGFREAGLALGLSRRETLRYVIGPLALRRMLPPLGNQW 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084914118 160 VTIVKLTSLVSVISLNELLLVGQRLYAQNFLVLETLAAVAIYYVLIVTLFGWLLQWAERHL 220
Cdd:PRK09494 156 IISIKDTSLFIVIGVAELTRQGQEIIAGNFRALEIWSAVAVIYLIITLVLSFILRRLERRM 216
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
273-500 |
1.76e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 119.90 E-value: 1.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 273 VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSL---ESIDRGEIVLFGNDFIKAGKRDdapvIRQgirRIGMVFQN-F 348
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTAKTVWD----IRE---KVGIVFQNpD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 349 NLFPHRTILDNVILapryhGLADSA----ELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDE 424
Cdd:PRK13640 95 NQFVGATVGDDVAF-----GLENRAvprpEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 425 PTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFAlSISDRIVFMENGHVVTDASPASIRSegDPRVRRFIGLE 500
Cdd:PRK13640 170 STSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFS--KVEMLKEIGLD 243
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
262-477 |
1.81e-30 |
|
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: 118.10 E-value: 1.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 262 RDIHKRYGN-HEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfIKAGKRDdapVIRqgiRR 340
Cdd:cd03254 6 ENVNFSYDEkKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGID-IRDISRK---SLR---SM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 IGMVFQNFNLFPhRTILDNVILApryHGLADSAELRR-----KGHGLLDRV--GLLAHAHKYPHQLSGGQQQRVAIARAL 413
Cdd:cd03254 79 IGVVLQDTFLFS-GTIMENIRLG---RPNATDEEVIEaakeaGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAM 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 414 AMEPDIMLFDEPTSALDPELVGEVLNVIRDLaREGMTMLIVTHEmdfaLSI---SDRIVFMENGHVV 477
Cdd:cd03254 155 LRDPKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHR----LSTiknADKILVLDDGKII 216
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
259-476 |
2.28e-30 |
|
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: 116.16 E-value: 2.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYG--NHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDdapvIRQ 336
Cdd:cd03246 1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNE----LGD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 337 girRIGMVFQNFNLFPHrTILDNVilapryhgladsaelrrkghglldrvgllahahkyphqLSGGQQQRVAIARALAME 416
Cdd:cd03246 77 ---HVGYLPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGN 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 417 PDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDfALSISDRIVFMENGHV 476
Cdd:cd03246 115 PRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
261-478 |
3.30e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 123.64 E-value: 3.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIvlfgndfikagkrddapVIRQGIrR 340
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV-----------------SIPKGL-R 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 IGMVFQNFNLFPHRTILDNVI--LAPRYHGLADSAELRRK---GHGLLDRVGLL------AHAHKYPHQ----------- 398
Cdd:COG0488 63 IGYLPQEPPLDDDLTVLDTVLdgDAELRALEAELEELEAKlaePDEDLERLAELqeefeaLGGWEAEARaeeilsglgfp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 399 ----------LSGGQQQRVAIARALAMEPDIMLFDEPTSALDpelvgevLNVIRDLA-----REGmTMLIVTHEMDFALS 463
Cdd:COG0488 143 eedldrpvseLSGGWRRRVALARALLSEPDLLLLDEPTNHLD-------LESIEWLEeflknYPG-TVLVVSHDRYFLDR 214
|
250
....*....|....*
gi 2084914118 464 ISDRIVFMENGHVVT 478
Cdd:COG0488 215 VATRILELDRGKLTL 229
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
258-472 |
5.76e-30 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 117.83 E-value: 5.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 258 ALLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESID-----RGEIVLFGNDFIKagKRDDAP 332
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYE--RRVNLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 333 VIRqgiRRIGMVFQNFNLFPhRTILDNVILAPRYHG------LADSAELRRKGHGLLDRVGllAHAHKYPHQLSGGQQQR 406
Cdd:PRK14258 85 RLR---RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGwrpkleIDDIVESALKDADLWDEIK--HKIHKSALDLSGGQQQR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 407 VAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLA-REGMTMLIVTHEMDFALSISDRIVFME 472
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDFTAFFK 225
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
261-485 |
2.47e-29 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 119.18 E-value: 2.47e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDApvirqgiRR 340
Cdd:PRK09536 6 VSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS-------RR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 IGMVFQNFNL--------------FPHRTILDNvilapryHGLADSAELRRKghglLDRVGLLAHAHKYPHQLSGGQQQR 406
Cdd:PRK09536 79 VASVPQDTSLsfefdvrqvvemgrTPHRSRFDT-------WTETDRAAVERA----MERTGVAQFADRPVTSLSGGERQR 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2084914118 407 VAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI 485
Cdd:PRK09536 148 VLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
272-477 |
2.91e-29 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 113.80 E-value: 2.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 272 EVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLES--IDRGEIVLfgNdfikaGKRDDAPVIRqgiRRIGMVFQNFN 349
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLI--N-----GRPLDKRSFR---KIIGYVPQDDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 350 LFPHRTILDNvilapryhgLADSAELRrkghglldrvgllahahkyphQLSGGQQQRVAIARALAMEPDIMLFDEPTSAL 429
Cdd:cd03213 93 LHPTLTVRET---------LMFAAKLR---------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGL 142
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2084914118 430 DPELVGEVLNVIRDLAREGMTMLIVTHE-MDFALSISDRIVFMENGHVV 477
Cdd:cd03213 143 DSSSALQVMSLLRRLADTGRTIICSIHQpSSEIFELFDKLLLLSQGRVI 191
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
259-478 |
4.73e-29 |
|
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: 113.39 E-value: 4.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTI--NSLESIDRGEIVLFGNDFIkagkrdDAPVIRQ 336
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDIT------DLPPEER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 337 GIRRIGMVFQNfnlfPhrtildnvilaPRYHGLADSAELRRKGHGLldrvgllahahkyphqlSGGQQQRVAIARALAME 416
Cdd:cd03217 75 ARLGIFLAFQY----P-----------PEIPGVKNADFLRYVNEGF-----------------SGGEKKRNEILQLLLLE 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 417 PDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTH-EMDFALSISDRIVFMENGHVVT 478
Cdd:cd03217 123 PDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyQRLLDYIKPDRVHVLYDGRIVK 185
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
261-477 |
1.02e-28 |
|
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: 113.48 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHE--VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFikagkRDdapVIRQGI 338
Cdd:cd03251 3 FKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV-----RD---YTLASL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RR-IGMVFQNFNLFpHRTILDNVILAPRYhglADSAELRRKGHglldrvglLAHAH----KYPH-----------QLSGG 402
Cdd:cd03251 75 RRqIGLVSQDVFLF-NDTVAENIAYGRPG---ATREEVEEAAR--------AANAHefimELPEgydtvigergvKLSGG 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 403 QQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLArEGMTMLIVTHEmdfaLSI---SDRIVFMENGHVV 477
Cdd:cd03251 143 QRQRIAIARALLKDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHR----LSTienADRIVVLEDGKIV 215
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
261-477 |
1.68e-28 |
|
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: 113.09 E-value: 1.68e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNH-EVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFikagKRDDAPVIRqgiR 339
Cdd:cd03253 3 FENVTFAYDPGrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI----REVTLDSLR---R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 340 RIGMVFQNFNLFpHRTILDNVilapRYHGL-ADSAELRRkghglldrVGLLAHAH----KYPHQ-----------LSGGQ 403
Cdd:cd03253 76 AIGVVPQDTVLF-NDTIGYNI----RYGRPdATDEEVIE--------AAKAAQIHdkimRFPDGydtivgerglkLSGGE 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084914118 404 QQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAReGMTMLIVTHEMDFALSiSDRIVFMENGHVV 477
Cdd:cd03253 143 KQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVN-ADKIIVLKDGRIV 214
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
271-477 |
5.67e-28 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 117.11 E-value: 5.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 271 HEVLKGIDLVVKPGEVISIIGPSGSGKT----SLIRTINSLESI-DRGEIVLFGNDFIKAgkrdDAPVIRqGIR--RIGM 343
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGESLLHA----SEQTLR-GVRgnKIAM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 344 VFQN--FNLFPHRTI---LDNVILAPRyhGLADSAElRRKGHGLLDRVGLLAHAHK---YPHQLSGGQQQRVAIARALAM 415
Cdd:PRK15134 97 IFQEpmVSLNPLHTLekqLYEVLSLHR--GMRREAA-RGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLT 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 416 EPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:PRK15134 174 RPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
274-490 |
7.76e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 112.15 E-value: 7.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 274 LKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIvLFGNDFIKAGKRDDapvIRQgirRIGMVFQN-FNLFP 352
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEI-FYNNQAITDDNFEK---LRK---HIGIVFQNpDNQFV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 353 HRTILDNVILAPRYHgLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPE 432
Cdd:PRK13648 98 GSIVKYDVAFGLENH-AVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2084914118 433 LVGEVLNVIRDLARE-GMTMLIVTHEMDFALSiSDRIVFMENGHVVTDASPASIRSEGD 490
Cdd:PRK13648 177 ARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| ectoine_ehuD |
TIGR03003 |
ectoine/hydroxyectoine ABC transporter, permease protein EhuD; Members of this family are ... |
3-220 |
1.78e-27 |
|
ectoine/hydroxyectoine ABC transporter, permease protein EhuD; Members of this family are presumed to act as permease subunits of ectoine ABC transporters. Operons containing this gene also contain the other genes of the ABC transporter and typically are found next to either ectoine utilization or ectoine biosynthesis operons.
Pssm-ID: 132048 [Multi-domain] Cd Length: 212 Bit Score: 109.56 E-value: 1.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 3 FDWAYFFSLFSVsaFWKACLTVVQLSTLSWSIGLVLGFLLASAKLSGHAWLRMPASFYIWLFRSIPLLVLLVFVYnlpQL 82
Cdd:TIGR03003 1 WDWEFVRQILPT--LIEGLKITILATALGFAIAAVLGLVFAILRRSAPTPISWPTSFVVEFIRGTPLLVQLYFLY---YV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 83 FPVTGSVLSQpFYSGLIALVLTETAYMAEIHRGGLLSVLKGQREAAKALGIRGVGAQRLVIIPQAIRISLPTLTNEYVTI 162
Cdd:TIGR03003 76 LPDIGIRLPA-LVAGVLGLGLHYATYAAEVYRAGIEAVPRGQWEAATALNLTARQTYRHIILPQAIPPIIPALGNYLVAM 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 163 VKLTSLVSVISLNELLLVGQRLYAQNFLVLETLAAVAIYYVLIVTLFGWLLQWAERHL 220
Cdd:TIGR03003 155 FKETPVLSAITVLELMNQAKSIGNSTFRYLEPMTLVGVFFLILSIISVFFLRRLEARL 212
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
267-470 |
4.96e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 107.70 E-value: 4.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 267 RYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVlfgndfiKAGKRDDAPVIRQG-------IR 339
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR-------RAGGARVAYVPQRSevpdslpLT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 340 RIGMVfqNFNLFPHRTILdnvilapRYHGLADSAELRRKghglLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDI 419
Cdd:NF040873 74 VRDLV--AMGRWARRGLW-------RRLTRDDRAAVDDA----LERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADL 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2084914118 420 MLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVF 470
Cdd:NF040873 141 LLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
165-489 |
5.76e-27 |
|
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.
Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 114.41 E-value: 5.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 165 LTSLVSVISLNE---LLLVGQRLYAQNFLVLETLAAVAIYYVLIVTLFGWLLQ-WAErhldLSRKNA---RTLDDTQAQA 237
Cdd:TIGR02204 244 LTAIVIVLVFGAivgVLWVGAHDVIAGKMSAGTLGQFVFYAVMVAGSIGTLSEvWGE----LQRAAGaaeRLIELLQAEP 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 238 LRQPASASKKRNEPVPGQpdaLLLRDIHKRYG---NHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGE 314
Cdd:TIGR02204 320 DIKAPAHPKTLPVPLRGE---IEFEQVNFAYParpDQPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGR 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 315 IVLFGNDFIKAgkrdDAPVIRQgirRIGMVFQNFNLFPHrTILDNVilapRYHGL-ADSAELRrkghglldRVGLLAHAH 393
Cdd:TIGR02204 397 ILLDGVDLRQL----DPAELRA---RMALVPQDPVLFAA-SVMENI----RYGRPdATDEEVE--------AAARAAHAH 456
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 394 KYPHQ---------------LSGGQQQRVAIARALAMEPDIMLFDEPTSALDPE---LVGEVLnvirDLAREGMTMLIVT 455
Cdd:TIGR02204 457 EFISAlpegydtylgergvtLSGGQRQRIAIARAILKDAPILLLDEATSALDAEseqLVQQAL----ETLMKGRTTLIIA 532
|
330 340 350
....*....|....*....|....*....|....
gi 2084914118 456 HEMDFALSiSDRIVFMENGHVVTDASPASIRSEG 489
Cdd:TIGR02204 533 HRLATVLK-ADRIVVMDQGRIVAQGTHAELIAKG 565
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
273-477 |
8.09e-27 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 108.13 E-value: 8.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 273 VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSL---ESIDRGEIVLFGndfiKAGKRDdapvirQGIRRIGMVFQNFN 349
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRvegGGTTSGQILFNG----QPRKPD------QFQKCVAYVRQDDI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 350 LFPHRTILDN----VILAPRYHgLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEP 425
Cdd:cd03234 92 LLPGLTVRETltytAILRLPRK-SSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 426 TSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFAL-SISDRIVFMENGHVV 477
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLfRLFDRILLLSSGEIV 223
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
273-474 |
1.58e-26 |
|
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: 106.40 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 273 VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTI-NSLESIDrGEIVLFGndfikagkrddapvirqgirRIGMVFQN---F 348
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALlGELEKLS-GSVSVPG--------------------SIAYVSQEpwiQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 349 NlfphRTILDNVIL-----APRYHGLADSAELRRK----GHGLLDRVGllahahkyphQ----LSGGQQQRVAIARALAM 415
Cdd:cd03250 79 N----GTIRENILFgkpfdEERYEKVIKACALEPDleilPDGDLTEIG----------EkginLSGGQKQRISLARAVYS 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084914118 416 EPDIMLFDEPTSALDPElVGEVL--NVIRDLAREGMTMLIVTHEMDFaLSISDRIVFMENG 474
Cdd:cd03250 145 DADIYLLDDPLSAVDAH-VGRHIfeNCILGLLLNNKTRILVTHQLQL-LPHADQIVVLDNG 203
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
248-477 |
1.61e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 112.43 E-value: 1.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 248 RNEPVPGQPdALLLRDIH-KRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAG 326
Cdd:COG3845 248 KAPAEPGEV-VLEVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 327 KRDdapVIRQGIRRI-------GMVfqnfnlfPHRTILDNVILapRYHglaDSAELRRkgHGLLDRVGLLAHAHKY---- 395
Cdd:COG3845 327 PRE---RRRLGVAYIpedrlgrGLV-------PDMSVAENLIL--GRY---RRPPFSR--GGFLDRKAIRAFAEELieef 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 396 ------PHQ----LSGGQQQRVAIARALAMEPDIMLFDEPTSALDpelVG---EVLNVIRDLAREGMTMLIVTHEMDFAL 462
Cdd:COG3845 390 dvrtpgPDTparsLSGGNQQKVILARELSRDPKLLIAAQPTRGLD---VGaieFIHQRLLELRDAGAAVLLISEDLDEIL 466
|
250
....*....|....*
gi 2084914118 463 SISDRIVFMENGHVV 477
Cdd:COG3845 467 ALSDRIAVMYEGRIV 481
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
259-485 |
1.70e-26 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 107.66 E-value: 1.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAgkrDDAPVIRQGI 338
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW---QTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 rriGMVFQNFNLFPHRTILDNVILAPRYHGLADSAELRRKGHGLLDRvgLLAHAHKYPHQLSGGQQQRVAIARALAMEPD 418
Cdd:PRK11614 83 ---AIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 419 IMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI 485
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDAL 224
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
269-471 |
1.91e-26 |
|
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: 112.38 E-value: 1.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 269 GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAgkrdDAPVIRqgiRRIGMVFQNF 348
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADA----DADSWR---DQIAWVPQHP 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 349 NLFPhRTILDNVILAPRYhglADSAELRRKGH--GLLDRV-----GLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIML 421
Cdd:TIGR02857 406 FLFA-GTIAENIRLARPD---ASDAEIREALEraGLDEFVaalpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLL 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2084914118 422 FDEPTSALDPELVGEVLNVIRDLAReGMTMLIVTHemDFALSI-SDRIVFM 471
Cdd:TIGR02857 482 LDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTH--RLALAAlADRIVVL 529
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
259-477 |
3.13e-26 |
|
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: 105.09 E-value: 3.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHE--VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKrddapVIRQ 336
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-----ALSS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 337 girRIGMVFQNFNLFpHRTILDNVilapryhgladsaelrrkghglldrvGLlahahkyphQLSGGQQQRVAIARALAME 416
Cdd:cd03247 76 ---LISVLNQRPYLF-DTTLRNNL--------------------------GR---------RFSGGERQRLALARILLQD 116
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084914118 417 PDIMLFDEPTSALDPELVGEVLNVIRDLAREgMTMLIVTHEMDfALSISDRIVFMENGHVV 477
Cdd:cd03247 117 APIVLLDEPTVGLDPITERQLLSLIFEVLKD-KTLIWITHHLT-GIEHMDKILFLENGKII 175
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
238-489 |
4.42e-26 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 112.14 E-value: 4.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 238 LRQPASASKKRNEPVPGQPDALLLRDIHKRYGNH--EVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEI 315
Cdd:TIGR01846 435 LNSPTEPRSAGLAALPELRGAITFENIRFRYAPDspEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQV 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 316 VLFGNDFIKAgkrdDAPVIRqgiRRIGMVFQNFNLFpHRTILDNVIL----APRYHGLAdSAELRrkghGLLDRVGLLAH 391
Cdd:TIGR01846 515 LVDGVDLAIA----DPAWLR---RQMGVVLQENVLF-SRSIRDNIALcnpgAPFEHVIH-AAKLA----GAHDFISELPQ 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 392 AHKYP-----HQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAReGMTMLIVTHEMDfALSISD 466
Cdd:TIGR01846 582 GYNTEvgekgANLSGGQRQRIAIARALVGNPRILIFDEATSALDYESEALIMRNMREICR-GRTVIIIAHRLS-TVRACD 659
|
250 260
....*....|....*....|...
gi 2084914118 467 RIVFMENGHVVTDASPASIRSEG 489
Cdd:TIGR01846 660 RIIVLEKGQIAESGRHEELLALQ 682
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
226-477 |
8.64e-26 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 110.57 E-value: 8.64e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 226 NARTLDDTQAQALRQPASASKKRNEPVPGQPDALLL-------------RDIHKR-YGNHEVLKGIDLVVKPGEVISIIG 291
Cdd:PRK15134 240 RAATLFSAPTHPYTQKLLNSEPSGDPVPLPEPASPLldveqlqvafpirKGILKRtVDHNVVVKNISFTLRPGETLGLVG 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 292 PSGSGKTS----LIRTINSlesidRGEIVLFGNDFIKAGKRDDAPVIRqgirRIGMVFQNFN--LFPHRTILDNVILAPR 365
Cdd:PRK15134 320 ESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNLNRRQLLPVRH----RIQVVFQDPNssLNPRLNVLQIIEEGLR 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 366 YHGLADSAELR-RKGHGLLDRVGLLAHA-HKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRD 443
Cdd:PRK15134 391 VHQPTLSAAQReQQVIAVMEEVGLDPETrHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKS 470
|
250 260 270
....*....|....*....|....*....|....*
gi 2084914118 444 L-AREGMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:PRK15134 471 LqQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVV 505
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
259-490 |
1.08e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 110.02 E-value: 1.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLE---SIDrGEIVLFGNDFIKAGKRDDApviR 335
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYphgTYE-GEIIFEGEELQASNIRDTE---R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 336 QGIRRIgmvFQNFNLFPHRTILDNVILA--PRYHGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARAL 413
Cdd:PRK13549 82 AGIAII---HQELALVKELSVLENIFLGneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 414 AMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENG-HVVTDasPASIRSEGD 490
Cdd:PRK13549 159 NKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGrHIGTR--PAAGMTEDD 234
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
248-477 |
1.32e-25 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 110.44 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 248 RNEPvPGQPD------ALLLRDIHKRYGNH-EVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGN 320
Cdd:PRK13657 319 VRDP-PGAIDlgrvkgAVEFDDVSFSYDNSrQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGT 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 321 DFikagkRDdapVIRQGIRR-IGMVFQNFNLFpHRTILDNVILapryhGLADS--AELRR-----KGHGLLDR--VGLLA 390
Cdd:PRK13657 398 DI-----RT---VTRASLRRnIAVVFQDAGLF-NRSIEDNIRV-----GRPDAtdEEMRAaaeraQAHDFIERkpDGYDT 463
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 391 HAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIrDLAREGMTMLIVTHEmdfaLSI---SDR 467
Cdd:PRK13657 464 VVGERGRQLSGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAAL-DELMKGRTTFIIAHR----LSTvrnADR 538
|
250
....*....|
gi 2084914118 468 IVFMENGHVV 477
Cdd:PRK13657 539 ILVFDNGRVV 548
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
249-477 |
1.66e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 109.91 E-value: 1.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 249 NEPVPGQPdALLLRDIHKRY--GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfIKAG 326
Cdd:PRK11160 330 STAAADQV-SLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQP-IADY 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 327 KRDDapvIRQGIrriGMVFQNFNLFPHrTILDNVILA-PRyhglADSAELrrkgHGLLDRVGLLAHAHKYP--------- 396
Cdd:PRK11160 408 SEAA---LRQAI---SVVSQRVHLFSA-TLRDNLLLAaPN----ASDEAL----IEVLQQVGLEKLLEDDKglnawlgeg 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 397 -HQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAReGMTMLIVTHEMdFALSISDRIVFMENGH 475
Cdd:PRK11160 473 gRQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ-NKTVLMITHRL-TGLEQFDRICVMDNGQ 550
|
..
gi 2084914118 476 VV 477
Cdd:PRK11160 551 II 552
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
263-490 |
1.92e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 105.47 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 263 DIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGN--DFIKAGkrddAPVIRQgirR 340
Cdd:PRK13638 6 DLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRG----LLALRQ---Q 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 IGMVFQNFNLFPHRTILD-NVILAPRYHGLADSAELRRkghglLDRVGLLAHAHKYPHQ----LSGGQQQRVAIARALAM 415
Cdd:PRK13638 79 VATVFQDPEQQIFYTDIDsDIAFSLRNLGVPEAEITRR-----VDEALTLVDAQHFRHQpiqcLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084914118 416 EPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSEGD 490
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTE 228
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
259-474 |
2.02e-25 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 104.02 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLfgndfikagkrDDAPVIRQGI 338
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIF-----------DGHPWTRKDL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRIGMVFQNFNLFPHRTILDNVILAPRYHGLADSAELRrkghgLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPD 418
Cdd:TIGR03740 70 HKIGSLIESPPLYENLTARENLKVHTTLLGLPDSRIDE-----VLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPK 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2084914118 419 IMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENG 474
Cdd:TIGR03740 145 LLILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEG 200
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
212-477 |
2.67e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 109.00 E-value: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 212 LLQWAERHldlsRKNARTldDTQAQA----------LRQPASASK---KRNEPVPGQPDALLLRDIHKRYGNHEVLKGID 278
Cdd:COG0488 262 EEEFIRRF----RAKARK--AKQAQSrikaleklerEEPPRRDKTveiRFPPPERLGKKVLELEGLSKSYGDKTLLDDLS 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 279 LVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIvlfgndfiKAGKRddapVirqgirRIGMVFQNF-NLFPHRTIL 357
Cdd:COG0488 336 LRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV--------KLGET----V------KIGYFDQHQeELDPDKTVL 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 358 DNVIlapRYHGLADSAELRrkghGLLDRvgLL---AHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELV 434
Cdd:COG0488 398 DELR---DGAPGGTEQEVR----GYLGR--FLfsgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDIETL 468
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2084914118 435 GEVLNVIRDLarEGmTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:COG0488 469 EALEEALDDF--PG-TVLLVSHDRYFLDRVATRILEFEDGGVR 508
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
259-490 |
2.88e-25 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 108.76 E-value: 2.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLE---SIDrGEIVLFGNDFIKAGKRDDApviR 335
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphgTWD-GEIYWSGSPLKASNIRDTE---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 336 QGIrriGMVFQNFNLFPHRTILDNVILAPRYH---GLADSAELRRKGHGLLDRVGLLAHAHKYP-HQLSGGQQQRVAIAR 411
Cdd:TIGR02633 78 AGI---VIIHQELTLVPELSVAENIFLGNEITlpgGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 412 ALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENG-HVVTdaSPASIRSEGD 490
Cdd:TIGR02633 155 ALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGqHVAT--KDMSTMSEDD 232
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
259-485 |
4.01e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 103.62 E-value: 4.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEivlfgndfikagkrddapVIRQGi 338
Cdd:COG1134 27 LLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR------------------VEVNG- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 rRI------GMVFQnfnlfPHRTILDNVILAPRYHGLaDSAELRRKghglLDRV----GLlahaHKYPHQ----LSGGQQ 404
Cdd:COG1134 88 -RVsallelGAGFH-----PELTGRENIYLNGRLLGL-SRKEIDEK----FDEIvefaEL----GDFIDQpvktYSSGMR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 405 QRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPAS 484
Cdd:COG1134 153 ARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
.
gi 2084914118 485 I 485
Cdd:COG1134 233 V 233
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
267-482 |
4.79e-25 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 102.96 E-value: 4.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 267 RYGNHE--VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDdapvIRQgirRIGMV 344
Cdd:cd03244 11 RYRPNLppVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHD----LRS---RISII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 345 FQNFNLFPHrTILDNviLAPryHGLADSAELRRkghgLLDRVGLLAHAHKYPHQL-----------SGGQQQRVAIARAL 413
Cdd:cd03244 84 PQDPVLFSG-TIRSN--LDP--FGEYSDEELWQ----ALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2084914118 414 AMEPDIMLFDEPTSALDPELVGEVLNVIRDlAREGMTMLIVTHEMDFALSiSDRIVFMENGHVVTDASP 482
Cdd:cd03244 155 LRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDSP 221
|
|
| PRK15069 |
PRK15069 |
histidine ABC transporter permease HisM; |
27-219 |
9.14e-25 |
|
histidine ABC transporter permease HisM;
Pssm-ID: 185029 [Multi-domain] Cd Length: 234 Bit Score: 102.44 E-value: 9.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 27 LSTLSWSIGLVLGFLLASAKLSGHAWLRMPASFYIWLFRSIPLLV-LLVFVYNLPQLFPVTG-SVLSQPFYSGL----IA 100
Cdd:PRK15069 29 LLVASVVIGFVLAVPLAIARVSSNKWIRFPVWLYTYVFRGTPLYVqLLVFYTGMYSLEIVRGtDLLDAFFRSGLnctiLA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 101 LVLTETAYMAEIHRGGLLSVLKGQREAAKALGIRGVGAQRLVIIPQAIRISLPTLTNEYVTIVKLTSLVSVISLNELLLV 180
Cdd:PRK15069 109 FTLNTCAYTTEIFAGAIRSVPHGEIEAARAYGMSTFKLYRRIILPSALRRALPAYSNEVILMLHATTLAFTATVPDILKI 188
|
170 180 190
....*....|....*....|....*....|....*....
gi 2084914118 181 GQRLYAQNFLVLETLAAVAIYYVLIVTLFGWLLQWAERH 219
Cdd:PRK15069 189 ARDINSATYQPFQAFGIAAVLYLIISFVLISLFRRAERR 227
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
262-477 |
1.52e-24 |
|
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: 107.11 E-value: 1.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 262 RDIHKRYG--NHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDdapvIRqgiR 339
Cdd:TIGR02203 334 RNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAS----LR---R 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 340 RIGMVFQNFNLFpHRTILDNVILAPRyhGLADSAELRR--KGHGLLDRVGLLAHAHKYP-----HQLSGGQQQRVAIARA 412
Cdd:TIGR02203 407 QVALVSQDVVLF-NDTIANNIAYGRT--EQADRAEIERalAAAYAQDFVDKLPLGLDTPigengVLLSGGQRQRLAIARA 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084914118 413 LAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAReGMTMLIVTHEMDfALSISDRIVFMENGHVV 477
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESERLVQAALERLMQ-GRTTLVIAHRLS-TIEKADRIVVMDDGRIV 546
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
268-503 |
4.91e-24 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.86 E-value: 4.91e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 268 YGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDA---------PVIRQGI 338
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLArrlallpqhHLTPEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRIGMVfqNFNLFPHRTILDNviLAPRYHGLADSAelrrkghglLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPD 418
Cdd:PRK11231 92 TVRELV--AYGRSPWLSLWGR--LSAEDNARVNQA---------MEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 419 IMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSEGdpRVRRFIG 498
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPG--LLRTVFD 236
|
....*
gi 2084914118 499 LEQEV 503
Cdd:PRK11231 237 VEAEI 241
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
259-477 |
5.95e-24 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 100.77 E-value: 5.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfikAGKRDDAPVIRQGI 338
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRD---GQLRDLYALSEAER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRI-----GMVFQNF--NLFPHRTILDNV-----ILAPRYHGladsaELRRKGHGLLDRVGL-LAHAHKYPHQLSGGQQQ 405
Cdd:PRK11701 84 RRLlrtewGFVHQHPrdGLRMQVSAGGNIgerlmAVGARHYG-----DIRATAGDWLERVEIdAARIDDLPTTFSGGMQQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 406 RVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:PRK11701 159 RLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVV 231
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
272-485 |
1.01e-23 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 100.25 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 272 EVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLfgndfikagkrDDAPV----IRQGIRRIGMVFQN 347
Cdd:PRK15112 27 EAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLI-----------DDHPLhfgdYSYRSQRIRMIFQD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 348 --FNLFPHRTILDNVILAPRYHGLADSAELRRKGHGLLDRVGLLA-HAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDE 424
Cdd:PRK15112 96 psTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPdHASYYPHMLAPGQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084914118 425 PTSALDPELVGEVLNVIRDL-AREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI 485
Cdd:PRK15112 176 ALASLDMSMRSQLINLMLELqEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADV 237
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
273-477 |
1.26e-23 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 104.06 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 273 VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfIKAGKRDDApvirqGiRRIGMVFQNFNLFP 352
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGAD-LSQWDREEL-----G-RHIGYLPQDVELFD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 353 HrTILDN-----------VILAPRyhgladsaelrrkghglldrvglLAHAH----KYP-----------HQLSGGQQQR 406
Cdd:COG4618 420 G-TIAENiarfgdadpekVVAAAK-----------------------LAGVHemilRLPdgydtrigeggARLSGGQRQR 475
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 407 VAIARALAMEPDIMLFDEPTSALDPElvGE--VLNVIRDLAREGMTMLIVTHEMDfALSISDRIVFMENGHVV 477
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPNSNLDDE--GEaaLAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQ 545
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
259-495 |
1.66e-23 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 99.20 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFikagkrDDAPVIRQGI 338
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDI------SLLPLHARAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRIGMVFQNFNLFPHRTILDNVILAPRYHGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPD 418
Cdd:PRK10895 78 RGIGYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 419 IMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSegDPRVRR 495
Cdd:PRK10895 158 FILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ--DEHVKR 232
|
|
| PRK11123 |
PRK11123 |
arginine ABC transporter permease ArtQ; |
7-219 |
3.30e-23 |
|
arginine ABC transporter permease ArtQ;
Pssm-ID: 182979 [Multi-domain] Cd Length: 238 Bit Score: 98.21 E-value: 3.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 7 YFFSLFSvsafwkACLTVVQLSTLSWSIGLVLGFLLASAKLSGHAWLRMPASFYIWLFRSIP--LLVLLVFVYNLPQLFP 84
Cdd:PRK11123 3 EFFPLAS------AAGMTVGLAVCALIVGLALAMLFAVWESAKWRPVAWPGTALVTLLRGLPeiLVVLFIYFGSSQLLLT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 85 VTG------------------SVLSQPFYSGLIALVLTETAYMAEIHRGGLLSVLKGQREAAKALGIRGVGAQRLVIIPQ 146
Cdd:PRK11123 77 LSDgftlnlgfvqipvqmdieNFEVSPFLCGVIALSLLYAAYASQTLRGALKAVPVGQWESGQALGLSKSAIFFRLVMPQ 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 147 AIRISLPTLTNEYVTIVKLTSLVSVISLNELLLVGQRLYA---QNFLVLETlaAVAIYyvLIVTLFG-WLLQWAERH 219
Cdd:PRK11123 157 MWRHALPGLGNQWLVLLKDTALVSLISVNDLMLQTKSIATrtqEPFTWYII--AAAIY--LVITLISqYILKRIELR 229
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
235-456 |
3.42e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 102.96 E-value: 3.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 235 AQALRQPASASKKRNEPVPGQPDALLLRDIH-KRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRG 313
Cdd:COG4178 339 EEALEAADALPEAASRIETSEDGALALEDLTlRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSG 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 314 EIVLfgndfiKAGKRddapvirqgirrigMVFqnfnL-----FPHRTiLDNVILAPRYHGLADSAELRRkghgLLDRVGL 388
Cdd:COG4178 419 RIAR------PAGAR--------------VLF----LpqrpyLPLGT-LREALLYPATAEAFSDAELRE----ALEAVGL 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084914118 389 LAHAHKY------PHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDlAREGMTMLIVTH 456
Cdd:COG4178 470 GHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
261-477 |
5.68e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 102.05 E-value: 5.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAgkrddAPVIRQGIrR 340
Cdd:PRK15439 14 ARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARL-----TPAKAHQL-G 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 IGMVFQNFNLFPHRTILDNVILapryhGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIM 420
Cdd:PRK15439 88 IYLVPQEPLLFPNLSVKENILF-----GLPKRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRIL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 421 LFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIA 219
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
268-485 |
6.83e-23 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 98.13 E-value: 6.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 268 YGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDApvirqgiRRIGMVFQN 347
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA-------RRIGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 348 FNLfPHRTILDNVILAPRYHGLADSAELRRKGHGLLDR----VGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFD 423
Cdd:PRK10253 90 ATT-PGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKamqaTGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 424 EPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI 485
Cdd:PRK10253 169 EPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
265-479 |
7.66e-23 |
|
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: 96.83 E-value: 7.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 265 HKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfikagkrddAPVIRqgirrIGMV 344
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRV---------SSLLG-----LGGG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 345 FQnfnlfPHRTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDE 424
Cdd:cd03220 95 FN-----PELTGRENIYLNGRLLGL-SRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDE 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2084914118 425 PTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTD 479
Cdd:cd03220 169 VLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
273-477 |
9.68e-23 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 101.96 E-value: 9.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 273 VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFikaGKRDDAPVIRQgirrIGMVFQNFNLFP 352
Cdd:TIGR03797 468 ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDL---AGLDVQAVRRQ----LGVVLQNGRLMS 540
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 353 HrTILDNVIL-----------APRYHGLADSAELRRKG-HGLLDRVGllahahkypHQLSGGQQQRVAIARALAMEPDIM 420
Cdd:TIGR03797 541 G-SIFENIAGgapltldeaweAARMAGLAEDIRAMPMGmHTVISEGG---------GTLSGGQRQRLLIARALVRKPRIL 610
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084914118 421 LFDEPTSALDpelvgevlN-----VIRDLAREGMTMLIVTHEmdfaLSI---SDRIVFMENGHVV 477
Cdd:TIGR03797 611 LFDEATSALD--------NrtqaiVSESLERLKVTRIVIAHR----LSTirnADRIYVLDAGRVV 663
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
259-474 |
1.26e-22 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 100.85 E-value: 1.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDApviRQGI 338
Cdd:PRK10762 5 LQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQ---EAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 rriGMVFQNFNLFPHRTILDNVILAPRY---HGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAM 415
Cdd:PRK10762 82 ---GIIHQELNLIPQLTIAENIFLGREFvnrFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSF 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2084914118 416 EPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENG 474
Cdd:PRK10762 159 ESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDG 217
|
|
| artM |
PRK11122 |
arginine ABC transporter permease ArtM; |
23-218 |
1.35e-22 |
|
arginine ABC transporter permease ArtM;
Pssm-ID: 182978 [Multi-domain] Cd Length: 222 Bit Score: 96.18 E-value: 1.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 23 TVVQLSTLSWSIGLVLGFLLASAKLSGHAWLRMPASFYIWLFRSIPLLVLLVFVYNLPQLF------PVTGSVLSQPFYS 96
Cdd:PRK11122 14 TSLTLTVASLLVALVLALIFTIILTLKTPVLVWLVRGYITLFTGTPLLVQIFLIYYGPGQFpwlqeyPWLWHLLSQPWLC 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 97 GLIALVLTETAYMAEIHRGGLLSVLKGQREAAKALGIRGVGAQRlVIIPQAIRISLPTLTNEYVTIVKLTSLVSVISLNE 176
Cdd:PRK11122 94 AMLALALNSAAYSTQLFYGAVRAIPEGQWQSCAALGMSKKQTLR-ILLPYAFKRALSSYSNEVVLVFKSTSLAYTITLMD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2084914118 177 LLLVGQRLYAQNFLVLETLAAVAIYYVL--IVTLfgwLLQWAER 218
Cdd:PRK11122 173 VMGYSQLLYGRTYDVMVFGAAGIIYLVVngLLTL---LMRLIER 213
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
261-477 |
1.72e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 100.63 E-value: 1.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDAPVirqgirR 340
Cdd:PRK09700 8 MAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL------G 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 IGMVFQNFNLFPHRTILDNV----ILAPRYHG--LADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALA 414
Cdd:PRK09700 82 IGIIYQELSVIDELTVLENLyigrHLTKKVCGvnIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 415 MEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
269-476 |
2.08e-22 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 100.50 E-value: 2.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 269 GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDAPvirqgirRIGMVFQNF 348
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK-------HIGYLPQDV 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 349 NLFPHrTILDNVilaPRYHGLADSAELRRKGHglldrvglLAHAH----KYPH-----------QLSGGQQQRVAIARAL 413
Cdd:TIGR01842 402 ELFPG-TVAENI---ARFGENADPEKIIEAAK--------LAGVHelilRLPDgydtvigpggaTLSGGQRQRIALARAL 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084914118 414 AMEPDIMLFDEPTSALDPElvGE--VLNVIRDLAREGMTMLIVTHEMDfALSISDRIVFMENGHV 476
Cdd:TIGR01842 470 YGDPKLVVLDEPNSNLDEE--GEqaLANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRI 531
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
277-485 |
4.82e-22 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 96.73 E-value: 4.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 277 IDLVVKPGEVISIIGPSGSGKTSLIRTINSLesID-----RGEIVLF-GNDFIKAGKRDDapviRQGI-RRIGMVFQN-- 347
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGL--IDypgrvMAEKLEFnGQDLQRISEKER----RNLVgAEVAMIFQDpm 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 348 FNLFPHRTILDNVILAPRYHGLADSAELRRKGHGLLDRVGLLAHAHK---YPHQLSGGQQQRVAIARALAMEPDIMLFDE 424
Cdd:PRK11022 100 TSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084914118 425 PTSALDPELVGEVLNVIRDLAR-EGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI 485
Cdd:PRK11022 180 PTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
252-477 |
4.84e-22 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 99.51 E-value: 4.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 252 VPGQPDALLLR---------DIHKRY-GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGND 321
Cdd:COG5265 342 VADAPDAPPLVvgggevrfeNVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQD 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 322 FikagkRDdapVIRQGIRR-IGMVFQNFNLFpHRTILDNVilapRYhGL--ADSAELRrkghglldRVGLLAHAHKY--- 395
Cdd:COG5265 422 I-----RD---VTQASLRAaIGIVPQDTVLF-NDTIAYNI----AY-GRpdASEEEVE--------AAARAAQIHDFies 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 396 -PHQ-----------LSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAReGMTMLIVTHEmdfaLS 463
Cdd:COG5265 480 lPDGydtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR-GRTTLVIAHR----LS 554
|
250
....*....|....*..
gi 2084914118 464 I---SDRIVFMENGHVV 477
Cdd:COG5265 555 TivdADEILVLEAGRIV 571
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
259-477 |
5.22e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 94.75 E-value: 5.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTI--NSLESIDRGEIVLFGNDFI--------KAGkr 328
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILelspderaRAG-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 329 ddapvirqgirrIGMVFQ---------NFNLFphRTILDNVILAPryhglADSAELRRKGHGLLDRVGL-LAHAHKYPHQ 398
Cdd:COG0396 79 ------------IFLAFQypveipgvsVSNFL--RTALNARRGEE-----LSAREFLKLLKEKMKELGLdEDFLDRYVNE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 399 -LSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHE---MDFalsIS-DRIVFMEN 473
Cdd:COG0396 140 gFSGGEKKRNEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYqriLDY---IKpDFVHVLVD 216
|
....
gi 2084914118 474 GHVV 477
Cdd:COG0396 217 GRIV 220
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
270-476 |
5.65e-22 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 94.46 E-value: 5.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 270 NHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGndfiKAGKRDDAPVIRqgiRRIGMVFQNFN 349
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDG----KPISQYEHKYLH---SKVSLVGQEPV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 350 LFPhRTILDNVIlapryHGLADSA-----ELRRKGHGLlDRVGLLAH-----AHKYPHQLSGGQQQRVAIARALAMEPDI 419
Cdd:cd03248 99 LFA-RSLQDNIA-----YGLQSCSfecvkEAAQKAHAH-SFISELASgydteVGEKGSQLSGGQKQRVAIARALIRNPQV 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 420 MLFDEPTSALDPELVGEVLNVIRDlAREGMTMLIVTHEMDfALSISDRIVFMENGHV 476
Cdd:cd03248 172 LILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLS-TVERADQILVLDGGRI 226
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
269-456 |
7.00e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 93.40 E-value: 7.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 269 GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLfgndfikAGKRDDAPVIRQGIRRIGmvFQNF 348
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKL-------DGGDIDDPDVAEACHYLG--HRNA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 349 nLFPHRTILDNVILAPRYHGLADSAElrrkgHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSA 428
Cdd:PRK13539 84 -MKPALTVAENLEFWAAFLGGEELDI-----AAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
|
170 180
....*....|....*....|....*....
gi 2084914118 429 LDPELVGEVLNVIRD-LAREGMtMLIVTH 456
Cdd:PRK13539 158 LDAAAVALFAELIRAhLAQGGI-VIAATH 185
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
266-477 |
8.01e-22 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 94.51 E-value: 8.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 266 KRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfikaGKRDDAPVIRQGIRRI---- 341
Cdd:TIGR02323 11 KSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRS----GAELELYQLSEAERRRlmrt 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 342 --GMVFQNFNLFPHRTILDNVILAPRYHGLADS--AELRRKGHGLLDRVGL-LAHAHKYPHQLSGGQQQRVAIARALAME 416
Cdd:TIGR02323 87 ewGFVHQNPRDGLRMRVSAGANIGERLMAIGARhyGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQIARNLVTR 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084914118 417 PDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:TIGR02323 167 PRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVV 228
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
259-459 |
1.06e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 93.63 E-value: 1.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAgkrddAPVI-RQg 337
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTL-----KPEIyRQ- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 338 irRIGMVFQNFNLFPHrTILDNVILAPRYHGLA-DSAELRRKghglLDRVGLLAHAHKYP-HQLSGGQQQRVAIARALAM 415
Cdd:PRK10247 82 --QVSYCAQTPTLFGD-TVYDNLIFPWQIRNQQpDPAIFLDD----LERFALPDTILTKNiAELSGGEKQRISLIRNLQF 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2084914118 416 EPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMD 459
Cdd:PRK10247 155 MPKVLLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHDKD 199
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
248-482 |
1.26e-21 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 98.20 E-value: 1.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 248 RNEPVPGQPDALLLRDIHKRYGNH---------EVLKGIDLVVKPGEVISIIGPSGSGKTSLIrtiNSLESIDRGEIVLF 318
Cdd:TIGR00955 6 RNSDVFGRVAQDGSWKQLVSRLRGcfcrerprkHLLKNVSGVAKPGELLAVMGSSGAGKTTLM---NALAFRSPKGVKGS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 319 GNDFIKaGKRDDAPVIRqgiRRIGMVFQNFNLFPHRTILDNVILapryhgladSAELRRKGHG-----------LLDRVG 387
Cdd:TIGR00955 83 GSVLLN-GMPIDAKEMR---AISAYVQQDDLFIPTLTVREHLMF---------QAHLRMPRRVtkkekrervdeVLQALG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 388 LLAHAHK---YPHQ---LSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFA 461
Cdd:TIGR00955 150 LRKCANTrigVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSE 229
|
250 260
....*....|....*....|..
gi 2084914118 462 L-SISDRIVFMENGHVVTDASP 482
Cdd:TIGR00955 230 LfELFDKIILMAEGRVAYLGSP 251
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
255-488 |
1.76e-21 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 97.29 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 255 QPDALLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDdapVI 334
Cdd:PRK11288 1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTA---AL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 335 RQGIRRIgmvFQNFNLFPHRTILDNVILA--PRYHGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARA 412
Cdd:PRK11288 78 AAGVAII---YQELHLVPEMTVAENLYLGqlPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 413 LAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRI-VFMENGHVVTDASPASIRSE 488
Cdd:PRK11288 155 LARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAItVFKDGRYVATFDDMAQVDRD 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
274-485 |
2.13e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 97.62 E-value: 2.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 274 LKGIDLVVKPGEVISIIGPSGSGKT----SLIRTINSLESIDRGEIVLF---GNDFIKAGKRDDAPVIRQGIRRIGMVFQ 346
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAGGLVQCDKMLLrrrSRQVIELSEQSAAQMRHVRGADMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 347 N--FNLFPHRTILDNVILAPRYHGLADSAELRRKGHGLLDRVGL-LAHA--HKYPHQLSGGQQQRVAIARALAMEPDIML 421
Cdd:PRK10261 112 EpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIpEAQTilSRYPHQLSGGMRQRVMIAMALSCRPAVLI 191
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084914118 422 FDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI 485
Cdd:PRK10261 192 ADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
148-487 |
2.39e-21 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 98.12 E-value: 2.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 148 IRISLPTLTNEYVTIVKLTSLVSV-ISLNELLLVGQRLYAQNFLVLETLAAVAIYYVLIVT--LFGWLLQW--AERHLDL 222
Cdd:PLN03232 1123 IRFTLANTSSNRWLTIRLETLGGVmIWLTATFAVLRNGNAENQAGFASTMGLLLSYTLNITtlLSGVLRQAskAENSLNS 1202
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 223 SRKNARTLDdtqaqaLRQPASASKKRNEPVPGQPDALLLR--DIHKRY--GNHEVLKGIDLVVKPGEVISIIGPSGSGKT 298
Cdd:PLN03232 1203 VERVGNYID------LPSEATAIIENNRPVSGWPSRGSIKfeDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKS 1276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 299 SLIRTINSLESIDRGEIVLFGNDFIKAGKRD---------DAPVIRQGIRRigmvfqnFNLFPHRTildnvilapryHGL 369
Cdd:PLN03232 1277 SMLNALFRIVELEKGRIMIDDCDVAKFGLTDlrrvlsiipQSPVLFSGTVR-------FNIDPFSE-----------HND 1338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 370 ADSAELRRKGH--GLLDR--VGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLA 445
Cdd:PLN03232 1339 ADLWEALERAHikDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEF 1418
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2084914118 446 REgMTMLIVTHEMDFALSiSDRIVFMENGHVVTDASPASIRS 487
Cdd:PLN03232 1419 KS-CTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLS 1458
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
267-482 |
8.80e-21 |
|
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: 90.55 E-value: 8.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 267 RYGNH--EVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDdapvIRqgiRRIGMV 344
Cdd:cd03369 15 RYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED----LR---SSLTII 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 345 FQNFNLFPHrTILDNVILAPRYHGLADSAELRRKGHGLldrvgllahahkyphQLSGGQQQRVAIARALAMEPDIMLFDE 424
Cdd:cd03369 88 PQDPTLFSG-TIRSNLDPFDEYSDEEIYGALRVSEGGL---------------NLSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084914118 425 PTSALDPELVGEVLNVIRDLArEGMTMLIVTHEM----DFalsisDRIVFMENGHVVTDASP 482
Cdd:cd03369 152 ATASIDYATDALIQKTIREEF-TNSTILTIAHRLrtiiDY-----DKILVMDAGEVKEYDHP 207
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
261-479 |
1.01e-20 |
|
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: 90.85 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKR-YGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfikAGKRDDAPVirqgiR 339
Cdd:cd03267 23 LKSLFKRkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV---PWKRRKKFL-----R 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 340 RIGMVF-QNFNLFPHRTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPD 418
Cdd:cd03267 95 RIGVVFgQKTQLWWDLPVIDSFYLLAAIYDL-PPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPE 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084914118 419 IMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTD 479
Cdd:cd03267 174 ILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
259-456 |
1.15e-20 |
|
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: 89.73 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAgkrddAPVIRQGI 338
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ-----RDEPHENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRIGmvfQNFNLFPHRTILDNVILAPRYHGLADsaelrRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPD 418
Cdd:TIGR01189 76 LYLG---HLPGLKPELSALENLHFWAAIHGGAQ-----RTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRP 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 2084914118 419 IMLFDEPTSALDPELVGEVLNVIRD-LAREGMTmLIVTH 456
Cdd:TIGR01189 148 LWILDEPTTALDKAGVALLAGLLRAhLARGGIV-LLTTH 185
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
262-490 |
1.62e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 95.17 E-value: 1.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 262 RDIHKRYGNH---EVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAgkrdDAPVIRqgi 338
Cdd:TIGR00958 482 QDVSFSYPNRpdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQY----DHHYLH--- 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRIGMVFQNFNLFpHRTILDNVILAPRYhglADSAELRRkghglldrVGLLAHAH----KYPH-----------QLSGGQ 403
Cdd:TIGR00958 555 RQVALVGQEPVLF-SGSVRENIAYGLTD---TPDEEIMA--------AAKAANAHdfimEFPNgydtevgekgsQLSGGQ 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 404 QQRVAIARALAMEPDIMLFDEPTSALDPE---LVGEvlnvirDLAREGMTMLIVTHEmdfaLSI---SDRIVFMENGHVV 477
Cdd:TIGR00958 623 KQRIAIARALVRKPRVLILDEATSALDAEceqLLQE------SRSRASRTVLLIAHR----LSTverADQILVLKKGSVV 692
|
250
....*....|...
gi 2084914118 478 TDASPASIRSEGD 490
Cdd:TIGR00958 693 EMGTHKQLMEDQG 705
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
261-475 |
1.91e-20 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 87.50 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIvlfgndfikagkrddapvirqgirr 340
Cdd:cd03221 3 LENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 igmvfqnfnlfphrTILDNVILApryhgladsaelrrkghglldrvgllahahkYPHQLSGGQQQRVAIARALAMEPDIM 420
Cdd:cd03221 58 --------------TWGSTVKIG-------------------------------YFEQLSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2084914118 421 LFDEPTSALDPELVGEVLNVIRDLARegmTMLIVTHEMDFALSISDRIVFMENGH 475
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEALKEYPG---TVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
275-476 |
2.82e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 93.70 E-value: 2.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 275 KGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfIKAGKRDDApvIRQGIRRIGMVFQNFNLFPHR 354
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKD-ISPRSPLDA--VKKGMAYITESRRDNGFFPNF 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 355 TILDNVILAPRYH--------GLADSAELRRKGHGLLDRVGLLAHA-HKYPHQLSGGQQQRVAIARALAMEPDIMLFDEP 425
Cdd:PRK09700 357 SIAQNMAISRSLKdggykgamGLFHEVDEQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2084914118 426 TSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHV 476
Cdd:PRK09700 437 TRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| TM_PBP2 |
cd06261 |
Transmembrane subunit (TM) found in Periplasmic Binding Protein (PBP)-dependent ATP-Binding ... |
25-211 |
5.64e-20 |
|
Transmembrane subunit (TM) found in Periplasmic Binding Protein (PBP)-dependent ATP-Binding Cassette (ABC) transporters which generally bind type 2 PBPs. These types of transporters consist of a PBP, two TMs, and two cytoplasmic ABC ATPase subunits, and are mainly involved in importing solutes from the environment. The solute is captured by the PBP which delivers it to a gated translocation pathway formed by the two TMs. The two ABCs bind and hydrolyze ATP and drive the transport reaction. For these transporters the ABCs and TMs are on independent polypeptide chains. These systems transport a diverse range of substrates. Most are specific for a single substrate or a group of related substrates; however some transporters are more promiscuous, transporting structurally diverse substrates such as the histidine/lysine and arginine transporter in Enterobacteriaceae. In the latter case, this is achieved through binding different PBPs with different specificities to the TMs. For other promiscuous transporters such as the multiple-sugar transporter Msm of Streptococcus mutans, the PBP has a wide substrate specificity. These transporters include the maltose-maltodextrin, phosphate and sulfate transporters, among others.
Pssm-ID: 119394 [Multi-domain] Cd Length: 190 Bit Score: 87.72 E-value: 5.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 25 VQLSTLSWSIGLVLGFLLASAKLSGHAWLRMPASFYIWLFRSIPLLVLLVFVYnlpQLFPVTGSVLSQPFYS--GLIALV 102
Cdd:cd06261 5 LLLALIATLLALVLGLLLGIILARKRGKLDRLLRRIIDLLLSLPSLVLGLLLV---LLFGVLLGWGILPGLGlpALILAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 103 LTETAYMAEIHRGGLLSVLKGQREAAKALGIRGVGAQRLVIIPQAIRISLPTLTNEYVTIVKLTSLVSVISLNELLLVGQ 182
Cdd:cd06261 82 LLIAPFARLIRRAALESIPKDLVEAARALGASPWQIFRRIILPLALPPILTGLVLAFARALGEFALVSFLGGGEAPGPGT 161
|
170 180
....*....|....*....|....*....
gi 2084914118 183 RLYAQNFLVLETLAAVAIYYVLIVTLFGW 211
Cdd:cd06261 162 GLLLIFAILFPGDLGVAAAVALILLLLSL 190
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
261-470 |
6.53e-20 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 88.48 E-value: 6.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRygnheVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLES--IDRGEIVLFGNDFikagkRDDAPVIrQGI 338
Cdd:COG2401 38 LRVVERY-----VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQF-----GREASLI-DAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRIGMVFQNFNlfphrtILDNVilapryhGLADSAELRRKghglldrvgllahahkyPHQLSGGQQQRVAIARALAMEPD 418
Cdd:COG2401 107 GRKGDFKDAVE------LLNAV-------GLSDAVLWLRR-----------------FKELSTGQKFRFRLALLLAERPK 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2084914118 419 IMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDF--ALsISDRIVF 470
Cdd:COG2401 157 LLVIDEFCSHLDRQTAKRVARNLQKLARRaGITLVVATHHYDVidDL-QPDLLIF 210
|
|
| BatB |
COG4597 |
ABC-type amino acid transport system, permease component [Amino acid transport and metabolism]; ... |
67-168 |
8.34e-20 |
|
ABC-type amino acid transport system, permease component [Amino acid transport and metabolism];
Pssm-ID: 443651 [Multi-domain] Cd Length: 397 Bit Score: 91.36 E-value: 8.34e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 67 IPLLVLLV----FVYNLPQL--FPVT-GSVLSQPFYSGLIALVLTETAYMAEIHRGGLLSVLKGQREAAKALGIRGVGAQ 139
Cdd:COG4597 231 LPLLAFLLlgapLSLDYPELkgFNFRgGLTLSPEFVALLLALSLYTAAFIAEIVRAGIQAVSKGQTEAARALGLRPGQTL 310
|
90 100
....*....|....*....|....*....
gi 2084914118 140 RLVIIPQAIRISLPTLTNEYVTIVKLTSL 168
Cdd:COG4597 311 RLVVLPQALRVIIPPLTSQYLNLTKNSSL 339
|
|
| HEQRo_perm_3TM |
TIGR01726 |
amine acid ABC transporter, permease protein, 3-TM region, His/Glu/Gln/Arg/opine family; This ... |
16-115 |
1.37e-19 |
|
amine acid ABC transporter, permease protein, 3-TM region, His/Glu/Gln/Arg/opine family; This model represents one of several classes of multiple membrane spanning regions found immediately N-terminal to the domain described by pfam00528, binding-protein-dependent transport systems inner membrane component. The region covered by this model generally is predicted to contain three transmembrane helices. Substrate specificities attributed to members of this family include histidine, arginine, glutamine, glutamate, and (in Agrobacterium) the opines octopine and nopaline. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 130787 [Multi-domain] Cd Length: 99 Bit Score: 83.74 E-value: 1.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 16 AFWKACLTVVQLSTLSWSIGLVLGFLLASAKLSGHAWLRMPASFYIWLFRSIPLLVLLVFVYNlpqLFPVTGSVLSqPFY 95
Cdd:TIGR01726 4 FLLKGLLLTLLLSVLSILLGLVLGLLLALLRLSGNRPLRWIATVYVELFRGTPLLVQLFFIYF---GLPLIGIRLS-PLT 79
|
90 100
....*....|....*....|
gi 2084914118 96 SGLIALVLTETAYMAEIHRG 115
Cdd:TIGR01726 80 AAVIALTLFYGAYLAEIFRG 99
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
261-486 |
4.17e-19 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 90.95 E-value: 4.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDD-APVIR---Q 336
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAvCPRIAympQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 337 GIRRigmvfqnfNLFPHRTILDNVILAPRYHGLaDSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAME 416
Cdd:NF033858 84 GLGK--------NLYPTLSVFENLDFFGRLFGQ-DAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHD 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 417 PDIMLFDEPTSALDP-------ELVGEvlnvIRDlAREGMTMLIVTHEMD----FalsisDRIVFMENGHVVTDASPASI 485
Cdd:NF033858 155 PDLLILDEPTTGVDPlsrrqfwELIDR----IRA-ERPGMSVLVATAYMEeaerF-----DWLVAMDAGRVLATGTPAEL 224
|
.
gi 2084914118 486 R 486
Cdd:NF033858 225 L 225
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
277-491 |
8.21e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 89.52 E-value: 8.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 277 IDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIdRGEIVLFGNDFikagkRDDAPviRQGIRRIGMVFQNFNLFpHRTI 356
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIEL-----RELDP--ESWRKHLSWVGQNPQLP-HGTL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 357 LDNVILApryHGLADSAELRRkghgLLDR------VGLLAHAHKYPHQ-----LSGGQQQRVAIARALAMEPDIMLFDEP 425
Cdd:PRK11174 440 RDNVLLG---NPDASDEQLQQ----ALENawvsefLPLLPQGLDTPIGdqaagLSVGQAQRLALARALLQPCQLLLLDEP 512
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2084914118 426 TSALD---PELVGEVLNVirdlAREGMTMLIVTHEMDFaLSISDRIVFMENGHVVTDASPASIRSEGDP 491
Cdd:PRK11174 513 TASLDahsEQLVMQALNA----ASRRQTTLMVTHQLED-LAQWDQIWVMQDGQIVQQGDYAELSQAGGL 576
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
255-477 |
1.06e-18 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 86.09 E-value: 1.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 255 QPDALLLRDIHKRYGN-HEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAgkrddapv 333
Cdd:PRK15056 3 QQAGIVVNDVTVTWRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQA-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 334 IRQGIrrIGMVFQNFNL---FPhrTILDNVILAPRYHGLA----DSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQR 406
Cdd:PRK15056 75 LQKNL--VAYVPQSEEVdwsFP--VLVEDVVMMGRYGHMGwlrrAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084914118 407 VAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVfMENGHVV 477
Cdd:PRK15056 151 VFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVL 220
|
|
| PRK15107 |
PRK15107 |
glutamate/aspartate ABC transporter permease GltK; |
2-204 |
1.83e-18 |
|
glutamate/aspartate ABC transporter permease GltK;
Pssm-ID: 185062 [Multi-domain] Cd Length: 224 Bit Score: 84.11 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 2 AFDWAYFFSlfSVSAFWKACLTVVQLSTLSWSIGLVLGFLLASAKLSGHAWLRMPASFYIWLFRSIPLLVLLVFVY---- 77
Cdd:PRK15107 3 EFDWSSIVP--SLPYLLDGLVITLKITVTAVVIGILWGTILAVMRLSSFKPVAWFAKAYVNVFRSIPLVMVLLWFYlivp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 78 ----NLPQLFPVTGSVLsqpfYSGLIALVLTETAYMAEIHRGGLLSVLKGQREAAKALGIRGVGAQRLVIIPQAIRISLP 153
Cdd:PRK15107 81 gflqNVLGLSPKTDIRL----ISAMVAFSMFEAAYYSEIIRAGIQSISRGQSSAALALGMTHWQSMKLIILPQAFRAMVP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2084914118 154 TLTNEYVTIVKLTSLVSVISLNELLLVGQRLYAQNFLVLE-TLAAVAIYYVL 204
Cdd:PRK15107 157 LLLTQGIVLFQDTSLVYVLSLADFFRTASTIGERDGTQVEmILFAGFVYFVI 208
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
277-494 |
1.94e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 88.04 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 277 IDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDdapVIRQGI-------RRIGMVfqnfn 349
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRD---AIRAGImlcpedrKAEGII----- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 350 lfPHRTILDNV-ILAPRYHGLADSAELRRKGHGLLDR-VGLLAHAHKYPHQ----LSGGQQQRVAIARALAMEPDIMLFD 423
Cdd:PRK11288 344 --PVHSVADNInISARRHHLRAGCLINNRWEAENADRfIRSLNIKTPSREQlimnLSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2084914118 424 EPTSALDpelVG---EVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVV-----TDASPASIRSEGDPRVR 494
Cdd:PRK11288 422 EPTRGID---VGakhEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAgelarEQATERQALSLALPRTS 497
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
261-474 |
3.41e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 87.09 E-value: 3.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGN--DFiKAGKRddapVIRQGI 338
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeiDF-KSSKE----ALENGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 rriGMVFQNFNLFPHRTILDNVILA--PRYHGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAME 416
Cdd:PRK10982 76 ---SMVHQELNLVLQRSVMDNMWLGryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYN 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 417 PDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENG 474
Cdd:PRK10982 153 AKIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
253-485 |
5.72e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 83.68 E-value: 5.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 253 PGQPDA-LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDF----IKAGK 327
Cdd:PRK10575 5 TNHSDTtFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLeswsSKAFA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 328 RDDAPVIRQGIRRIGMvfqnfnlfphrTILDNVILApRY--HGLAD--SAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQ 403
Cdd:PRK10575 85 RKVAYLPQQLPAAEGM-----------TVRELVAIG-RYpwHGALGrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 404 QQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASP 482
Cdd:PRK10575 153 RQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTP 232
|
...
gi 2084914118 483 ASI 485
Cdd:PRK10575 233 AEL 235
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
273-488 |
8.87e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 84.19 E-value: 8.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 273 VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTI------NSLESIDRgeIVLFGNDFIK--AGKRddapviRQGIRR-IGM 343
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAIcgitkdNWHVTADR--FRWNGIDLLKlsPRER------RKIIGReIAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 344 VFQNFN--LFPHRTI---LDNVILAPRYHGladsAELRRKGH------GLLDRVGLLAHAH---KYPHQLSGGQQQRVAI 409
Cdd:COG4170 94 IFQEPSscLDPSAKIgdqLIEAIPSWTFKG----KWWQRFKWrkkraiELLHRVGIKDHKDimnSYPHELTEGECQKVMI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 410 ARALAMEPDIMLFDEPTSALDPELVGEVLnviRDLAR----EGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI 485
Cdd:COG4170 170 AMAIANQPRLLIADEPTNAMESTTQAQIF---RLLARlnqlQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQI 246
|
...
gi 2084914118 486 RSE 488
Cdd:COG4170 247 LKS 249
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
275-485 |
1.56e-17 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 82.05 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 275 KGIDLVVKPGEVISIIGPSGSGKTslIRTINSLESIDRGEIVLFGNDFIkagkrDDAPVIRQGIR--RIGMVFQN----F 348
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLL-----DGKPVAPCALRgrKIATIMQNprsaF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 349 NlfPHRTILDNVILAPRYHG-LADSAELRRkghgLLDRVGLlAHAHK----YPHQLSGGQQQRVAIARALAMEPDIMLFD 423
Cdd:PRK10418 93 N--PLHTMHTHARETCLALGkPADDATLTA----ALEAVGL-ENAARvlklYPFEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 424 EPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI 485
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
256-471 |
2.10e-17 |
|
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: 85.22 E-value: 2.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 256 PDALLLRDIHkRYG-NHEVLKGIDlVVKPGEVISIIGPSGSGKTSLIRtinslesIDRGEIV--LfgndfikaGKRDDAP 332
Cdd:COG1245 72 PEELEEDPVH-RYGeNGFRLYGLP-VPKKGKVTGILGPNGIGKSTALK-------ILSGELKpnL--------GDYDEEP 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 333 VIRQGIRRigmvFQNFNLFPHRTILDN-----------VILAPRYHG-----LADSAELRRKGHGLLDRVGLLAHAHKYP 396
Cdd:COG1245 135 SWDEVLKR----FRGTELQDYFKKLANgeikvahkpqyVDLIPKVFKgtvreLLEKVDERGKLDELAEKLGLENILDRDI 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 397 HQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDpelVGEVLNV---IRDLAREGMTMLIVTHemDFAL--SISDRIVFM 471
Cdd:COG1245 211 SELSGGELQRVAIAAALLRDADFYFFDEPSSYLD---IYQRLNVarlIRELAEEGKYVLVVEH--DLAIldYLADYVHIL 285
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
276-456 |
2.74e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 80.23 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 276 GIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGndfikagkrddapvirQGIRRIGMVFqNFNLF---- 351
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG----------------EPIRRQRDEY-HQDLLylgh 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 352 -----PHRTILDNVILAPRYHGLADSAELrrkgHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPT 426
Cdd:PRK13538 82 qpgikTELTALENLRFYQRLHGPGDDEAL----WEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPF 157
|
170 180 190
....*....|....*....|....*....|
gi 2084914118 427 SALDPELVGEVLNVIRDLAREGMTMLIVTH 456
Cdd:PRK13538 158 TAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
261-482 |
4.81e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.93 E-value: 4.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 261 LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVlfgndfikagkrddapviRQGIRR 340
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK------------------RNGKLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 IGMVFQNFNLFPhrTILDNVILAPRYHGLADSAELRRKghglLDRVGLlAHAHKYPHQ-LSGGQQQRVAIARALAMEPDI 419
Cdd:PRK09544 69 IGYVPQKLYLDT--TLPLTVNRFLRLRPGTKKEDILPA----LKRVQA-GHLIDAPMQkLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084914118 420 MLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMeNGHVVTDASP 482
Cdd:PRK09544 142 LVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTP 204
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
271-485 |
8.69e-17 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 80.26 E-value: 8.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 271 HEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTI--------NSLESIDRGEIVLFGNDFikagKRDDAPviRQGIRRIG 342
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALagdltgggAPRGARVTGDVTLNGEPL----AAIDAP--RLARLRAV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 343 MVFQNFNLFPHRTilDNVILAPRYHGLADSAELRRKGHGLLDRVGLLAHAHKYPHQ----LSGGQQQRVAIARALAM--- 415
Cdd:PRK13547 88 LPQAAQPAFAFSA--REIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRdvttLSGGELARVQFARVLAQlwp 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 416 ------EPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASI 485
Cdd:PRK13547 166 phdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
191-474 |
9.08e-17 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 82.76 E-value: 9.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 191 VLETLAAVAIYYVLIVTLF----------GWLlqwAERHLDLSRKNARTLddtqAQAL-RQPASASKKRNEPVPgQPDAL 259
Cdd:PRK10938 177 LLASLHQSGITLVLVLNRFdeipdfvqfaGVL---ADCTLAETGEREEIL----QQALvAQLAHSEQLEGVQLP-EPDEP 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 260 L-------------LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIrtinSLESIDR-----GEIVLFGNd 321
Cdd:PRK10938 249 SarhalpaneprivLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLL----SLITGDHpqgysNDLTLFGR- 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 322 fikagKRDDAPVIRQGIRRIGMVFQNFNLfPHR--TILDNVILAPRYH--GL--ADSAELRRKGHGLLDRVGLLAHAHKY 395
Cdd:PRK10938 324 -----RRGSGETIWDIKKHIGYVSSSLHL-DYRvsTSVRNVILSGFFDsiGIyqAVSDRQQKLAQQWLDILGIDKRTADA 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 396 P-HQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDP---ELVGEVLNVirdLAREGMTMLIVT--HEMDFALSISDRIV 469
Cdd:PRK10938 398 PfHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPlnrQLVRRFVDV---LISEGETQLLFVshHAEDAPACITHRLE 474
|
....*
gi 2084914118 470 FMENG 474
Cdd:PRK10938 475 FVPDG 479
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
259-481 |
9.69e-17 |
|
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: 83.25 E-value: 9.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYG-NHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFikagKRDDAPVIRQg 337
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSL----KDIDRHTLRQ- 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 338 irRIGMVFQNFNLFPHrTILDNVILAPRYHGLADS-------AELRRKGHGLldRVGLLAHAHKYPHQLSGGQQQRVAIA 410
Cdd:TIGR01193 549 --FINYLPQEPYIFSG-SILENLLLGAKENVSQDEiwaaceiAEIKDDIENM--PLGYQTELSEEGSSISGGQKQRIALA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084914118 411 RALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREgmTMLIVTHEMDFAlSISDRIVFMENGHVVTDAS 481
Cdd:TIGR01193 624 RALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGS 691
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
259-477 |
1.12e-16 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 82.53 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTIN------SLEsidrGEIVLfgndfikagkrDDAP 332
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSgvyphgSYE----GEILF-----------DGEV 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 333 VIRQGIR---RIGMVF--QNFNLFPHRTILDNVILA--PRYHGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQ 405
Cdd:NF040905 67 CRFKDIRdseALGIVIihQELALIPYLSIAENIFLGneRAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQ 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084914118 406 RVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:NF040905 147 LVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
256-471 |
1.17e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 82.93 E-value: 1.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 256 PDALLLRDIHkRYG-NHEVLKGIDlVVKPGEVISIIGPSGSGKTSLIRtinslesIDRGEIVLFGNDFIKAGKRDDapVI 334
Cdd:PRK13409 72 PEELEEEPVH-RYGvNGFKLYGLP-IPKEGKVTGILGPNGIGKTTAVK-------ILSGELIPNLGDYEEEPSWDE--VL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 335 RqgiRRIGMVFQNFnlFphRTILDNVI----------LAPRY-HG----LADSAELRRKGHGLLDRVGLLAHAHKYPHQL 399
Cdd:PRK13409 141 K---RFRGTELQNY--F--KKLYNGEIkvvhkpqyvdLIPKVfKGkvreLLKKVDERGKLDEVVERLGLENILDRDISEL 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 400 SGGQQQRVAIARALAMEPDIMLFDEPTSALDpelVGEVLNV---IRDLArEGMTMLIVTHEM---DFalsISDRIVFM 471
Cdd:PRK13409 214 SGGELQRVAIAAALLRDADFYFFDEPTSYLD---IRQRLNVarlIRELA-EGKYVLVVEHDLavlDY---LADNVHIA 284
|
|
| PRK15135 |
PRK15135 |
histidine ABC transporter permease HisQ; |
19-227 |
1.23e-16 |
|
histidine ABC transporter permease HisQ;
Pssm-ID: 185089 [Multi-domain] Cd Length: 228 Bit Score: 79.07 E-value: 1.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 19 KACLTVVQLSTLSWSIGLVLGFLLASAKLSGHAWLRMPASFYIWLFRSIPLLVLLVFVYNLPQ--LFPVTGSV-LSQ--- 92
Cdd:PRK15135 11 QGALVTLELALSSVVLAVIIGLIGAGGKLSQNRLLGLIFEGYTTLIRGVPDLVLMLLIFYGLQiaLNSVTEALgVGQidi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 93 -PFYSGLIALVLTETAYMAEIHRGGLLSVLKGQREAAKALGIRGVGAQRLVIIPQAIRISLPTLTNEYVTIVKLTSLVSV 171
Cdd:PRK15135 91 dPMVAGIITLGFIYGAYFTETFRGAFMAVPKGHIEAATAFGFTRGQVFRRIMFPAMMRYALPGIGNNWQVILKATALVSL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 172 ISLNELL----LVGQRLYAQNFLVLetlaAVAIYYVLIVTLFGWLLQWAERHLDLSRKNA 227
Cdd:PRK15135 171 LGLEDVVkatqLAGKSTWEPFYFAI----VCGVIYLVFTTVSNGVLLWLERRYSVGVKRA 226
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
273-456 |
1.87e-16 |
|
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: 77.92 E-value: 1.87e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 273 VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNdfikaGKRDDAPVIRQGIRRIGmvFQNfNLFP 352
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGG-----PLDFQRDSIARGLLYLG--HAP-GIKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 353 HRTILDNVILAPRYHGLADSAELrrkghglLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPE 432
Cdd:cd03231 87 TLSVLENLRFWHADHSDEQVEEA-------LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKA 159
|
170 180
....*....|....*....|....
gi 2084914118 433 LVGEVLNVIRDLAREGMTMLIVTH 456
Cdd:cd03231 160 GVARFAEAMAGHCARGGMVVLTTH 183
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
270-456 |
2.08e-16 |
|
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: 76.81 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 270 NHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGeivlfgndfikagkrddapvirqgirRIGMVFQNFN 349
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSG--------------------------RIGMPEGEDL 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 350 LF-PHRTILdnvilaPRyhgladsaelrrkghglldrvGLLAHAHKYP--HQLSGGQQQRVAIARALAMEPDIMLFDEPT 426
Cdd:cd03223 67 LFlPQRPYL------PL---------------------GTLREQLIYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEAT 119
|
170 180 190
....*....|....*....|....*....|
gi 2084914118 427 SALDPELVGEVLNVIRDlarEGMTMLIVTH 456
Cdd:cd03223 120 SALDEESEDRLYQLLKE---LGITVISVGH 146
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
254-488 |
2.19e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 80.55 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 254 GQPDALLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSgktslirtinsleSIDRGEIV--LFGNDfikAGKR--- 328
Cdd:NF000106 9 GARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GA-------------A**RGALPahV*GPD---AGRRpwr 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 329 -DDAPVIRQGIRRigmvfqnfNLFPHRTIL----------DNVILAPRYHGLAdSAELRRKGHGLLDRVGLLAHAHKYPH 397
Cdd:NF000106 73 f*TWCANRRALRR--------TIG*HRPVR*grresfsgrENLYMIGR*LDLS-RKDARARADELLERFSLTEAAGRAAA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 398 QLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVV 477
Cdd:NF000106 144 KYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVI 223
|
250
....*....|.
gi 2084914118 478 TDASPASIRSE 488
Cdd:NF000106 224 ADGKVDELKTK 234
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
236-477 |
2.91e-16 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 81.30 E-value: 2.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 236 QALRQPASASKKRNEPVPGQPDALL--LRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRG 313
Cdd:PRK10789 291 RAMLAEAPVVKDGSEPVPEGRGELDvnIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEG 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 314 EIvLFGNDFIKAGKRDDAPvirqgiRRIGMVFQNFNLFPHrTILDNVILapryhGLADSAELRrkghglLDRVGLLAHAH 393
Cdd:PRK10789 371 DI-RFHDIPLTKLQLDSWR------SRLAVVSQTPFLFSD-TVANNIAL-----GRPDATQQE------IEHVARLASVH 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 394 K--------YPHQ-------LSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLaREGMTMLIVTHEM 458
Cdd:PRK10789 432 DdilrlpqgYDTEvgergvmLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQW-GEGRTVIISAHRL 510
|
250
....*....|....*....
gi 2084914118 459 DfALSISDRIVFMENGHVV 477
Cdd:PRK10789 511 S-ALTEASEILVMQHGHIA 528
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
284-474 |
3.88e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 79.38 E-value: 3.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 284 GEVISIIGPSGSGKTSLIRTINSLesidrgeivLFGNDFIKAGKRDDAPVI---------RQGIRRIGMVFQN--FNLFP 352
Cdd:PRK09473 42 GETLGIVGESGSGKSQTAFALMGL---------LAANGRIGGSATFNGREIlnlpekelnKLRAEQISMIFQDpmTSLNP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 353 HRTILDNVILAPRYHGLADSAELRRKGHGLLDRVGLlAHAHK----YPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSA 428
Cdd:PRK09473 113 YMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKM-PEARKrmkmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTA 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2084914118 429 LDPELVGEVLNVIRDLAREGMTMLI-VTHEMDFALSISDRIVFMENG 474
Cdd:PRK09473 192 LDVTVQAQIMTLLNELKREFNTAIImITHDLGVVAGICDKVLVMYAG 238
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
270-476 |
4.17e-16 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 80.54 E-value: 4.17e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 270 NHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGndfiKAGKRDDA-PVIRQGI------RRIG 342
Cdd:PRK10982 260 RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHG----KKINNHNAnEAINHGFalvteeRRST 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 343 MVFQN----FNlfphrTILDNVILAPRYHGLADSAELRRKGHGLLDRVGLLAHAHKYP-HQLSGGQQQRVAIARALAMEP 417
Cdd:PRK10982 336 GIYAYldigFN-----SLISNIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQiGSLSGGNQQKVIIGRWLLTQP 410
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2084914118 418 DIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHV 476
Cdd:PRK10982 411 EILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
263-470 |
6.13e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 80.62 E-value: 6.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 263 DIHKRYGNH--EVLKGidlVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEI-----VLFGNDFIKAGKrdDAPViR 335
Cdd:PRK13409 345 DLTKKLGDFslEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVdpelkISYKPQYIKPDY--DGTV-E 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 336 QGIRRIGmvfqnfnlfphrTILDNvilAPRYHGLADSAELRRkghgLLDRvgllahahkYPHQLSGGQQQRVAIARALAM 415
Cdd:PRK13409 419 DLLRSIT------------DDLGS---SYYKSEIIKPLQLER----LLDK---------NVKDLSGGELQRVAIAACLSR 470
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 416 EPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDR-IVF 470
Cdd:PRK13409 471 DADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDHDIYMIDYISDRlMVF 527
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
285-482 |
6.22e-16 |
|
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: 81.21 E-value: 6.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 285 EVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFikagkRDDAPVIRQGIrriGMVFQNFNLFPHRTILDNVILAP 364
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI-----ETNLDAVRQSL---GMCPQHNILFHHLTVAEHILFYA 1028
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 365 RYHGLA-DSAELRRKGhgLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRD 443
Cdd:TIGR01257 1029 QLKGRSwEEAQLEMEA--MLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLK 1106
|
170 180 190
....*....|....*....|....*....|....*....
gi 2084914118 444 LaREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASP 482
Cdd:TIGR01257 1107 Y-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
249-490 |
1.16e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 80.17 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 249 NEPVPGQPDA--LLLRDIHKRYGNH--EVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIK 324
Cdd:PLN03130 1226 NRPPPGWPSSgsIKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISK 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 325 AGKRD---------DAPVIRQGIRRigmvfqnFNLFPHRTildnvilapryHGLADSAELRRKGHgLLDRV-----GLLA 390
Cdd:PLN03130 1306 FGLMDlrkvlgiipQAPVLFSGTVR-------FNLDPFNE-----------HNDADLWESLERAH-LKDVIrrnslGLDA 1366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 391 HAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAReGMTMLIVTHEMDFALSiSDRIVF 470
Cdd:PLN03130 1367 EVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFK-SCTMLIIAHRLNTIID-CDRILV 1444
|
250 260
....*....|....*....|
gi 2084914118 471 MENGHVVTDASPASIRSEGD 490
Cdd:PLN03130 1445 LDAGRVVEFDTPENLLSNEG 1464
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
270-477 |
1.36e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 79.29 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 270 NHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFG---NDFIKAGKRDdapvirqgirRIGMVFQ 346
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlRDYTLASLRN----------QVALVSQ 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 347 NFNLFpHRTILDNVILAPRYHGLADSAElrrkghglldRVGLLAHA----HKYPH-----------QLSGGQQQRVAIAR 411
Cdd:PRK11176 425 NVHLF-NDTIANNIAYARTEQYSREQIE----------EAARMAYAmdfiNKMDNgldtvigengvLLSGGQRQRIAIAR 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2084914118 412 ALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLaREGMTMLIVTHEMDfALSISDRIVFMENGHVV 477
Cdd:PRK11176 494 ALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLS-TIEKADEILVVEDGEIV 557
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
266-477 |
1.56e-15 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 74.99 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 266 KRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSL----ESIDrGEIVLFGNDFIKAGKRDDAPVIrqgirri 341
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRtegnVSVE-GDIHYNGIPYKEFAEKYPGEII------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 342 gMVFQNFNLFPHRTILDNVILApryhgladsaeLRRKGHGLLdRVgllahahkyphqLSGGQQQRVAIARALAMEPDIML 421
Cdd:cd03233 87 -YVSEEDVHFPTLTVRETLDFA-----------LRCKGNEFV-RG------------ISGGERKRVSIAEALVSRASVLC 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 422 FDEPTSALDPELVGEVLNVIRDLARE-GMTMLI-VTHEMDFALSISDRIVFMENGHVV 477
Cdd:cd03233 142 WDNSTRGLDSSTALEILKCIRTMADVlKTTTFVsLYQASDEIYDLFDKVLVLYEGRQI 199
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
239-483 |
2.55e-15 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 78.30 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 239 RQPASASKKRNEPVPGQPDALLLRDIHKRYGNHE-----VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRG 313
Cdd:COG4615 308 AAEPAAADAAAPPAPADFQTLELRGVTYRYPGEDgdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESG 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 314 EIVLfgndfikagkrDDAPVIRQGI----RRIGMVFQNFNLFphrtildnvilaPRYHGLaDSAELRRKGHGLLDRVGLl 389
Cdd:COG4615 388 EILL-----------DGQPVTADNReayrQLFSAVFSDFHLF------------DRLLGL-DGEADPARARELLERLEL- 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 390 ahAHKYPHQ--------LSGGQQQRVAIARALAMEPDIMLFDEPTSALDP--------ELVGEvlnvirdLAREGMTMLI 453
Cdd:COG4615 443 --DHKVSVEdgrfsttdLSQGQRKRLALLVALLEDRPILVFDEWAADQDPefrrvfytELLPE-------LKARGKTVIA 513
|
250 260 270
....*....|....*....|....*....|
gi 2084914118 454 VTHEmDFALSISDRIVFMENGHVVTDASPA 483
Cdd:COG4615 514 ISHD-DRYFDLADRVLKMDYGKLVELTGPA 542
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
273-457 |
2.74e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 78.77 E-value: 2.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 273 VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTInslesidRGEIVlfGNDFIKAGKRDDAPVIRQGIRRIGMVFQNFNLFP 352
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRIQ--GNNFTGTILANNRKPTKQILKRTGFVTQDDILYP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 353 HRTILDNVILAP--RYHGLADSAELRRKGHGLLDRVGLLAH-----AHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEP 425
Cdd:PLN03211 154 HLTVRETLVFCSllRLPKSLTKQEKILVAESVISELGLTKCentiiGNSFIRGISGGERKRVSIAHEMLINPSLLILDEP 233
|
170 180 190
....*....|....*....|....*....|..
gi 2084914118 426 TSALDPELVGEVLNVIRDLAREGMTMLIVTHE 457
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQ 265
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
273-485 |
3.94e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 77.52 E-value: 3.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 273 VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTI--NSLESIDRGEIVLFGNDfIKAGKRDDApvIRQGI-------RRIGM 343
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgRSYGRNISGTVFKDGKE-VDVSTVSDA--IDAGLayvtedrKGYGL 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 344 VFQNfnlfphrTILDNVILA--PRY--HGLADSAE-----------LRRKGHGLLDRVGllahahkyphQLSGGQQQRVA 408
Cdd:NF040905 352 NLID-------DIKRNITLAnlGKVsrRGVIDENEeikvaeeyrkkMNIKTPSVFQKVG----------NLSGGNQQKVV 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 409 IARALAMEPDIMLFDEPTSALDpelVG---EVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVV-----TDA 480
Cdd:NF040905 415 LSKWLFTDPDVLILDEPTRGID---VGakyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITgelprEEA 491
|
....*
gi 2084914118 481 SPASI 485
Cdd:NF040905 492 SQERI 496
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
179-474 |
5.50e-15 |
|
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: 78.13 E-value: 5.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 179 LVGQRLYAqnflvletLAAVAIYYVLIVTLFgwllqwaERHLDLSRKNArtlDDTQAQALRQPASASKKRNEPVPG--QP 256
Cdd:TIGR01257 1874 LIGKNLVA--------MAVEGVVYFLLTLLI-------QHHFFLSRWIA---EPAKEPIFDEDDDVAEERQRIISGgnKT 1935
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 257 DALLLRDIHKRYG--NHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAgkrddapvi 334
Cdd:TIGR01257 1936 DILRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN--------- 2006
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 335 rqgirrIGMVFQNFNLFPHRTILDNVI-------LAPRYHGLAdSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRV 407
Cdd:TIGR01257 2007 ------ISDVHQNMGYCPQFDAIDDLLtgrehlyLYARLRGVP-AEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKL 2079
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 408 AIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENG 474
Cdd:TIGR01257 2080 STAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
260-486 |
5.99e-15 |
|
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: 74.71 E-value: 5.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 260 LLRDIHKRYG-NHEVLKGIDlVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRG---------EIVLF--GN---DFIK 324
Cdd:cd03236 2 LEDEPVHRYGpNSFKLHRLP-VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGkfddppdwdEILDEfrGSelqNYFT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 325 AGKRDDAPVIR--QGIRRI-----GMVFQNFNLFPHRTILDNVIlapryhglaDSAELRrkghGLLDRvgllahahkYPH 397
Cdd:cd03236 81 KLLEGDVKVIVkpQYVDLIpkavkGKVGELLKKKDERGKLDELV---------DQLELR----HVLDR---------NID 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 398 QLSGGQQQRVAIARALAMEPDIMLFDEPTSALDpelVGEVLN---VIRDLAREGMTMLIVTHEMDFALSISDRI--VFME 472
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLD---IKQRLNaarLIRELAEDDNYVLVVEHDLAVLDYLSDYIhcLYGE 215
|
250
....*....|....*.
gi 2084914118 473 NG--HVVTdaSPASIR 486
Cdd:cd03236 216 PGayGVVT--LPKSVR 229
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
269-460 |
8.43e-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: 76.90 E-value: 8.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 269 GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLfgndfikagkrddapviRQGIRrIGMVFQNF 348
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP-----------------QPGIK-VGYLPQEP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 349 NLFPHRTILDNVILA--------PRYHG---------------LADSAELRRK-----GHGLLDRVGLLAHAHKYP---- 396
Cdd:TIGR03719 78 QLDPTKTVRENVEEGvaeikdalDRFNEisakyaepdadfdklAAEQAELQEIidaadAWDLDSQLEIAMDALRCPpwda 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 397 --HQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVG--EvlnviRDLAREGMTMLIVTHEMDF 460
Cdd:TIGR03719 158 dvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAwlE-----RHLQEYPGTVVAVTHDRYF 220
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
269-474 |
9.36e-15 |
|
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: 72.66 E-value: 9.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 269 GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINslesiDRGEIVLFGNDFIKAGKRDDAPVIRqgirRIGMVFQNF 348
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLA-----GRKTAGVITGEILINGRPLDKNFQR----STGYVEQQD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 349 NLFPHRTildnVILAPRYhgladSAELRrkghglldrvgllahahkyphQLSGGQQQRVAIARALAMEPDIMLFDEPTSA 428
Cdd:cd03232 89 VHSPNLT----VREALRF-----SALLR---------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSG 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2084914118 429 LDPELVGEVLNVIRDLAREGMTMLIVTHEMdfalSIS-----DRIVFMENG 474
Cdd:cd03232 139 LDSQAAYNIVRFLKKLADSGQAILCTIHQP----SASifekfDRLLLLKRG 185
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
259-456 |
1.10e-14 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 73.67 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLE--SIDRGEIVLFGNDFIKAgkrddAPVIRQ 336
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLEL-----SPEDRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 337 GiRRIGMVFQNFNLFP---HRTILDNVILAPR-YHG------------LADSAELRRKGHGLLDR---VGllahahkyph 397
Cdd:PRK09580 77 G-EGIFMAFQYPVEIPgvsNQFFLQTALNAVRsYRGqepldrfdfqdlMEEKIALLKMPEDLLTRsvnVG---------- 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084914118 398 qLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPE---LVGEVLNVIRDLARegmTMLIVTH 456
Cdd:PRK09580 146 -FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDalkIVADGVNSLRDGKR---SFIIVTH 203
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
274-476 |
1.14e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 77.09 E-value: 1.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 274 LKGIDLVVKPGEVISIIGPSGSGKTSLIrtinsleSIDRGEIvlfgndfikAGKRDDAPVIRQGIRRIGMVFQNFNlfph 353
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLI-------SAMLGEL---------PPRSDASVVIRGTVAYVPQVSWIFN---- 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 354 RTILDNVIL-----APRYHGLADSAELRRKghglLDRV--GLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPT 426
Cdd:PLN03130 693 ATVRDNILFgspfdPERYERAIDVTALQHD----LDLLpgGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2084914118 427 SALDPELVGEVLN-VIRDLAReGMTMLIVTHEMDFaLSISDRIVFMENGHV 476
Cdd:PLN03130 769 SALDAHVGRQVFDkCIKDELR-GKTRVLVTNQLHF-LSQVDRIILVHEGMI 817
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
284-487 |
1.37e-14 |
|
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: 73.60 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 284 GEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGND------FIKAgkrDDAPVIRQGIRRIGMVFQNFNLFphrtil 357
Cdd:cd03237 25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTvsykpqYIKA---DYEGTVRDLLSSITKDFYTHPYF------ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 358 DNVILAPRyhgladsaelrrKGHGLLDRVGLlahahkyphQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEV 437
Cdd:cd03237 96 KTEIAKPL------------QIEQILDREVP---------ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 438 LNVIRDLA-REGMTMLIVTHEMDFALSISDR-IVFMENGHVVTDAS-PASIRS 487
Cdd:cd03237 155 SKVIRRFAeNNEKTAFVVEHDIIMIDYLADRlIVFEGEPSVNGVANpPQSLRS 207
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
399-476 |
2.03e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 2.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 399 LSGGQQQRVAIARALAMEPDIMLFDEPTSALDpelVG---EVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGH 475
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD---VGakkEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGR 472
|
.
gi 2084914118 476 V 476
Cdd:PRK10762 473 I 473
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
263-487 |
2.31e-14 |
|
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: 75.59 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 263 DIHKRYGNH--EVLKGidlVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEI-----VLFGNDFIKAGKrdDAPVir 335
Cdd:COG1245 346 DLTKSYGGFslEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVdedlkISYKPQYISPDY--DGTV-- 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 336 qgirrigmvfqnfnlfphRTILDNVIlAPRYhglaDSAELRrkgHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAM 415
Cdd:COG1245 419 ------------------EEFLRSAN-TDDF----GSSYYK---TEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSR 472
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 416 EPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRI-VFM----ENGHVvtdASPASIRS 487
Cdd:COG1245 473 DADLYLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLmVFEgepgVHGHA---SGPMDMRE 547
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
281-479 |
2.45e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 75.25 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 281 VKPGEVISIIGPSGSGKTSLIRTI-NSLESIDRGEIVLFGNdfiKAGKRDDAPVIRQGIRRIGMVFQNFNLFPHRTILDN 359
Cdd:TIGR02633 283 LRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGK---PVDIRNPAQAIRAGIAMVPEDRKRHGIVPILGVGKN 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 360 VILA--PRYHGLA---DSAELRRKGHGLlDRVGLLAHAHKYP-HQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPEL 433
Cdd:TIGR02633 360 ITLSvlKSFCFKMridAAAELQIIGSAI-QRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2084914118 434 VGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTD 479
Cdd:TIGR02633 439 KYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
281-474 |
4.35e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 74.58 E-value: 4.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 281 VKPGEVISIIGPSGSGKTSLIRTI-NSLESIDRGEIVLFGNdfiKAGKRDDAPVIRQGI-------RRIGMVfqnfnlfP 352
Cdd:PRK13549 285 LRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGK---PVKIRNPQQAIAQGIamvpedrKRDGIV-------P 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 353 HRTILDNVILA--PRYHG---LADSAELRRKGHGLlDRVGL-LAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPT 426
Cdd:PRK13549 355 VMGVGKNITLAalDRFTGgsrIDDAAELKTILESI-QRLKVkTASPELAIARLSGGNQQKAVLAKCLLLNPKILILDEPT 433
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2084914118 427 SALDpelVG---EVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENG 474
Cdd:PRK13549 434 RGID---VGakyEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEG 481
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
227-476 |
4.41e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.32 E-value: 4.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 227 ARTLDDTQAQALRQPASaskkRNEPVPGQPdALLLRDIhkrygNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINS 306
Cdd:PRK15439 242 EKSLSASQKLWLELPGN----RRQQAAGAP-VLTVEDL-----TGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYG 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 307 LESIDRGEIVLFGNDFikaGKRDDAPVIRQGIRRIGMVFQNFNLFPHRTILDNVIlAPRYHGL-------ADSAELRRKG 379
Cdd:PRK15439 312 LRPARGGRIMLNGKEI---NALSTAQRLARGLVYLPEDRQSSGLYLDAPLAWNVC-ALTHNRRgfwikpaRENAVLERYR 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 380 HGLLDRvglLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMD 459
Cdd:PRK15439 388 RALNIK---FNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLE 464
|
250
....*....|....*..
gi 2084914118 460 FALSISDRIVFMENGHV 476
Cdd:PRK15439 465 EIEQMADRVLVMHQGEI 481
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
250-486 |
8.41e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.01 E-value: 8.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 250 EPVPGQPDALLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfIKAGKRD 329
Cdd:NF033858 258 PADDDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQP-VDAGDIA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 330 dapvIRqgiRRIGMVFQNFNLFPHRTILDNVILAPRYHGLADsAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAI 409
Cdd:NF033858 337 ----TR---RRVGYMSQAFSLYGELTVRQNLELHARLFHLPA-AEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSL 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 410 ARALAMEPDIMLFDEPTSALDPelvgevlnVIRD--------LARE-GMTMLIVTHEMDFALSiSDRIVFMENGHVVTDA 480
Cdd:NF033858 409 AVAVIHKPELLILDEPTSGVDP--------VARDmfwrllieLSREdGVTIFISTHFMNEAER-CDRISLMHAGRVLASD 479
|
....*.
gi 2084914118 481 SPASIR 486
Cdd:NF033858 480 TPAALV 485
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
277-482 |
8.50e-14 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 72.53 E-value: 8.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 277 IDLVVKPGEVISIIGPSGSGKTSLIRTI------NSLESIDRgeiVLFGN-DFIKAGKRDDAPVIRqgiRRIGMVFQNFN 349
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdNWRVTADR---MRFDDiDLLRLSPRERRKLVG---HNVSMIFQEPQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 350 --LFPHRTILDNVILA-----------PRYHGLadsaelRRKGHGLLDRVGLLAHA---HKYPHQLSGGQQQRVAIARAL 413
Cdd:PRK15093 100 scLDPSERVGRQLMQNipgwtykgrwwQRFGWR------KRRAIELLHRVGIKDHKdamRSFPYELTEGECQKVMIAIAL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 414 AMEPDIMLFDEPTSALDPELVGEvlnVIRDLAR----EGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASP 482
Cdd:PRK15093 174 ANQPRLLIADEPTNAMEPTTQAQ---IFRLLTRlnqnNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPS 243
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
268-478 |
9.56e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 73.83 E-value: 9.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 268 YGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVlFGNDFIKAGKRDDAP---------VIRQGI 338
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRII-YEQDLIVARLQQDPPrnvegtvydFVAEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRIGMVFQNFnlfpHRtILDNVILAPRYHGLADSAELRRK--GHGL----------LDRVGLlaHAHKYPHQLSGGQQQR 406
Cdd:PRK11147 92 EEQAEYLKRY----HD-ISHLVETDPSEKNLNELAKLQEQldHHNLwqlenrinevLAQLGL--DPDAALSSLSGGWLRK 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084914118 407 VAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLarEGmTMLIVTHEMDFALSISDRIVFMENGHVVT 478
Cdd:PRK11147 165 AALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTF--QG-SIIFISHDRSFIRNMATRIVDLDRGKLVS 233
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
264-492 |
1.03e-13 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 72.04 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 264 IHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGND-FikagKRDDAPVirqgiRRIG 342
Cdd:COG4586 28 FRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpF----KRRKEFA-----RRIG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 343 MVF-QNFNLFPHRTILDNVILAPRYHGLADSAELRRKGH--GLLDRVGLLahaHKYPHQLSGGQQQRVAIARALAMEPDI 419
Cdd:COG4586 99 VVFgQRSQLWWDLPAIDSFRLLKAIYRIPDAEYKKRLDElvELLDLGELL---DTPVRQLSLGQRMRCELAAALLHRPKI 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084914118 420 MLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSEGDPR 492
Cdd:COG4586 176 LFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFGPY 249
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
274-488 |
1.55e-13 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 70.25 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 274 LKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESiDRGEIVLFGNDFikagkrDDAPVIRQGIRR----------IGM 343
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPL------SDWSAAELARHRaylsqqqsppFAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 344 -VFQnfnlfphrtildnvILAPRYHGLADSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARAL-----AMEP 417
Cdd:COG4138 85 pVFQ--------------YLALHQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 418 D--IMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSE 488
Cdd:COG4138 151 EgqLLLLDEPMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTP 223
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
259-477 |
4.61e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 68.90 E-value: 4.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTI--NSLESIDRGEIVLFGNDFIKAGKRDDApviRQ 336
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIagHPAYKILEGDILFKGESILDLEPEERA---HL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 337 GIRrigMVFQNFNLFPHRTILDNVILAprYHGladsaelRRKGHGL---------------LDRVGLLAH-AHKYPHQ-L 399
Cdd:CHL00131 85 GIF---LAFQYPIEIPGVSNADFLRLA--YNS-------KRKFQGLpeldplefleiinekLKLVGMDPSfLSRNVNEgF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 400 SGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHE---MDFAlsISDRIVFMENGHV 476
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYqrlLDYI--KPDYVHVMQNGKI 230
|
.
gi 2084914118 477 V 477
Cdd:CHL00131 231 I 231
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
274-476 |
4.75e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 71.93 E-value: 4.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 274 LKGIDLVVKPGEVISIIGPSGSGKTSLIRTInslesidRGEIvlfgndfikAGKRDDAPVIRQGIRRIGMVFQNFNlfph 353
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAM-------LGEL---------SHAETSSVVIRGSVAYVPQVSWIFN---- 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 354 RTILDNVIL-----APRYHGLADSAELRRK-----GHGLLDrVGllahahKYPHQLSGGQQQRVAIARALAMEPDIMLFD 423
Cdd:PLN03232 693 ATVRENILFgsdfeSERYWRAIDVTALQHDldllpGRDLTE-IG------ERGVNISGGQKQRVSMARAVYSNSDIYIFD 765
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 424 EPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFaLSISDRIVFMENGHV 476
Cdd:PLN03232 766 DPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHF-LPLMDRIILVSEGMI 817
|
|
| BPD_transp_1 |
pfam00528 |
Binding-protein-dependent transport system inner membrane component; The alignments cover the ... |
35-220 |
5.79e-13 |
|
Binding-protein-dependent transport system inner membrane component; The alignments cover the most conserved region of the proteins, which is thought to be located in a cytoplasmic loop between two transmembrane domains. The members of this family have a variable number of transmembrane helices.
Pssm-ID: 334128 [Multi-domain] Cd Length: 183 Bit Score: 67.32 E-value: 5.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 35 GLVLGFLLAsakLSGHAWLRMPASFYIWLFRSIPLLVLLVFVYNLPQLfpvtgSVLSQPFYSGLIALVLTETAYMAEIHR 114
Cdd:pfam00528 1 GIPLGIIAA---LRRGRRLDRLLRPLIDLLQALPSFVLAILLVVIAIL-----SILGHGILPAIILALLGWAGYARLIRR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 115 GGLLSVLKGQREAAKALGIRGVGAQRLVIIPQAIRISLPTLTNEYVTIVKLTSLVSVI----SLNELLLVGQrLYAQNFL 190
Cdd:pfam00528 73 AALRSLPSDLVEAARALGASRWQIFRKIILPNALPPILTGLALAFGGALGGAVLLEFLgswpGLGLLLIEAI-LGYDYPE 151
|
170 180 190
....*....|....*....|....*....|
gi 2084914118 191 VLETLAAVAIYYVLIVTLFGWLLQWAERHL 220
Cdd:pfam00528 152 IQGPVLAAALILLLLNLLVDILQRLLDPRV 181
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
274-476 |
1.81e-11 |
|
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: 66.89 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 274 LKGIDLVVKPGEVISIIGPSGSGKTSLIRTInsLESIDRGEivlfGNDFIKAGKrddAPVIRQGIRRIGMVFQNFnLFPH 353
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSAL--LAEMDKVE----GHVHMKGSV---AYVPQQAWIQNDSLRENI-LFGK 723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 354 -------RTILDNVILAPRYHGL--ADSAELRRKGHglldrvgllahahkyphQLSGGQQQRVAIARALAMEPDIMLFDE 424
Cdd:TIGR00957 724 alnekyyQQVLEACALLPDLEILpsGDRTEIGEKGV-----------------NLSGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 425 PTSALDPELVGEVL-NVIrdlAREGM----TMLIVTHEMDFaLSISDRIVFMENGHV 476
Cdd:TIGR00957 787 PLSAVDAHVGKHIFeHVI---GPEGVlknkTRILVTHGISY-LPQVDVIIVMSGGKI 839
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
273-472 |
2.51e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 63.33 E-value: 2.51e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 273 VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDfIKAGKRDdapvirqgiRRIGMVFQNFNLFP 352
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKT-ATRGDRS---------RFMAYLGHLPGLKA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 353 HRTILDNVILAPRYHGladsAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPE 432
Cdd:PRK13543 96 DLSTLENLHFLCGLHG----RRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2084914118 433 LVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFME 472
Cdd:PRK13543 172 GITLVNRMISAHLRGGGAALVTTHGAYAAPPVRTRMLTLE 211
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
263-499 |
3.63e-11 |
|
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: 61.82 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 263 DIHKRYGNHEVLKGIDlVVKPGEVISIIGPSGSGKTSLIRTINSLEsidrgeivlfgndfIKAGKRDDAPVIRqgirrig 342
Cdd:cd03222 5 DCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQL--------------IPNGDNDEWDGIT------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 343 mvfqnfnlfphrtildnVILAPRYHgladsaelrrkghglldrvgllahahkyphQLSGGQQQRVAIARALAMEPDIMLF 422
Cdd:cd03222 63 -----------------PVYKPQYI------------------------------DLSGGELQRVAIAAALLRNATFYLF 95
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2084914118 423 DEPTSALDPELVGEVLNVIRDLAREGM-TMLIVTHEMDFALSISDRI-VFMENGHVVTDASPASIRSEGDPRVRRFIGL 499
Cdd:cd03222 96 DEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIhVFEGEPGVYGIASQPKGTREGINRFLRGYLI 174
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
259-474 |
3.72e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 65.38 E-value: 3.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRYGNHEV-LKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLfgndfikagkrDDAPVIRQG 337
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILL-----------DGKPVTAEQ 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 338 I----RRIGMVFQNFNLFPHrtildnvILAPRyhGLADSAELRRKghgLLDRVGLlahAHKYPH--------QLSGGQQQ 405
Cdd:PRK10522 392 PedyrKLFSAVFTDFHLFDQ-------LLGPE--GKPANPALVEK---WLERLKM---AHKLELedgrisnlKLSKGQKK 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 406 RVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHEmDFALSISDRIVFMENG 474
Cdd:PRK10522 457 RLALLLALAEERDILLLDEWAADQDPHFRREFYQVLLPLLQEmGKTIFAISHD-DHYFIHADRLLEMRNG 525
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
266-456 |
3.87e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 65.14 E-value: 3.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 266 KRYG-NHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLfgndfikagkrddAPvirqGIRrIGMV 344
Cdd:PRK11819 14 KVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARP-------------AP----GIK-VGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 345 FQNFNLFPHRTILDNVILA--------PRYHGLADS-AELRRKGHGLLDRVGLL------AHAHKYPHQ----------- 398
Cdd:PRK11819 76 PQEPQLDPEKTVRENVEEGvaevkaalDRFNEIYAAyAEPDADFDALAAEQGELqeiidaADAWDLDSQleiamdalrcp 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 399 --------LSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVG--EvlnviRDLAREGMTMLIVTH 456
Cdd:PRK11819 156 pwdakvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAwlE-----QFLHDYPGTVVAVTH 218
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
399-471 |
4.03e-11 |
|
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: 61.57 E-value: 4.03e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084914118 399 LSGGQQQRVAIARALAMEPD--IMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFaLSISDRIVFM 471
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLDV-LSSADWIIDF 161
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
258-469 |
5.11e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 64.91 E-value: 5.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 258 ALLLRDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDAPvirqg 337
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDHAY----- 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 338 irrigmVFQN-FNLFP----HRTILDNvILAPRyhgladsaelrrkghGLLDRvgLL---AHAHKYPHQLSGGQQQRVAI 409
Cdd:PRK15064 394 ------DFENdLTLFDwmsqWRQEGDD-EQAVR---------------GTLGR--LLfsqDDIKKSVKVLSGGEKGRMLF 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 410 ARALAMEPDIMLFDEPTSALDPELVgEVLNVIRDLArEGmTMLIVTHEMDFALSISDRIV 469
Cdd:PRK15064 450 GKLMMQKPNVLVMDEPTNHMDMESI-ESLNMALEKY-EG-TLIFVSHDREFVSSLATRII 506
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
273-474 |
5.49e-11 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 65.52 E-value: 5.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 273 VLKGIDLVVKPGEVISIIGPSGSGKTSLIrtiNSLESIDRGEIVLFGNDFIKAGKRDDAPVirqgiRRIGMVFQNFNLFP 352
Cdd:TIGR00956 778 ILNNVDGWVKPGTLTALMGASGAGKTTLL---NVLAERVTTGVITGGDRLVNGRPLDSSFQ-----RSIGYVQQQDLHLP 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 353 HRTILDNVILapryhgladSAELRRKGH-------GLLDRVGLLAHAHKYPHQLSG--------GQQQRVAIARALAMEP 417
Cdd:TIGR00956 850 TSTVRESLRF---------SAYLRQPKSvsksekmEYVEEVIKLLEMESYADAVVGvpgeglnvEQRKRLTIGVELVAKP 920
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2084914118 418 DIMLF-DEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSIS-DRIVFMENG 474
Cdd:TIGR00956 921 KLLLFlDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHQPSAILFEEfDRLLLLQKG 979
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
395-489 |
9.94e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.67 E-value: 9.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 395 YPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDP---ELVGEVLNVIRDLAREgmTMLIVTHEMDfALSISDRIVFM 471
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSnseKLIEKTIVDIKDKADK--TIITIAHRIA-SIKRSDKIVVF 1431
|
90
....*....|....*...
gi 2084914118 472 ENghvvTDASPASIRSEG 489
Cdd:PTZ00265 1432 NN----PDRTGSFVQAHG 1445
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
274-474 |
1.47e-10 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 61.19 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 274 LKGIDLVVKPGEVISIIGPSGSGKTSLIRTInslesidRGEIVLFGNDFIKAGKRDDAPVIRQGIRR----IGMVFQNFN 349
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAI-------LGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQKPW 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 350 LFpHRTILDNVILAP-----RYHGLADSAELRRKghglldrVGLLAHAHKYPH-----QLSGGQQQRVAIARALAMEPDI 419
Cdd:cd03290 90 LL-NATVEENITFGSpfnkqRYKAVTDACSLQPD-------IDLLPFGDQTEIgergiNLSGGQRQRICVARALYQNTNI 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 420 MLFDEPTSALDPELVGEVLN--VIRDLAREGMTMLIVTHEMDFaLSISDRIVFMENG 474
Cdd:cd03290 162 VFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQY-LPHADWIIAMKDG 217
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
281-488 |
1.97e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.10 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 281 VKPGEVISIIGPSGSGKTSLIRTINSLESIDrGEIVLFGNDFikagkrDDAPVIRQGIRRIGMVFQNFNLFphrtildnv 360
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPL------EAWSAAELARHRAYLSQQQTPPF--------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 361 iLAPRYHGLA-------DSAELRRKGHGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARA-LAMEPDI------MLFDEPT 426
Cdd:PRK03695 83 -AMPVFQYLTlhqpdktRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDInpagqlLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084914118 427 SALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMENGHVVTDASPASIRSE 488
Cdd:PRK03695 162 NSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTP 223
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
273-474 |
3.66e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 61.03 E-value: 3.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 273 VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTInslesidRGEIVlfgndfIKAGKrddapvIRQGiRRIGMVFQNFNLFP 352
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLI-------LGELE------PSEGK------IKHS-GRISFSSQFSWIMP 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 353 HrTILDNVILAPRYHgladsaELRRKGhgLLDRVGLLAHAHKYPHQ-----------LSGGQQQRVAIARALAMEPDIML 421
Cdd:cd03291 112 G-TIKENIIFGVSYD------EYRYKS--VVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2084914118 422 FDEPTSALDPELVGEVLN--VIRDLAREgmTMLIVTHEMDfALSISDRIVFMENG 474
Cdd:cd03291 183 LDSPFGYLDVFTEKEIFEscVCKLMANK--TRILVTSKME-HLKKADKILILHEG 234
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
244-482 |
4.60e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 62.49 E-value: 4.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 244 ASKKRNEPVPGQPDALLLRDIHKRY--GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGND 321
Cdd:PTZ00243 1294 ASPTSAAPHPVQAGSLVFEGVQMRYreGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGRE 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 322 FIKAGKRDdapvIRqgiRRIGMVFQNFNLFpHRTILDNVilAPRYHglADSAELRRKGH--GLLDRV-----GLLAHAHK 394
Cdd:PTZ00243 1374 IGAYGLRE----LR---RQFSMIPQDPVLF-DGTVRQNV--DPFLE--ASSAEVWAALElvGLRERVaseseGIDSRVLE 1441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 395 YPHQLSGGQQQRVAIARALAME-PDIMLFDEPTSALDPELVGEVLNVIRDlAREGMTMLIVTHEMDfALSISDRIVFMEN 473
Cdd:PTZ00243 1442 GGSNYSVGQRQLMCMARALLKKgSGFILMDEATANIDPALDRQIQATVMS-AFSAYTVITIAHRLH-TVAQYDKIIVMDH 1519
|
....*....
gi 2084914118 474 GHVVTDASP 482
Cdd:PTZ00243 1520 GAVAEMGSP 1528
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
268-466 |
1.80e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 57.65 E-value: 1.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 268 YGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFikagKRDDAPVIRQgirrIGMVFQN 347
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQKQ----LCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 348 FNLFPHRTILDNVILapRYHGLADSAELRRkghglLDRVGLLAHAHKYP-HQLSGGQQQRVAIARALAMEPDIMLFDEPT 426
Cdd:PRK13540 83 SGINPYLTLRENCLY--DIHFSPGAVGITE-----LCRLFSLEHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2084914118 427 SALDPELVGEVLNVIRDLAREGMTMLIVTHEmDFALSISD 466
Cdd:PRK13540 156 VALDELSLLTIITKIQEHRAKGGAVLLTSHQ-DLPLNKAD 194
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
273-485 |
2.69e-09 |
|
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: 59.96 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 273 VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRD---------DAPVIRQGIRRigM 343
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDlrfkitiipQDPVLFSGSLR--M 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 344 VFQNFNLFPHRTILDNVILApRYHGLADSAElrrkghglldrVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFD 423
Cdd:TIGR00957 1379 NLDPFSQYSDEEVWWALELA-HLKTFVSALP-----------DKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLD 1446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084914118 424 EPTSALDPELVGEVLNVIRDlAREGMTMLIVTHEMDfalSISD--RIVFMENGHVVTDASPASI 485
Cdd:TIGR00957 1447 EATAAVDLETDNLIQSTIRT-QFEDCTVLTIAHRLN---TIMDytRVIVLDKGEVAEFGAPSNL 1506
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
272-483 |
2.96e-09 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.79 E-value: 2.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 272 EVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVlfgndfikaGKRDDAPVIRQGirrigmvfqnfnLF 351
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW---------AERSIAYVPQQA------------WI 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 352 PHRTILDNVIL--APRYHGLADS-------AELRRKGHGLLDRVGllahahKYPHQLSGGQQQRVAIARALAMEPDIMLF 422
Cdd:PTZ00243 733 MNATVRGNILFfdEEDAARLADAvrvsqleADLAQLGGGLETEIG------EKGVNLSGGQKARVSLARAVYANRDVYLL 806
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084914118 423 DEPTSALDPElVGEvlNVIRDL---AREGMTMLIVTHEMDFaLSISDRIVFMENGHVVTDASPA 483
Cdd:PTZ00243 807 DDPLSALDAH-VGE--RVVEECflgALAGKTRVLATHQVHV-VPRADYVVALGDGRVEFSGSSA 866
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
262-477 |
3.50e-09 |
|
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: 59.18 E-value: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 262 RDIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLF----------------------- 318
Cdd:TIGR03719 326 ENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGetvklayvdqsrdaldpnktvwe 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 319 ----GNDFIKAGKRDDAPviRQGIRRigmvfqnFNLfphrtildnvilapryhgladsaelrrKGHGLLDRVGllahahk 394
Cdd:TIGR03719 406 eisgGLDIIKLGKREIPS--RAYVGR-------FNF---------------------------KGSDQQKKVG------- 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 395 yphQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAreGMTMLIvTHEMDFALSISDRIVFME-N 473
Cdd:TIGR03719 443 ---QLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFA--GCAVVI-SHDRWFLDRIATHILAFEgD 516
|
....
gi 2084914118 474 GHVV 477
Cdd:TIGR03719 517 SHVE 520
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
273-475 |
3.98e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 59.54 E-value: 3.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 273 VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTInslesidRGEIVlfgndfikagkRDDAPVIRQGirRIGMVFQNFNLFP 352
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMI-------MGELE-----------PSEGKIKHSG--RISFSPQTSWIMP 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 353 HrTILDNVILAP-----RYHGLADSAELRrkghgllDRVGLLAHAHKYPH-----QLSGGQQQRVAIARALAMEPDIMLF 422
Cdd:TIGR01271 501 G-TIKDNIIFGLsydeyRYTSVIKACQLE-------EDIALFPEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLL 572
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2084914118 423 DEPTSALDPELVGEVLN--VIRDLAREgmTMLIVTHEMDFaLSISDRIVFMENGH 475
Cdd:TIGR01271 573 DSPFTHLDVVTEKEIFEscLCKLMSNK--TRILVTSKLEH-LKKADKILLLHEGV 624
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
259-488 |
4.52e-09 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 57.56 E-value: 4.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 259 LLLRDIHKRY--GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDrGEIVLFGNDFikagkrdDAPVIRQ 336
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSW-------NSVPLQK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 337 GIRRIGMVFQNFNLF--PHRTILDNvilapryHGLADSAELRRkghgLLDRVGLLAHAHKYPHQL-----------SGGQ 403
Cdd:cd03289 75 WRKAFGVIPQKVFIFsgTFRKNLDP-------YGKWSDEEIWK----VAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGH 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 404 QQRVAIARALAMEPDIMLFDEPTSALDPeLVGEVLNVIRDLAREGMTMLIVTHEMDfALSISDRIVFMENGHVVTDASPA 483
Cdd:cd03289 144 KQLMCLARSVLSKAKILLLDEPSAHLDP-ITYQVIRKTLKQAFADCTVILSEHRIE-AMLECQRFLVIEENKVRQYDSIQ 221
|
....*
gi 2084914118 484 SIRSE 488
Cdd:cd03289 222 KLLNE 226
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
242-490 |
1.49e-08 |
|
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: 55.69 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 242 ASASKKRNEPVPGQPDALLLRDIHKRYGNH--EVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFG 319
Cdd:cd03288 3 ASISGSSNSGLVGLGGEIKIHDLCVRYENNlkPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 320 NDFIKagkrddAPVirQGIR-RIGMVFQN---------FNLFPHRTILDNVIlaprYHGLaDSAELRRKGHGLLDrvGLL 389
Cdd:cd03288 83 IDISK------LPL--HTLRsRLSIILQDpilfsgsirFNLDPECKCTDDRL----WEAL-EIAQLKNMVKSLPG--GLD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 390 AHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPElVGEVLNVIRDLAREGMTMLIVTHEMDFALSiSDRIV 469
Cdd:cd03288 148 AVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMA-TENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVL 225
|
250 260
....*....|....*....|.
gi 2084914118 470 FMENGHVVTDASPASIRSEGD 490
Cdd:cd03288 226 VLSRGILVECDTPENLLAQED 246
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
283-471 |
4.07e-08 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 52.75 E-value: 4.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 283 PGEVISIIGPSGSGKTSLIRTInslesidrgeIVLFGNDFIKAGKRDDApvirqgirrigmvfqnfnlfphrtildnvil 362
Cdd:cd03227 20 EGSLTIITGPNGSGKSTILDAI----------GLALGGAQSATRRRSGV------------------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 363 APRYHGLADSAELrrkghglldrVGLLahahkypHQLSGGQQQRVAIARALA----MEPDIMLFDEPTSALDPELVGEVL 438
Cdd:cd03227 59 KAGCIVAAVSAEL----------IFTR-------LQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALA 121
|
170 180 190
....*....|....*....|....*....|...
gi 2084914118 439 NVIRDLAREGMTMLIVTHEMDFALsISDRIVFM 471
Cdd:cd03227 122 EAILEHLVKGAQVIVITHLPELAE-LADKLIHI 153
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
393-478 |
5.15e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.64 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 393 HKYPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDpelVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFME 472
Cdd:PLN03073 339 VKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLH 415
|
....*.
gi 2084914118 473 NGHVVT 478
Cdd:PLN03073 416 GQKLVT 421
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
273-477 |
1.03e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 54.34 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 273 VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRddapVIRQGIrriGMVFQN----- 347
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS----VLRQGV---AMVQQDpvvla 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 348 ----FNLFPHRTI--------LDNVILAPRYHGLADsaelrrkghGLLDRVGllahahKYPHQLSGGQQQRVAIARALAM 415
Cdd:PRK10790 429 dtflANVTLGRDIseeqvwqaLETVQLAELARSLPD---------GLYTPLG------EQGNNLSVGQKQLLALARVLVQ 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2084914118 416 EPDIMLFDEPTSALDPELVGEVLNVIRdLAREGMTMLIVTHEMDFALSiSDRIVFMENGHVV 477
Cdd:PRK10790 494 TPQILILDEATANIDSGTEQAIQQALA-AVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAV 553
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
399-504 |
1.27e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 54.45 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 399 LSGGQQQRVAIARALAME-PDIM-LFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEmDFALSISDRIVFME---- 472
Cdd:PRK00635 477 LSGGEQERTALAKHLGAElIGITyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADRIIDIGpgag 555
|
90 100 110
....*....|....*....|....*....|....
gi 2084914118 473 --NGHVVTDASPASIRSEGDPRVRRFigLEQEVT 504
Cdd:PRK00635 556 ifGGEVLFNGSPREFLAKSDSLTAKY--LRQELT 587
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
283-475 |
1.78e-07 |
|
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: 50.45 E-value: 1.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 283 PGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDAPVIRQGIRrigmvfqnfnlfphrtildnvil 362
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGK----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 363 apryhgladsaelrrkghglldrvgllahahkyPHQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVL---- 438
Cdd:smart00382 58 ---------------------------------KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLllee 104
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2084914118 439 --NVIRDLAREGMTMLIVTHEMDFALS-----ISDRIVFMENGH 475
Cdd:smart00382 105 lrLLLLLKSEKNLTVILTTNDEKDLGPallrrRFDRRIVLLLIL 148
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
274-482 |
1.84e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 52.23 E-value: 1.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 274 LKGIDLVVKPGEVISIIGPSGSGKTSLIRTI--NSLESIDRGEIVLFGN-DFIK-AGKRDDAPVIRQG-IRR-------- 340
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTlyPALARRLHLKKEQPGNhDRIEgLEHIDKVIVIDQSpIGRtprsnpat 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 341 -------IGMVF------QNFN------LFPHRTILDnVILAPRYHGL---ADSAELRRKGHGLLDrVGLlahahKYPH- 397
Cdd:cd03271 91 ytgvfdeIRELFcevckgKRYNretlevRYKGKSIAD-VLDMTVEEALeffENIPKIARKLQTLCD-VGL-----GYIKl 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 398 -----QLSGGQQQRVAIARALAME---PDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDfALSISDRIV 469
Cdd:cd03271 164 gqpatTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLD-VIKCADWII 242
|
250
....*....|....*....
gi 2084914118 470 FM------ENGHVVTDASP 482
Cdd:cd03271 243 DLgpeggdGGGQVVASGTP 261
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
273-477 |
2.30e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.57 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 273 VLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINS----LESIDRGEIVLFG--NDFIKAGKRDDapVIRQGirrigmvfQ 346
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASntdgFHIGVEGVITYDGitPEEIKKHYRGD--VVYNA--------E 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 347 NFNLFPHRTILDNVILAP-------RYHGLADSAELRRKGHGLLDRVGLlahAHKYPHQ--------LSGGQQQRVAIAR 411
Cdd:TIGR00956 146 TDVHFPHLTVGETLDFAArcktpqnRPDGVSREEYAKHIADVYMATYGL---SHTRNTKvgndfvrgVSGGERKRVSIAE 222
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2084914118 412 ALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLARE-GMTMLIVTHE-MDFALSISDRIVFMENGHVV 477
Cdd:TIGR00956 223 ASLGGAKIQCWDNATRGLDSATALEFIRALKTSANIlDTTPLVAIYQcSQDAYELFDKVIVLYEGYQI 290
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
274-469 |
2.35e-07 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 51.49 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 274 LKGIDLVVKPGEVISIIGPSGSGKTSLI----------RTINSLESidrgeivlFGNDFIKAGKRDD-------APVIRQ 336
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrRYVESLSA--------YARQFLGQMDKPDvdsieglSPAIAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 337 GIRRIGmvfQNfnlfPHRT------ILDnvilaprYHGLADSAELRRKGHGLLDRVGL--LAHAHKYPhQLSGGQQQRVA 408
Cdd:cd03270 83 DQKTTS---RN----PRSTvgtvteIYD-------YLRLLFARVGIRERLGFLVDVGLgyLTLSRSAP-TLSGGEAQRIR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2084914118 409 IARALAMEPD--IMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDfALSISDRIV 469
Cdd:cd03270 148 LATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDED-TIRAADHVI 209
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
263-432 |
3.81e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 52.43 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 263 DIHKRYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLF------------------------ 318
Cdd:PRK11819 329 NLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGetvklayvdqsrdaldpnktvwee 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 319 ---GNDFIKAGKRD---DAPVIRqgirrigmvfqnFNLfphrtildnvilapryhgladsaelrrKGHGLLDRVGllaha 392
Cdd:PRK11819 409 isgGLDIIKVGNREipsRAYVGR------------FNF---------------------------KGGDQQKKVG----- 444
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2084914118 393 hkyphQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPE 432
Cdd:PRK11819 445 -----VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDVE 479
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
398-458 |
5.79e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.34 E-value: 5.79e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084914118 398 QLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPE---LVGEVLNVIRdlAREGMTMLIVTHEM 458
Cdd:PTZ00265 579 KLSGGQKQRISIARAIIRNPKILILDEATSSLDNKseyLVQKTINNLK--GNENRITIIIAHRL 640
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
251-431 |
7.05e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 52.22 E-value: 7.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 251 PVPGQpdaLLLRDIHKRY--GNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDrGEIVLFG---NDFIKA 325
Cdd:TIGR01271 1213 PSGGQ---MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGvswNSVTLQ 1288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 326 GKRDDAPVIRQGIRRIGMVFQNfNLFPHRTILDNvilapryhgladsaELRRkghgLLDRVGLLAHAHKYPHQL------ 399
Cdd:TIGR01271 1289 TWRKAFGVIPQKVFIFSGTFRK-NLDPYEQWSDE--------------EIWK----VAEEVGLKSVIEQFPDKLdfvlvd 1349
|
170 180 190
....*....|....*....|....*....|....*..
gi 2084914118 400 -----SGGQQQRVAIARALAMEPDIMLFDEPTSALDP 431
Cdd:TIGR01271 1350 ggyvlSNGHKQLMCLARSILSKAKILLLDEPSAHLDP 1386
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
289-460 |
8.55e-07 |
|
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: 49.53 E-value: 8.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 289 IIGPSGSGKTSLIrtinslESIdrgEIVLFGNDFI-KAGKRDDAPVIRQGIRR--IGMVFQNFN---LFPHRT--ILDNV 360
Cdd:cd03240 27 IVGQNGAGKTTII------EAL---KYALTGELPPnSKGGAHDPKLIREGEVRaqVKLAFENANgkkYTITRSlaILENV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 361 ILAPRyhglADSAELrrkghgLLDRVGllahahkyphQLSGGQQQ------RVAIARALAMEPDIMLFDEPTSALDPELV 434
Cdd:cd03240 98 IFCHQ----GESNWP------LLDMRG----------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENI 157
|
170 180
....*....|....*....|....*...
gi 2084914118 435 GEVL-NVIRDLAREG-MTMLIVTHEMDF 460
Cdd:cd03240 158 EESLaEIIEERKSQKnFQLIVITHDEEL 185
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
399-459 |
2.10e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 50.40 E-value: 2.10e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084914118 399 LSGGQQQRVAIARAL---AMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMD 459
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLD 893
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
286-456 |
2.65e-06 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 48.08 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 286 VISIIGPSGSGKTSLIRTInslesidrgEIVLFGNDFIKAGKRDDapVIRQGIR--RIGMVFQN-------------FNL 350
Cdd:COG0419 25 LNLIVGPNGAGKSTILEAI---------RYALYGKARSRSKLRSD--LINVGSEeaSVELEFEHggkryrierrqgeFAE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 351 FPH------RTILDNVILAPRYHGLADSA-ELRRKGHGLLDRVGLLAHAHKY----------PHQLSGGQQQRVAIARAL 413
Cdd:COG0419 94 FLEakpserKEALKRLLGLEIYEELKERLkELEEALESALEELAELQKLKQEilaqlsgldpIETLSGGERLRLALADLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2084914118 414 AMEPDimlfdepTSALDPELVGEVLNVIRDLAregmtmlIVTH 456
Cdd:COG0419 174 SLILD-------FGSLDEERLERLLDALEELA-------IITH 202
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
281-456 |
2.73e-06 |
|
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: 50.13 E-value: 2.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 281 VKPGEVISIIGPSGSGKTSLIRTInslesidrGEI-VLFGNDFIKAGKRddapvirqgirRIGMVFQNfNLFPHRTILDN 359
Cdd:TIGR00954 475 VPSGNNLLICGPNGCGKSSLFRIL--------GELwPVYGGRLTKPAKG-----------KLFYVPQR-PYMTLGTLRDQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 360 VILAPRyhgladSAELRRKG---------------HGLLDRVGLLAHAHKYPHQLSGGQQQRVAIARALAMEPDIMLFDE 424
Cdd:TIGR00954 535 IIYPDS------SEDMKRRGlsdkdleqildnvqlTHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180 190
....*....|....*....|....*....|..
gi 2084914118 425 PTSALDPELVGEVLNVIRDLareGMTMLIVTH 456
Cdd:TIGR00954 609 CTSAVSVDVEGYMYRLCREF---GITLFSVSH 637
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
270-456 |
6.49e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 46.79 E-value: 6.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 270 NHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKrddaPVIrqgirriGMVFQNFN 349
Cdd:PRK13541 12 EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAK----PYC-------TYIGHNLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 350 LFPHRTILDNVILAPRYHglaDSAELRR------KGHGLLDrvgllahahKYPHQLSGGQQQRVAIARALAMEPDIMLFD 423
Cdd:PRK13541 81 LKLEMTVFENLKFWSEIY---NSAETLYaaihyfKLHDLLD---------EKCYSLSSGMQKIVAIARLIACQSDLWLLD 148
|
170 180 190
....*....|....*....|....*....|...
gi 2084914118 424 EPTSALDPELVGEVLNVIRDLAREGMTMLIVTH 456
Cdd:PRK13541 149 EVETNLSKENRDLLNNLIVMKANSGGIVLLSSH 181
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
267-454 |
2.12e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 2.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 267 RYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINslesidrGEIVLFGNDFIKAGKRDDAPVIRQGIRRIGMVFQ 346
Cdd:PRK10938 12 RLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALA-------GELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 347 NFN---LFPH-----RT----ILDNVILAPRYHGLAdsaELRRKGHgLLDRvgllahAHKYphqLSGGQQQRVAIARALA 414
Cdd:PRK10938 85 RNNtdmLSPGeddtgRTtaeiIQDEVKDPARCEQLA---QQFGITA-LLDR------RFKY---LSTGETRKTLLCQALM 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2084914118 415 MEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIV 454
Cdd:PRK10938 152 SEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLV 191
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
275-456 |
2.44e-05 |
|
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: 46.23 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 275 KGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNDFIKAGKRDDAPVIRQGIRRIGMVFQNFNLFPHR 354
Cdd:pfam13304 116 EELRLGLDVEERIELSLSELSDLISGLLLLSIISPLSFLLLLDEGLLLEDWAVLDLAADLALFPDLKELLQRLVRGLKLA 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 355 TI-LDNVILAPRYHGLADSAELRRKGHGLLDRVGLLAhahkYPHQLSGGQQQ---RVAIARALAMEPDIMLFDEPTSALD 430
Cdd:pfam13304 196 DLnLSDLGEGIEKSLLVDDRLRERGLILLENGGGGEL----PAFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLH 271
|
170 180
....*....|....*....|....*.
gi 2084914118 431 PELVGEVLNVIRDLAREGMTMLIVTH 456
Cdd:pfam13304 272 PKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
406-460 |
2.56e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 46.81 E-value: 2.56e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084914118 406 RVAIARALAMEPDIMLFDEPTSALDpelvgevLNVIRDLarEGM------TMLIVTHEMDF 460
Cdd:PRK15064 163 RVLLAQALFSNPDILLLDEPTNNLD-------INTIRWL--EDVlnernsTMIIISHDRHF 214
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
267-473 |
6.33e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.55 E-value: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 267 RYGNHEVLKGIDLVVKPGEVISIIGPSGSGKTSLIRTINSLESIDRGEIVLFGNdFIKAGKRDDAPVIRQ--------GI 338
Cdd:PRK10636 10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN-WQLAWVNQETPALPQpaleyvidGD 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 339 RRIGMVFQNFNLFPHRTilDNVILApRYHGLADSAE---LRRKGHGLLDRVGLLAHAHKYP-HQLSGGQQQRVAIARALA 414
Cdd:PRK10636 89 REYRQLEAQLHDANERN--DGHAIA-TIHGKLDAIDawtIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALI 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2084914118 415 MEPDIMLFDEPTSALDpelVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIVFMEN 473
Cdd:PRK10636 166 CRSDLLLLDEPTNHLD---LDAVIWLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQ 221
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
274-500 |
6.83e-05 |
|
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: 44.99 E-value: 6.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 274 LKGIDLVVKPGEVIsIIGPSGSGKTSLIRTINSLESiDRGEIVLFGNDFIKAGKRDDAPV-----IRQGIRRI-GMVFQN 347
Cdd:COG3593 14 IKDLSIELSDDLTV-LVGENNSGKSSILEALRLLLG-PSSSRKFDEEDFYLGDDPDLPEIeieltFGSLLSRLlRLLLKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 348 FNLFPHRTILDNV-------------ILAPRYHGLADSAELRRKGHG-----LLDRVGL-LAHAHKYP-HQLSGGQQQRV 407
Cdd:COG3593 92 EDKEELEEALEELneelkealkalneLLSEYLKELLDGLDLELELSLdeledLLKSLSLrIEDGKELPlDRLGSGFQRLI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 408 AIARALAM-------EPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSIS-DRIVFMENGHVVTD 479
Cdd:COG3593 172 LLALLSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVPlENIRRLRRDSGGTT 251
|
250 260
....*....|....*....|..
gi 2084914118 480 ASPASIRSEGDPR-VRRFIGLE 500
Cdd:COG3593 252 STKLIDLDDEDLRkLLRYLGVT 273
|
|
| PhnE |
COG3639 |
ABC-type phosphate/phosphonate transport system, permease component [Inorganic ion transport ... |
4-148 |
7.09e-05 |
|
ABC-type phosphate/phosphonate transport system, permease component [Inorganic ion transport and metabolism];
Pssm-ID: 442856 [Multi-domain] Cd Length: 244 Bit Score: 44.30 E-value: 7.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 4 DWAYFfslfsvSAFWKACLTVVQLSTLSWSIGLVLGF---LLASAKLSGHAWLRMPASFYIWLFRSIPLLVL-LVFVynl 79
Cdd:COG3639 42 DWSYL------PDLLSALLETLAIALLGTLLGAVLALplaFLAARNLAPNPWVRLLARRLLNVLRAIPELVWaLIFV--- 112
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084914118 80 pqlfPVTGsvLSqPFySGLIALVLTETAYMaeihrGGLLS-----VLKGQREAAKALGIRGVGAQRLVIIPQAI 148
Cdd:COG3639 113 ----AAVG--LG-PF-AGVLALAIHTIGFL-----GKLFAeaieeIDPGPVEALRATGASRLQVIRYGVLPQVL 173
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
399-482 |
3.00e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.68 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 399 LSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSIS-DRIVFMENGHVV 477
Cdd:PLN03140 1020 LSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSIDIFEAfDELLLMKRGGQV 1099
|
....*
gi 2084914118 478 TDASP 482
Cdd:PLN03140 1100 IYSGP 1104
|
|
| PhnE |
TIGR01097 |
phosphonate ABC transporter, permease protein PhnE; Phosphonates are a class of compound ... |
4-148 |
4.99e-04 |
|
phosphonate ABC transporter, permease protein PhnE; Phosphonates are a class of compound analogous to organic phosphates, but in which the C-O-P linkage is replaced by a direct, stable C-P bond. Some bacteria can utilize phosphonates as a source of phosphorus. This family consists of permease proteins of known or predicted phosphonate ABC transporters. Often this protein is found as a duplicated pair, occasionally as a fused pair. Certain "second" copies score in between the trusted and noise cutoff and should be considered true hits (by context). [Transport and binding proteins, Anions]
Pssm-ID: 273441 [Multi-domain] Cd Length: 250 Bit Score: 41.76 E-value: 4.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 4 DWAYFfslfsvSAFWKACLTVVQLSTLSWSIGLVLGF---LLASAKLSGHAWLRMPASFYIWLFRSIPLLVL-LVFVYnl 79
Cdd:TIGR01097 49 DWSYL------PRILKALLETLAMAILGTVLAAVLAVplaLLAARNITPSPWLYGLARLLLNFLRAIPELVWaLIFVA-- 120
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2084914118 80 pqlfpvtgSVLSQPFySGLIALVLTETAYMAEIHRGGLLSVLKGQREAAKALGIRGVGAQRLVIIPQAI 148
Cdd:TIGR01097 121 --------AVGLGPF-AGVLALAFHTVGFLGKLFAEAIEEVDPGPVEALRATGASKLQVIRYGVLPQVL 180
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
329-469 |
5.52e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 42.65 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 329 DDAPVIRQ-GIRRIGMVFQNFnlfPHRTILDNVILAP-----RYHG-LADSAELRRKGHGLLDRVGLLAHAHKYPHQ-LS 400
Cdd:TIGR00618 876 DKLNGINQiKIQFDGDALIKF---LHEITLYANVRLAnqsegRFHGrYADSHVNARKYQGLALLVADAYTGSVRPSAtLS 952
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2084914118 401 GGQQQRVAIARALAMEP----------DIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFALSISDRIV 469
Cdd:TIGR00618 953 GGETFLASLSLALALADllstsggtvlDSLFIDEGFGSLDEDSLDRAIGILDAIREGSKMIGIISHVPEFRERIPHRIL 1031
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
399-469 |
7.23e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 7.23e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2084914118 399 LSGGQQQRVAIARAL---AMEPDIMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDFaLSISDRIV 469
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHV-VKVADYVL 882
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
397-457 |
7.35e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 7.35e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2084914118 397 HQLSGGQQQRVAIARALAMEPDIMLFDEPTSALDPELVgEVLnvIRDLAREGMTMLIVTHE 457
Cdd:PLN03073 626 YTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAV-EAL--IQGLVLFQGGVLMVSHD 683
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
399-459 |
7.67e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 42.32 E-value: 7.67e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2084914118 399 LSGGQQQRVAIARALAmEPD----IMLFDEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMD 459
Cdd:COG0178 827 LSGGEAQRVKLASELS-KRStgktLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNLD 890
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
399-485 |
7.77e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 42.31 E-value: 7.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 399 LSGGQQQRVAIARALAMEPDIMLF--DEPTSALDPELVGEVLNVIRDLAREGMTMLIVTHEMDfALSISDRIVFM----- 471
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGLTGVLYvlDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDED-TIRAADYVIDIgpgag 567
|
90
....*....|....*
gi 2084914118 472 -ENGHVVTDASPASI 485
Cdd:TIGR00630 568 eHGGEVVASGTPEEI 582
|
|
| FbpB |
COG1178 |
ABC-type Fe3+ transport system, permease component [Inorganic ion transport and metabolism]; |
1-218 |
8.27e-04 |
|
ABC-type Fe3+ transport system, permease component [Inorganic ion transport and metabolism];
Pssm-ID: 440791 [Multi-domain] Cd Length: 538 Bit Score: 42.07 E-value: 8.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 1 MAFDWAYFFSLFSVSAFWKACLTVVQLSTLSWSIGLVLGFLLASAKLSGHAWLRMPASFYIWLFRSIPLLVL---LVFVY 77
Cdd:COG1178 320 DNLTLDNYRFVLLDPSLLRALLNSLLLALLAALLAVLLALLLAYLVRRRRGRLARLLDRLAMLPYAVPGIVLglgLLLLF 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 78 NLPQLFPVTGSVLsqpfysgLIALVLTeTAYMAEIHR---GGLLSVLKGQREAAKALGIRGVGAQRLVIIPQAIRislpt 154
Cdd:COG1178 400 NRPLPLLLYGTLA-------ILVLAYV-VRFLPFALRsleAALAQIDPSLEEAARSLGASPLRTLRRVTLPLLRP----- 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 155 ltneyvTIVKLTSLVSVISLNEL---LLvgqrLYAQNFLVLETL-------------AAVAIYYVLIVTLFGWLLQWAER 218
Cdd:COG1178 467 ------GLLAAALLVFVTSMKELsatLL----LRPPGFETLAVLiyqlassgrygeaAALALLLVLVSLLPVLLLERLLG 536
|
|
| ABC_ATPase |
pfam09818 |
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. ... |
400-481 |
1.30e-03 |
|
ATPase of the ABC class; This is the C-terminal ATPase domain from bacterial ABC class ATPases. This entry also includes MRB1590 from Trypanosoma brucei brucei has a central ATPase domain homologous to this domain.
Pssm-ID: 462914 Cd Length: 282 Bit Score: 40.66 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 400 SGGQQQRVAIARALAMEPDIMLFDEPTSA--------LDPELVG---EVLNVIRDLARE-----GMTMLIVTHEMDFALS 463
Cdd:pfam09818 159 SGSTSQAANIMEALEAGASLLLIDEDTSAtnfmirdeRMQALVSkdkEPITPFVDRVRSlyddlGVSTILVVGGSGDYLD 238
|
90
....*....|....*...
gi 2084914118 464 ISDRIVFMENgHVVTDAS 481
Cdd:pfam09818 239 VADTVILMDE-YRPSDVT 255
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
398-473 |
1.32e-03 |
|
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213239 [Multi-domain] Cd Length: 243 Bit Score: 40.32 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2084914118 398 QLSGGQQQRVAIARALAM---EPDIM-LFDEPTSALDPELVGEVLNVIRDLAREgmTMLIVT---HEMdfaLSISDRI-- 468
Cdd:cd03272 158 QLSGGQKSLVALALIFAIqkcDPAPFyLFDEIDAALDAQYRTAVANMIKELSDG--AQFITTtfrPEL---LEVADKFyg 232
|
....*
gi 2084914118 469 VFMEN 473
Cdd:cd03272 233 VKFRN 237
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
396-457 |
2.53e-03 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 40.41 E-value: 2.53e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2084914118 396 PHQLSGGQQQ------RVAIARALA--------MEPdiMLFDEPTSALDPELVGEVLNVIRDLAREGM-TMLIVTHE 457
Cdd:PRK02224 779 PEQLSGGERAlfnlslRCAIYRLLAegiegdapLPP--LILDEPTVFLDSGHVSQLVDLVESMRRLGVeQIVVVSHD 853
|
|
| |
