|
Name |
Accession |
Description |
Interval |
E-value |
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-331 |
1.42e-144 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 411.78 E-value: 1.42e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTADGRLSAvLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRR 80
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTA-LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRAIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:COG1135 80 ARRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 161 SVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSLLGQQ 240
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 241 LLPLTPA------------AATHSDLLLRLSYRWDvPVATDWISRLSQQWALQIDLLGGHVEVINGRLAGRLQagVRFQG 308
Cdd:COG1135 240 FLPTVLNdelpeellarlrEAAGGGRLVRLTFVGE-SADEPLLSELARRFGVDVNILSGGIEEIQGTPVGRLI--VELEG 316
|
330 340
....*....|....*....|...
gi 1319887251 309 ERLSPARLQGLLAQLGITAEILD 331
Cdd:COG1135 317 DDAAIDAALAYLREQGVVVEVLG 339
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-330 |
3.35e-107 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 316.74 E-value: 3.35e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTADGRLSAvLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRR 80
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHA-LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRAIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:PRK11153 80 ARRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 161 SVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARP------- 233
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPkhpltre 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 234 --DSLLGQQLLP-----LTPAAATHSDLLLRLSYRW---DVPVatdwISRLSQQWALQIDLLGGHVEVINGRLAGRLQAG 303
Cdd:PRK11153 240 fiQSTLHLDLPEdylarLQAEPTTGSGPLLRLEFTGesvDAPL----LSETARRFGVDFNILSGQIDYIGGVKFGSLLVE 315
|
330 340
....*....|....*....|....*..
gi 1319887251 304 VRfqGERLSPARLQGLLAQLGITAEIL 330
Cdd:PRK11153 316 LT--GDPGDIQAAIAYLQEHGVKVEVL 340
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-233 |
1.48e-101 |
|
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: 298.34 E-value: 1.48e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTADGRLSAvLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRR 80
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTA-LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRAIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:cd03258 80 ARRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1319887251 161 SVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARP 233
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-239 |
5.25e-86 |
|
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: 259.14 E-value: 5.25e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYrtaDGRLsaVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRR 80
Cdd:COG1127 5 MIEVRNLTKSF---GDRV--VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRAIGTVFQSSALLSRRTAWENVALPL-AWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALR 159
Cdd:COG1127 80 LRRRIGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 160 PSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSLLGQ 239
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDDPWVRQ 239
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-221 |
2.05e-85 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 256.89 E-value: 2.05e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTADGRLsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRR 80
Cdd:COG1136 4 LLELRNLTKSYGTGEGEV-TALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERR-AIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALR 159
Cdd:COG1136 83 LRRrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1319887251 160 PSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRtAADAVAEIRDGTIV 221
Cdd:COG1136 163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAA-RADRVIRLRDGRIV 223
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-235 |
4.51e-81 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 246.44 E-value: 4.51e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYrtadGRLsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSAlSGEALRR 80
Cdd:COG1126 1 MIEIENLHKSF----GDL-EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTD-SKKDINK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRAIGTVFQSSALLSRRTAWENVALPLAW-LGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALR 159
Cdd:COG1126 75 LRRKVGMVFQQFNLFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1319887251 160 PSVLLADEATSGLDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDS 235
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-220 |
8.33e-80 |
|
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: 242.40 E-value: 8.33e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRTADGRLSAvLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRE 81
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQA-LKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRA-IGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:cd03255 80 RRRhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 161 SVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTaADAVAEIRDGTI 220
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-248 |
6.81e-79 |
|
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: 249.82 E-value: 6.81e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTADGRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRR 80
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRAIGTVFQ--SSALLSRRTAWENVALPLAWLGVV-ERDIKARVGELLESVGLSHK-ADAWPAQLSGGQRQRIGIARAL 156
Cdd:COG1123 340 LRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLsRAERRERVAELLERVGLPPDlADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 157 ALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSL 236
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHP 499
|
250
....*....|..
gi 1319887251 237 LGQQLLPLTPAA 248
Cdd:COG1123 500 YTRALLAAVPSL 511
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-239 |
1.10e-77 |
|
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: 237.79 E-value: 1.10e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRTadgrlSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRE 81
Cdd:cd03261 1 IELRGLTKSFGG-----RTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQSSALLSRRTAWENVALPL-AWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:cd03261 76 RRRMGMLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1319887251 161 SVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSLLGQ 239
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDDPLVRQ 234
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-221 |
1.25e-73 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 226.86 E-value: 1.25e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRtaDGRLsaVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRR 80
Cdd:COG2884 1 MIRFENVSKRYP--GGRE--ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRAIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:COG2884 77 LRRRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1319887251 161 SVLLADEATSGLDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTIV 221
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-220 |
1.79e-72 |
|
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: 223.56 E-value: 1.79e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRTAdgrlsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSAlSGEALRRE 81
Cdd:cd03262 1 IEIKNLHKSFGDF-----HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINEL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQSSALLSRRTAWENVALPLAW-LGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:cd03262 75 RQKVGMVFQQFNLFPHLTVLENITLAPIKvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 161 SVLLADEATSGLDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTI 220
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-242 |
2.11e-71 |
|
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: 221.99 E-value: 2.11e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTADGRLsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSalsGEALRR 80
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRV-PVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVT---RRRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRAIGTVFQS--SALLSRRTAWENVALPLAWLGVveRDIKARVGELLESVGLSHK-ADAWPAQLSGGQRQRIGIARALA 157
Cdd:COG1124 77 FRRRVQMVFQDpyASLHPRHTVDRILAEPLRIHGL--PDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 158 LRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSLL 237
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPY 234
|
....*
gi 1319887251 238 GQQLL 242
Cdd:COG1124 235 TRELL 239
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-224 |
6.14e-69 |
|
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: 215.06 E-value: 6.14e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTADGRLSAVlKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRR 80
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKAL-DDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRAIGTVFQ--SSALLSRRTAWENVALPLAWLGVVERD--IKARVGELLESVGLSHK-ADAWPAQLSGGQRQRIGIARA 155
Cdd:cd03257 80 RRKEIQMVFQdpMSSLNPRMTIGEQIAEPLRIHGKLSKKeaRKEAVLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1319887251 156 LALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYG 224
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-233 |
1.04e-67 |
|
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: 214.92 E-value: 1.04e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTADGRLSAVlKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQP---DSGSIRINGQDLSALSGEA 77
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAV-DGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 78 LRRER-RAIGTVFQS--SALLSRRTAWENVALPL-AWLGVVERDIKARVGELLESVGLSHK---ADAWPAQLSGGQRQRI 150
Cdd:COG0444 80 LRKIRgREIQMIFQDpmTSLNPVMTVGDQIAEPLrIHGGLSKAEARERAIELLERVGLPDPerrLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 151 GIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLL 230
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELF 239
|
...
gi 1319887251 231 ARP 233
Cdd:COG0444 240 ENP 242
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-236 |
1.12e-67 |
|
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: 211.81 E-value: 1.12e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLykSYRTADGRlsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRE 81
Cdd:COG1122 1 IELENL--SFSYPGGT--PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 rraIGTVFQSS-ALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:COG1122 77 ---VGLVFQNPdDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1319887251 161 SVLLADEATSGLDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSL 236
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELL 228
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-229 |
1.79e-67 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 212.22 E-value: 1.79e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTADgrlsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRR 80
Cdd:COG3638 2 MLELRNLSKRYPGGT----PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRAIGTVFQSSALLSRRTAWENV--------ALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGI 152
Cdd:COG3638 78 LRRRIGMIFQQFNLVPRLSVLTNVlagrlgrtSTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1319887251 153 ARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDL 229
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-206 |
9.60e-67 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 210.72 E-value: 9.60e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTADGRLsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEalrr 80
Cdd:COG1116 7 ALELRGVSKRFPTGGGGV-TALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 erraIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:COG1116 82 ----RGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1319887251 161 SVLLADEATSGLDPQaTASVL-ALLKRLRDEYQLAIVLITHEMD-AVR 206
Cdd:COG1116 158 EVLLMDEPFGALDAL-TRERLqDELLRLWQETGKTVLFVTHDVDeAVF 204
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-236 |
9.35e-66 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 211.11 E-value: 9.35e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTAdgrlsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgealrR 80
Cdd:COG3842 5 ALELENVSKRYGDV-----TALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP-----P 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRAIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:COG3842 75 EKRNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1319887251 161 SVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEM-DAVrTAADAVAEIRDGTIVQYGRIEDLLARPDSL 236
Cdd:COG3842 155 RVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQeEAL-ALADRIAVMNDGRIEQVGTPEEIYERPATR 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-224 |
8.52e-65 |
|
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: 203.91 E-value: 8.52e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 4 IDDLYKSYRTADgrlsaVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgealrRERR 83
Cdd:cd03259 3 LKGLSKTYGSVR-----ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP-----PERR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 84 AIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVL 163
Cdd:cd03259 73 NIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1319887251 164 LADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYG 224
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-222 |
5.11e-63 |
|
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: 199.62 E-value: 5.11e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRTADGRLSaVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGqdlsalsgEALRRE 81
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVT-ALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG--------EPVTGP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPS 161
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1319887251 162 VLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMD-AVRTaADAVA--EIRDGTIVQ 222
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDeAVFL-ADRVVvlSARPGRIVA 214
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-232 |
7.44e-63 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 199.90 E-value: 7.44e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYrtadGRLSAVlKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRe 81
Cdd:COG1131 1 IEVRGLTKRY----GDKTAL-DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 rraIGTVFQSSALLSRRTAWENVALpLAWL-GVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:COG1131 75 ---IGYVPQEPALYPDLTVRENLRF-FARLyGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDP 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1319887251 161 SVLLADEATSGLDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLAR 232
Cdd:COG1131 151 ELLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR 221
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-219 |
1.27e-62 |
|
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: 198.46 E-value: 1.27e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 4 IDDLYKSYrtaDGRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRErr 83
Cdd:cd03225 2 LKNLSFSY---PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 84 aIGTVFQSSAL-LSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSV 162
Cdd:cd03225 77 -VGLVFQNPDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1319887251 163 LLADEATSGLDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGT 219
Cdd:cd03225 156 LLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-222 |
7.95e-62 |
|
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: 196.89 E-value: 7.95e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTADGRLSaVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRR 80
Cdd:COG4181 8 IIELRGLTKTVGTGAGELT-ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRA-IGTVFQSSALLSRRTAWENVALPLAWLGvvERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALR 159
Cdd:COG4181 87 LRARhVGFVFQSFQLLPTLTALENVMLPLELAG--RRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1319887251 160 PSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEM-DAVRtaADAVAEIRDGTIVQ 222
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPaLAAR--CDRVLRLRAGRLVE 226
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-233 |
1.84e-61 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 199.19 E-value: 1.84e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 4 IDDLYKSY---RTADGRLSAVLK---GLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEA 77
Cdd:COG4608 10 VRDLKKHFpvrGGLFGRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 78 LRRERRAIGTVFQ--SSALLSRRTAWENVALPLAWLGVV-ERDIKARVGELLESVGL--SHkADAWPAQLSGGQRQRIGI 152
Cdd:COG4608 90 LRPLRRRMQMVFQdpYASLNPRMTVGDIIAEPLRIHGLAsKAERRERVAELLELVGLrpEH-ADRYPHEFSGGQRQRIGI 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 153 ARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLAR 232
Cdd:COG4608 169 ARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYAR 248
|
.
gi 1319887251 233 P 233
Cdd:COG4608 249 P 249
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-229 |
8.20e-61 |
|
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: 194.71 E-value: 8.20e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYrtADGRlsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRE 81
Cdd:cd03256 1 IEVENLSKTY--PNGK--KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQSSALLSRRTAWENVALPL--------AWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIA 153
Cdd:cd03256 77 RRQIGMIFQQFNLIERLSVLENVLSGRlgrrstwrSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1319887251 154 RALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDL 229
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-233 |
3.15e-59 |
|
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: 190.59 E-value: 3.15e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYrtadGRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRE 81
Cdd:cd03295 1 IEFENVTKRY----GGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 rraIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGL--SHKADAWPAQLSGGQRQRIGIARALALR 159
Cdd:cd03295 77 ---IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAAD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1319887251 160 PSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARP 233
Cdd:cd03295 154 PPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSP 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-219 |
4.45e-59 |
|
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: 188.16 E-value: 4.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRTADgrlsaVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEaLRRE 81
Cdd:cd03229 1 LELKNVSKRYGQKT-----VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDE-LPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQSSALLSRRTAWENVALPlawlgvverdikarvgellesvglshkadawpaqLSGGQRQRIGIARALALRPS 161
Cdd:cd03229 75 RRRIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1319887251 162 VLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGT 219
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-255 |
1.69e-58 |
|
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: 196.66 E-value: 1.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLykSYRTADGRLSAVlKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPD---SGSIRINGQDLSALSgEA 77
Cdd:COG1123 4 LLEVRDL--SVRYPGGDVPAV-DGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELS-EA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 78 LRRERraIGTVFQS-SALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARAL 156
Cdd:COG1123 80 LRGRR--IGMVFQDpMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 157 ALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSL 236
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQAL 237
|
250 260
....*....|....*....|....
gi 1319887251 237 -----LGQQLLPLTPAAATHSDLL 255
Cdd:COG1123 238 aavprLGAARGRAAPAAAAAEPLL 261
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-242 |
6.07e-58 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 188.09 E-value: 6.07e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYrtadGRLSaVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQ----------DL 70
Cdd:COG4598 8 ALEVRDLHKSF----GDLE-VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEeirlkpdrdgEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 71 SALSGEALRRERRAIGTVFQSSALLSRRTAWENVAL-PLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQR 149
Cdd:COG4598 83 VPADRRQLQRIRTRLGMVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 150 IGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVlITHEMDAVRTAADAVAEIRDGTIVQYGRIEDL 229
Cdd:COG4598 163 AAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLV-VTHEMGFARDVSSHVVFLHQGRIEEQGPPAEV 241
|
250
....*....|...
gi 1319887251 230 LARPDSLLGQQLL 242
Cdd:COG4598 242 FGNPKSERLRQFL 254
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-220 |
9.53e-58 |
|
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: 186.07 E-value: 9.53e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYrtadGRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRE 81
Cdd:cd03292 1 IEFINVTKTY----PNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPS 161
Cdd:cd03292 77 RRKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1319887251 162 VLLADEATSGLDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTI 220
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-224 |
1.14e-57 |
|
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: 186.74 E-value: 1.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTADgrlsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRR 80
Cdd:TIGR02315 1 MLEVENLSKVYPNGK----QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRAIGTVFQSSALLSRRTAWENVALP-LA-------WLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGI 152
Cdd:TIGR02315 77 LRRRIGMIFQHYNLIERLTVLENVLHGrLGykptwrsLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1319887251 153 ARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYG 224
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDG 228
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-236 |
1.92e-57 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 189.51 E-value: 1.92e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTADgrlsaVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgealrR 80
Cdd:COG3839 3 SLELENVSKSYGGVE-----ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLP-----P 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRAIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:COG3839 73 KDRNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1319887251 161 SVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSL 236
Cdd:COG3839 153 KVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANL 228
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-236 |
2.14e-57 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 189.20 E-value: 2.14e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRTADgrlsaVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDL-SALSGealrR 80
Cdd:COG1118 3 IEVRNISKRFGSFT-----LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPP----R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRaIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:COG1118 74 ERR-VGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1319887251 161 SVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSL 236
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATP 228
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
26-233 |
4.28e-57 |
|
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: 185.92 E-value: 4.28e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 26 SLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRERR-AIGTVFQSSALLSRRTAWENV 104
Cdd:cd03294 44 SLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRkKISMVFQSFALLPHRTVLENV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 105 ALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLALL 184
Cdd:cd03294 124 AFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDEL 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1319887251 185 KRLRDEYQLAIVLITHEMD-AVRTaADAVAEIRDGTIVQYGRIEDLLARP 233
Cdd:cd03294 204 LRLQAELQKTIVFITHDLDeALRL-GDRIAIMKDGRLVQVGTPEEILTNP 252
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-224 |
1.05e-56 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 183.54 E-value: 1.05e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRTadgrlSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLL-----EQPDSGSIRINGQDLSALSGE 76
Cdd:cd03260 1 IELRDLNVYYGD-----KHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 77 ALRReRRAIGTVFQSSALLsRRTAWENVALPLAWLGVVERD-IKARVGELLESVGLSH--KADAWPAQLSGGQRQRIGIA 153
Cdd:cd03260 76 VLEL-RRRVGMVFQKPNPF-PGSIYDNVAYGLRLHGIKLKEeLDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1319887251 154 RALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYqlAIVLITHEMDAVRTAADAVAEIRDGTIVQYG 224
Cdd:cd03260 154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFG 222
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-242 |
1.75e-56 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 183.80 E-value: 1.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTadgrlSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRIN------GQDLSALS 74
Cdd:PRK11264 3 AIEVKNLVKKFHG-----QTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGditidtARSLSQQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 75 GeALRRERRAIGTVFQSSALLSRRTAWENVAL-PLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIA 153
Cdd:PRK11264 78 G-LIRQLRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 154 RALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQlAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARP 233
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADP 235
|
....*....
gi 1319887251 234 DSLLGQQLL 242
Cdd:PRK11264 236 QQPRTRQFL 244
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-249 |
2.02e-54 |
|
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: 186.04 E-value: 2.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 16 GRLSAVlKGLSLQVPERSITAVVGPSGAGKSTLARCISLLeQPDSGSIRINGQDLSALSGEALRRERRAIGTVFQS--SA 93
Cdd:COG4172 297 GHVKAV-DGVSLTLRRGETLGLVGESGSGKSTLGLALLRL-IPSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDpfGS 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 94 LLSRRTAWENVALPLAWLGV----VERDikARVGELLESVGLSHKA-DAWPAQLSGGQRQRIGIARALALRPSVLLADEA 168
Cdd:COG4172 375 LSPRMTVGQIIAEGLRVHGPglsaAERR--ARVAEALEEVGLDPAArHRYPHEFSGGQRQRIAIARALILEPKLLVLDEP 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 169 TSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSLLGQQLLpltpAA 248
Cdd:COG4172 453 TSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALL----AA 528
|
.
gi 1319887251 249 A 249
Cdd:COG4172 529 A 529
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-241 |
5.46e-54 |
|
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: 178.01 E-value: 5.46e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYrtaDGRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLsaLSGEALRRE 81
Cdd:TIGR04520 1 IEVENVSFSY---PESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT--LDEENLWEI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQS------SAllsrrTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARA 155
Cdd:TIGR04520 76 RKKVGMVFQNpdnqfvGA-----TVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 156 LALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMD-AVRtaADAVAEIRDGTIVQYGRIEDLLARPD 234
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEeAVL--ADRVIVMNKGKIVAEGTPREIFSQVE 228
|
....*..
gi 1319887251 235 SLLGQQL 241
Cdd:TIGR04520 229 LLKEIGL 235
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
22-277 |
8.09e-54 |
|
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: 178.03 E-value: 8.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRERRAIGTVFQ-SSALLSRRTA 100
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLRKKVGLVFQfPEHQLFEETV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 WENVALPLAWLGVVERDIKARVGELLESVGLSHK-ADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATAS 179
Cdd:TIGR04521 101 YKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGRKE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 180 VLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSLlgqqllpltpaaathsdlllrLS 259
Cdd:TIGR04521 181 ILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVDEL---------------------EK 239
|
250
....*....|....*...
gi 1319887251 260 YRWDVPVATDWISRLSQQ 277
Cdd:TIGR04521 240 IGLDVPEITELARKLKEK 257
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-226 |
8.84e-54 |
|
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: 177.15 E-value: 8.84e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYrtadGRLSAVlKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgeALRR 80
Cdd:COG0411 4 LLEVRGLTKRF----GGLVAV-DDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLP--PHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRAIGTVFQSSALLSRRTAWENVALPL------AWLGVV---------ERDIKARVGELLESVGLSHKADAWPAQLSGG 145
Cdd:COG0411 77 ARLGIARTFQNPRLFPELTVLENVLVAAharlgrGLLAALlrlprarreEREARERAEELLERVGLADRADEPAGNLSYG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 146 QRQRIGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVaeirdgTIVQYGR 225
Cdd:COG0411 157 QQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRI------VVLDFGR 230
|
.
gi 1319887251 226 I 226
Cdd:COG0411 231 V 231
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
21-236 |
3.26e-53 |
|
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: 174.73 E-value: 3.26e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEalrreRRAIGTVFQSSALLSRRTA 100
Cdd:cd03300 15 ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH-----KRPVNTVFQNYALFPHLTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 WENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASV 180
Cdd:cd03300 90 FENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDM 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1319887251 181 LALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSL 236
Cdd:cd03300 170 QLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANR 225
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
19-235 |
5.74e-53 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 174.51 E-value: 5.74e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 19 SAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGqdLSALSGEALRRE-RRAIGTVFQSSALLSR 97
Cdd:PRK09493 14 TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVDERLiRQEAGMVFQQFYLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 98 RTAWENVAL-PLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQA 176
Cdd:PRK09493 92 LTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPEL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1319887251 177 TASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDS 235
Cdd:PRK09493 172 RHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPS 229
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-230 |
1.29e-52 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 174.08 E-value: 1.29e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYrtaDGRlsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgealRR 80
Cdd:COG1120 1 MLEAENLSVGY---GGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLS----RR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ER-RAIGTVFQSSALLSRRTAWENVAL---P-LAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARA 155
Cdd:COG1120 72 ELaRRIAYVPQEPPAPFGLTVRELVALgryPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1319887251 156 LALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLL 230
Cdd:COG1120 152 LAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-235 |
5.37e-52 |
|
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: 171.75 E-value: 5.37e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgealrRERRAIGTVFQSSALLSRRTA 100
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP-----PEKRDISYVPQNYALFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 WENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASV 180
Cdd:cd03299 89 YKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1319887251 181 LALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDS 235
Cdd:cd03299 169 REELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKN 223
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-311 |
1.24e-51 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 174.50 E-value: 1.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYrtadGRlSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGealrRE 81
Cdd:PRK10851 3 IEIANIKKSF----GR-TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA----RD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRaIGTVFQSSALLSRRTAWENVALPLAWLGVVER----DIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALA 157
Cdd:PRK10851 74 RK-VGFVFQHYALFRHMTVFDNIAFGLTVLPRRERpnaaAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 158 LRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDS-- 235
Cdd:PRK10851 153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATrf 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 236 --------------LLGQQL--------LPLTPAAATHSDLLLR---------LSYRWDVPVATDWISRLSQQWALQIDL 284
Cdd:PRK10851 233 vlefmgevnrlqgtIRGGQFhvgahrwpLGYTPAYQGPVDLFLRpwevdisrrTSLDSPLPVQVLEVSPKGHYWQLVVQP 312
|
330 340
....*....|....*....|....*..
gi 1319887251 285 LGGHVEVINGRLAGRLQAGVRfqGERL 311
Cdd:PRK10851 313 LGWYNEPLTVVMHGDIDAPQR--GERL 337
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-232 |
2.24e-51 |
|
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: 170.42 E-value: 2.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTadgrlSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEAlrr 80
Cdd:COG4555 1 MIEVENLSKKYGK-----VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREA--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 eRRAIGTVFQSSALLSRRTAWENVALpLAWL-GVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALR 159
Cdd:COG4555 73 -RRQIGVLPDERGLYDRLTVRENIRY-FAELyGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1319887251 160 PSVLLADEATSGLDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLAR 232
Cdd:COG4555 151 PKVLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-235 |
2.26e-51 |
|
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: 170.21 E-value: 2.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYrtadGRLSAvLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEalrre 81
Cdd:cd03296 3 IEVRNVSKRF----GDFVA-LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQSSALLSRRTAWENVALPLAWLGVVER----DIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALA 157
Cdd:cd03296 73 ERNVGFVFQHYALFRHMTVFDNVAFGLRVKPRSERppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1319887251 158 LRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDS 235
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPAS 230
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-230 |
3.06e-51 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 170.27 E-value: 3.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYrtaDGRLsaVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLsalsgealRR 80
Cdd:COG1121 6 AIELENLTVSY---GGRP--VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP--------RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRAIGTVFQSSALlSRR---TAWENVALPLA----WLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIA 153
Cdd:COG1121 73 ARRRIGYVPQRAEV-DWDfpiTVRDVVLMGRYgrrgLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1319887251 154 RALALRPSVLLADEATSGLDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIrDGTIVQYGRIEDLL 230
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVL 226
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
5-247 |
3.94e-50 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 169.76 E-value: 3.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 5 DDLYKSYRTADGRLSA-----VLKGLSLQVpERSIT-AVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEAL 78
Cdd:PRK11308 9 IDLKKHYPVKRGLFKPerlvkALDGVSFTL-ERGKTlAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 79 RRERRAIGTVFQS--SALLSRRTAWENVALPLAW---LGVVERdiKARVGELLESVGL-SHKADAWPAQLSGGQRQRIGI 152
Cdd:PRK11308 88 KLLRQKIQIVFQNpyGSLNPRKKVGQILEEPLLIntsLSAAER--REKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 153 ARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLAR 232
Cdd:PRK11308 166 ARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNN 245
|
250
....*....|....*
gi 1319887251 233 PDSLLGQQLLPLTPA 247
Cdd:PRK11308 246 PRHPYTQALLSATPR 260
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
21-220 |
4.85e-50 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 165.76 E-value: 4.85e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRErraIGTVFQSSALLSrrta 100
Cdd:COG4619 15 ILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQ---VAYVPQEPALWG---- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 wENVA--LPLAWLGVVERDIKARVGELLESVGLSHKADAWPA-QLSGGQRQRIGIARALALRPSVLLADEATSGLDPQAT 177
Cdd:COG4619 88 -GTVRdnLPFPFQLRERKFDRERALELLERLGLPPDILDKPVeRLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENT 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1319887251 178 ASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTI 220
Cdd:COG4619 167 RRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-220 |
5.16e-50 |
|
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: 164.49 E-value: 5.16e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRTadgrlSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRe 81
Cdd:cd03230 1 IEVRNLSKRYGK-----KTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 rraIGTVFQSSALLSRRTAWENValplawlgvverdikarvgellesvglshkadawpaQLSGGQRQRIGIARALALRPS 161
Cdd:cd03230 75 ---IGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1319887251 162 VLLADEATSGLDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTI 220
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
26-259 |
7.46e-50 |
|
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: 169.90 E-value: 7.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 26 SLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDL-SALSGEALRRERRAIGTVFQSSALLSRRTAWENV 104
Cdd:COG4148 19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLqDSARGIFLPPHRRRIGYVFQEARLFPHLSVRGNL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 105 ALPLAWLGVVERdiKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLALL 184
Cdd:COG4148 99 LYGRKRAPRAER--RISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILPYL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 185 KRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPD--SLLGQQ----LLPLTPAAATHSDLLLRL 258
Cdd:COG4148 177 ERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDllPLAGGEeagsVLEATVAAHDPDYGLTRL 256
|
.
gi 1319887251 259 S 259
Cdd:COG4148 257 A 257
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
2-234 |
3.89e-49 |
|
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: 164.53 E-value: 3.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYrtadGRLSAVlKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgeALRRE 81
Cdd:cd03219 1 LEVRGLTKRF----GGLVAL-DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLP--PHEIA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQSSALLSRRTAWENVALP----------LAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIG 151
Cdd:cd03219 74 RLGIGRTFQIPRLFPELTVLENVMVAaqartgsgllLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 152 IARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLA 231
Cdd:cd03219 154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
...
gi 1319887251 232 RPD 234
Cdd:cd03219 233 NPR 235
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
21-224 |
8.11e-49 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 164.03 E-value: 8.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQ--DLSA-LSGEALRRERRAIGTVFQSSALLSR 97
Cdd:COG4161 17 ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQkPSEKAIRLLRQKVGMVFQQYNLWPH 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 98 RTAWEN-VALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQA 176
Cdd:COG4161 97 LTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDPEI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1319887251 177 TASVLALLKRLRdeyQLAI--VLITHEMDAVRTAADAVAEIRDGTIVQYG 224
Cdd:COG4161 177 TAQVVEIIRELS---QTGItqVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-242 |
1.14e-48 |
|
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: 171.02 E-value: 1.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTADGRLSAVlKGLSLQVPERSITAVVGPSGAGKSTLARCI-SLLEQPD---SGSIRINGQDLSALSGE 76
Cdd:COG4172 6 LLSVEDLSVAFGQGGGTVEAV-KGVSFDIAAGETLALVGESGSGKSVTALSIlRLLPDPAahpSGSILFDGQDLLGLSER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 77 ALRRER-RAIGTVFQ--SSALLSRRTAWENVALPLAW-LGVVERDIKARVGELLESVGLSH---KADAWPAQLSGGQRQR 149
Cdd:COG4172 85 ELRRIRgNRIAMIFQepMTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDperRLDAYPHQLSGGQRQR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 150 IGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDL 229
Cdd:COG4172 165 VMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAEL 244
|
250
....*....|...
gi 1319887251 230 LARPDSLLGQQLL 242
Cdd:COG4172 245 FAAPQHPYTRKLL 257
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-224 |
1.48e-48 |
|
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: 162.04 E-value: 1.48e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRTadgrlSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEalrre 81
Cdd:cd03301 1 VELENVTKRFGN-----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPS 161
Cdd:cd03301 71 DRDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1319887251 162 VLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYG 224
Cdd:cd03301 151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-242 |
2.41e-48 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 163.22 E-value: 2.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRTADgrlsaVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQD----------LS 71
Cdd:PRK10619 6 LNVIDLHKRYGEHE-----VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqLK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 72 ALSGEALRRERRAIGTVFQSSALLSRRTAWENV-ALPLAWLGVVERDIKARVGELLESVGLSHKA-DAWPAQLSGGQRQR 149
Cdd:PRK10619 81 VADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 150 IGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQlAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDL 229
Cdd:PRK10619 161 VSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
250
....*....|...
gi 1319887251 230 LARPDSLLGQQLL 242
Cdd:PRK10619 240 FGNPQSPRLQQFL 252
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
19-224 |
2.96e-48 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 162.49 E-value: 2.96e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 19 SAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQ--DLSALSGE-ALRRERRAIGTVFQSSALL 95
Cdd:PRK11124 15 HQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDkAIRELRRNVGMVFQQYNLW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 96 SRRTAWEN-VALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDP 174
Cdd:PRK11124 95 PHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALDP 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1319887251 175 QATASVLALLKRLRdEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYG 224
Cdd:PRK11124 175 EITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-235 |
4.89e-48 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 161.46 E-value: 4.89e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLykSYRTADGRLSAvlkglSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEalrr 80
Cdd:COG3840 1 MLRLDDL--TYRYGDFPLRF-----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA---- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 eRRAIGTVFQSSALLSRRTAWENVAL---PLAWLGVVERdikARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALA 157
Cdd:COG3840 70 -ERPVSMLFQENNLFPHLTVAQNIGLglrPGLKLTAEQR---AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1319887251 158 LRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDS 235
Cdd:COG3840 146 RKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPP 223
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
21-233 |
1.21e-47 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 161.36 E-value: 1.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLL--EQPD---SGSIRINGQDLSAlSGEALRRERRAIGTVFQSSALL 95
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDIYD-PDVDVVELRRRVGMVFQKPNPF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 96 SRrTAWENVALPLAWLGVVER-DIKARVGELLESVGL----SHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATS 170
Cdd:COG1117 105 PK-SIYDNVAYGLRLHGIKSKsELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTS 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1319887251 171 GLDPQATASVLALLKRLRDEYqlAIVLITHEMD-AVRtAADAVAEIRDGTIVQYGRIEDLLARP 233
Cdd:COG1117 184 ALDPISTAKIEELILELKKDY--TIVIVTHNMQqAAR-VSDYTAFFYLGELVEFGPTEQIFTNP 244
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
21-224 |
2.42e-47 |
|
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: 159.24 E-value: 2.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLsalsgealRRERRAIGTVFQSSALLSRR-- 98
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL--------EKERKRIGYVPQRRSIDRDFpi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 99 TAWENVALPLA----WLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDP 174
Cdd:cd03235 86 SVRDVVLMGLYghkgLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1319887251 175 QATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIrDGTIVQYG 224
Cdd:cd03235 166 KTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL-NRTVVASG 213
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-218 |
2.75e-47 |
|
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: 157.54 E-value: 2.75e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYrtaDGRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALrre 81
Cdd:cd03228 1 IEFKNVSFSY---PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQSSALLSrRTAWENValplawlgvverdikarvgellesvglshkadawpaqLSGGQRQRIGIARALALRPS 161
Cdd:cd03228 75 RKNIAYVPQDPFLFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1319887251 162 VLLADEATSGLDPQATASVLALLKRLRDEyqLAIVLITHEMDAVRtAADAVAEIRDG 218
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRALAKG--KTVIVIAHRLSTIR-DADRIIVLDDG 170
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-229 |
6.69e-47 |
|
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: 158.30 E-value: 6.69e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYrtadGRLSAVlKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEAlrre 81
Cdd:cd03265 1 IEVENLVKKY----GDFEAV-RGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREV---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPS 161
Cdd:cd03265 72 RRRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1319887251 162 VLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDL 229
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
37-236 |
1.71e-46 |
|
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: 160.35 E-value: 1.71e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 37 VVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEalrreRRAIGTVFQSSALLSRRTAWENVALPLAWLGVVER 116
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH-----LRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 117 DIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIV 196
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1319887251 197 LITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSL 236
Cdd:TIGR01187 156 FVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANL 195
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-224 |
2.36e-46 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 161.27 E-value: 2.36e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYrtaDGRlsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEalrre 81
Cdd:PRK09452 15 VELRGISKSF---DGK--EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE----- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPS 161
Cdd:PRK09452 85 NRHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1319887251 162 VLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYG 224
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDG 227
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
1-230 |
3.92e-46 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 157.66 E-value: 3.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRT-----ADGRLsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSG 75
Cdd:TIGR02769 2 LLEVRDVTHTYRTgglfgAKQRA-PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 76 EALRRERRAIGTVFQS--SALLSRRTAWENVALPLAWL-GVVERDIKARVGELLESVGL-SHKADAWPAQLSGGQRQRIG 151
Cdd:TIGR02769 81 KQRRAFRRDVQLVFQDspSAVNPRMTVRQIIGEPLRHLtSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1319887251 152 IARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLL 230
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLL 239
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-170 |
7.14e-46 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 153.19 E-value: 7.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRErraIGTVFQSSALLSRRTAW 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKE---IGYVFQDPQLFPRLTVR 77
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1319887251 102 ENVALPLAWLGVVERDIKARVGELLESVGLSHKAD----AWPAQLSGGQRQRIGIARALALRPSVLLADEATS 170
Cdd:pfam00005 78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-249 |
7.50e-45 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 154.46 E-value: 7.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTAD----GRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGE 76
Cdd:PRK10419 3 LLNVSGLSHHYAHGGlsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 77 ALRRERRAIGTVFQSS--ALLSRRTAWENVALPLAWL-GVVERDIKARVGELLESVGLSHK-ADAWPAQLSGGQRQRIGI 152
Cdd:PRK10419 83 QRKAFRRDIQMVFQDSisAVNPRKTVREIIREPLRHLlSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 153 ARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLaR 232
Cdd:PRK10419 163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKL-T 241
|
250 260
....*....|....*....|.
gi 1319887251 233 PDSLLGQQL----LPLTPAAA 249
Cdd:PRK10419 242 FSSPAGRVLqnavLPAFPVRR 262
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
6-249 |
3.77e-44 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 160.27 E-value: 3.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 6 DLYKSYRTADGRLsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRERRA- 84
Cdd:PRK10535 9 DIRRSYPSGEEQV-EVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLRREh 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 85 IGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLL 164
Cdd:PRK10535 88 FGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVIL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 165 ADEATSGLDPQATASVLALLKRLRDEYQLAIVlITHEmDAVRTAADAVAEIRDGTIVQygrieDLLARPDSLLGQQLLPL 244
Cdd:PRK10535 168 ADEPTGALDSHSGEEVMAILHQLRDRGHTVII-VTHD-PQVAAQAERVIEIRDGEIVR-----NPPAQEKVNVAGGTEPV 240
|
....*
gi 1319887251 245 TPAAA 249
Cdd:PRK10535 241 VNTAS 245
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-241 |
1.29e-43 |
|
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: 159.61 E-value: 1.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYrtaDGRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALrre 81
Cdd:COG2274 474 IELENVSFRY---PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL--- 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQSSALLSrRTAWENVAlplawLGVVERDIkARVGELLESVGLSHKADAWP-----------AQLSGGQRQRI 150
Cdd:COG2274 548 RRQIGVVLQDVFLFS-GTIRENIT-----LGDPDATD-EEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRL 620
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 151 GIARALALRPSVLLADEATSGLDPQATASVLALLKRLRdeYQLAIVLITHEMDAVRtAADAVAEIRDGTIVQYGRIEDLL 230
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRLL--KGRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEELL 697
|
250
....*....|....
gi 1319887251 231 ARPD---SLLGQQL 241
Cdd:COG2274 698 ARKGlyaELVQQQL 711
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-224 |
1.87e-43 |
|
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: 149.06 E-value: 1.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTADGRLSAVlKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRR 80
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAV-DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 erraIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:cd03266 80 ----LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1319887251 161 SVLLADEATSGLDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYG 224
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
25-224 |
2.31e-43 |
|
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: 148.98 E-value: 2.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 25 LSLQVPErSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDL-SALSGEALRRERRAIGTVFQSSALLSRRTAWEN 103
Cdd:cd03297 17 IDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfDSRKKINLPPQQRKIGLVFQQYALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 104 VALPLAwlGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLAL 183
Cdd:cd03297 96 LAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1319887251 184 LKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYG 224
Cdd:cd03297 174 LKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
22-245 |
2.08e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 148.63 E-value: 2.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSA-LSGEALRRERRAIGTVFQ-SSALLSRRT 99
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgKKNKKLKPLRKKVGIVFQfPEHQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 100 AWENVALPLAWLGVVERDIKARVGELLESVGLSHKA-DAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATA 178
Cdd:PRK13634 103 VEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELlARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRK 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1319887251 179 SVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSLLGQQL-LPLT 245
Cdd:PRK13634 183 EMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPDELEAIGLdLPET 250
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
21-219 |
5.42e-42 |
|
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: 143.15 E-value: 5.42e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRErraIGTVFQssallsrrta 100
Cdd:cd00267 14 ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRR---IGYVPQ---------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 wenvalplawlgvverdikarvgellesvglshkadawpaqLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASV 180
Cdd:cd00267 81 -----------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERL 119
|
170 180 190
....*....|....*....|....*....|....*....
gi 1319887251 181 LALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGT 219
Cdd:cd00267 120 LELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-243 |
6.07e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 147.15 E-value: 6.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYrtADGrlSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSaLSGEALRR 80
Cdd:PRK13639 1 ILETRDLKYSY--PDG--TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRAIGTVFQSS-ALLSRRTAWENVAL-PLAwLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALAL 158
Cdd:PRK13639 76 VRKTVGIVFQNPdDQLFAPTVEEDVAFgPLN-LGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 159 RPSVLLADEATSGLDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSLLG 238
Cdd:PRK13639 155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIRK 233
|
....*.
gi 1319887251 239 QQL-LP 243
Cdd:PRK13639 234 ANLrLP 239
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
21-224 |
1.08e-41 |
|
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: 143.34 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgealRRER-RAIGTVFQSsallsrrt 99
Cdd:cd03214 14 VLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS----PKELaRKIAYVPQA-------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 100 awenvalplawlgvverdikarvgelLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATAS 179
Cdd:cd03214 82 --------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIE 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1319887251 180 VLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYG 224
Cdd:cd03214 136 LLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-233 |
1.10e-41 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 145.44 E-value: 1.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLL-----EQPDSGSIRINGQDLSALSGEALRRErraIGTVFQSSALL 95
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIELRRR---VQMVFQIPNPI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 96 SRRTAWENVALPLAWLGVV--ERDIKARVGELLESVGL----SHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEAT 169
Cdd:PRK14247 95 PNLSIFENVALGLKLNRLVksKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1319887251 170 SGLDPQATASVLALLKRLRDEyqLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARP 233
Cdd:PRK14247 175 ANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNP 236
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-246 |
2.90e-41 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 145.33 E-value: 2.90e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTAdgrlSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSAlsgEALRR 80
Cdd:PRK13652 3 LIETRDLCYSYSGS----KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK---ENIRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRAIGTVFQSSA-LLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALR 159
Cdd:PRK13652 76 VRKFVGLVFQNPDdQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 160 PSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSLLGQ 239
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLARV 235
|
....*...
gi 1319887251 240 QL-LPLTP 246
Cdd:PRK13652 236 HLdLPSLP 243
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
22-237 |
9.61e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 144.10 E-value: 9.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSAlsgEALRRERRAIGTVFQS-SALLSRRTA 100
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE---ENVWDIRHKIGMVFQNpDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 WENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASV 180
Cdd:PRK13650 100 EDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLEL 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1319887251 181 LALLKRLRDEYQLAIVLITHEMDAVrTAADAVAEIRDGTIVQYGRIEDLLARPDSLL 237
Cdd:PRK13650 180 IKTIKGIRDDYQMTVISITHDLDEV-ALSDRVLVMKNGQVESTSTPRELFSRGNDLL 235
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
21-232 |
1.69e-40 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 149.54 E-value: 1.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRerrAIGTVFQSSALLSRrTA 100
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRR---QIGVVPQDTFLFSG-TI 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 WENVALplawlGVVERDiKARVGELLESVGLSHKADAWP-----------AQLSGGQRQRIGIARALALRPSVLLADEAT 169
Cdd:COG1132 431 RENIRY-----GRPDAT-DEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILILDEAT 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1319887251 170 SGLDPQATASVLALLKRLRDEYqlAIVLITHEMDAVRtAADAVAEIRDGTIVQYGRIEDLLAR 232
Cdd:COG1132 505 SALDTETEALIQEALERLMKGR--TTIVIAHRLSTIR-NADRILVLDDGRIVEQGTHEELLAR 564
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
19-236 |
2.33e-40 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 144.86 E-value: 2.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 19 SAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgealrRERRAIGTVFQSSALLSRR 98
Cdd:PRK11432 19 NTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS-----IQQRDICMVFQSYALFPHM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 99 TAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATA 178
Cdd:PRK11432 94 SLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRR 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1319887251 179 SVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSL 236
Cdd:PRK11432 174 SMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASR 231
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-237 |
3.23e-40 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 142.46 E-value: 3.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRTADgrlSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQdlsALSGEALRRE 81
Cdd:PRK13635 6 IRVEHISFRYPDAA---TYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQS-SALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:PRK13635 80 RRQVGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1319887251 161 SVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVrTAADAVAEIRDGTIVQYGRIEDLLARPDSLL 237
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEIFKSGHMLQ 235
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-203 |
9.01e-40 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 140.77 E-value: 9.01e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYrTADGRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQdlsALSGEALRR 80
Cdd:COG4525 3 MLTVRHVSVRY-PGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGV---PVTGPGADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 erraiGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:COG4525 79 -----GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1319887251 161 SVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMD 203
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVE 196
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-224 |
9.19e-40 |
|
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: 139.25 E-value: 9.19e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRtaDGRlsaVLKGLSLQVPErSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEAlrre 81
Cdd:cd03264 1 LQLENLTKRYG--KKR---ALDGVSLTLGP-GMYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKL---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQSSALLSRRTAWENVALpLAWL-GVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:cd03264 71 RRRIGYLPQEFGVYPNFTVREFLDY-IAWLkGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1319887251 161 SVLLADEATSGLDPQATASVLALLKRLRDEyqlAIVLI-THEMDAVRTAADAVAEIRDGTIVQYG 224
Cdd:cd03264 150 SILIVDEPTAGLDPEERIRFRNLLSELGED---RIVILsTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
22-237 |
1.51e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 140.66 E-value: 1.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQdlsALSGEALRRERRAIGTVFQSSallsrrtaw 101
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQ---AITDDNFEKLRKHIGIVFQNP--------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 102 EN----------VALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSG 171
Cdd:PRK13648 93 DNqfvgsivkydVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1319887251 172 LDPQATASVLALLKRLRDEYQLAIVLITHEMDAVrTAADAVAEIRDGTIVQYGRIEDLLARPDSLL 237
Cdd:PRK13648 173 LDPDARQNLLDLVRKVKSEHNITIISITHDLSEA-MEADHVIVMNKGTVYKEGTPTEIFDHAEELT 237
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
11-241 |
2.18e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 140.37 E-value: 2.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 11 YRTADGrlSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSaLSGEALRRERRAIGTVFQ 90
Cdd:PRK13636 13 YNYSDG--THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMKLRESVGMVFQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 91 S--SALLSRrTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEA 168
Cdd:PRK13636 90 DpdNQLFSA-SVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEP 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1319887251 169 TSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSLLGQQL 241
Cdd:PRK13636 169 TAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRKVNL 241
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-221 |
3.80e-39 |
|
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: 137.73 E-value: 3.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRTADgrlsaVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgEALRRe 81
Cdd:cd03268 1 LKTNDLTKTYGKKR-----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI-EALRR- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 rraIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKarvgELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPS 161
Cdd:cd03268 74 ---IGALIEAPGFYPNLTARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 162 VLLADEATSGLDPQATASVLALLKRLRDeYQLAIVLITHEMDAVRTAADAVAEIRDGTIV 221
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRD-QGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
5-222 |
3.83e-39 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 138.41 E-value: 3.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 5 DDLYKSYRtaDGRLSA-VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRER- 82
Cdd:PRK11629 9 DNLCKRYQ--EGSVQTdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRn 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 83 RAIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSV 162
Cdd:PRK11629 87 QKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 163 LLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVaEIRDGTIVQ 222
Cdd:PRK11629 167 VLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQL-EMRDGRLTA 225
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-242 |
4.94e-39 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 138.82 E-value: 4.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCIS-LLEQPDS----GSIRINGQDLSALSGEALRrERRAIGTVFQSSALL 95
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNrLLELNEEarveGEVRLFGRNIYSPDVDPIE-VRREVGMVFQYPNPF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 96 SRRTAWENVALPLAWLGVV--ERDIKARVGELLESVGL----SHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEAT 169
Cdd:PRK14267 98 PHLTIYDNVAIGVKLNGLVksKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPT 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1319887251 170 SGLDPQATASVLALLKRLRDEYqlAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSLLGQQLL 242
Cdd:PRK14267 178 ANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
25-234 |
8.78e-39 |
|
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: 140.63 E-value: 8.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 25 LSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDL-SALSGEALRRERRAIGTVFQSSALLSRRTAWEN 103
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 104 VALPLAWLGVVERDIK-ARVGELLesvGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLA 182
Cdd:TIGR02142 96 LRYGMKRARPSERRISfERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1319887251 183 LLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPD 234
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPD 224
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-224 |
9.13e-39 |
|
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: 136.87 E-value: 9.13e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 4 IDDLYKSYRTadgRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRerr 83
Cdd:cd03263 3 IRNLTKTYKK---GTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQS--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 84 aIGTVFQSSALLSRRTAWENVALpLAWL-GVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSV 162
Cdd:cd03263 77 -LGYCPQFDALFDELTVREHLRF-YARLkGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1319887251 163 LLADEATSGLDPQATASVLALLKRLRDeyQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYG 224
Cdd:cd03263 155 LLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
19-229 |
9.36e-39 |
|
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: 137.27 E-value: 9.36e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 19 SAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEalRRERRAIGTVFQSSALLSRR 98
Cdd:TIGR03410 13 SHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPH--ERARAGIAYVPQGREIFPRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 99 TAWENVALPLAWLGVVERDIKARVGEL---LESVgLSHKAdawpAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQ 175
Cdd:TIGR03410 91 TVEENLLTGLAALPRRSRKIPDEIYELfpvLKEM-LGRRG----GDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQPS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1319887251 176 ATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDL 229
Cdd:TIGR03410 166 IIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
22-236 |
1.04e-38 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 139.03 E-value: 1.04e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSAlSGEALRRERRAIGTVFQSSAL-LSRRTA 100
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDIRKKVGLVFQYPEYqLFEETI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 WENVALPLAWLGVVERDIKARVGELLESVGLSHK--ADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATA 178
Cdd:PRK13637 102 EKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEdyKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1319887251 179 SVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSL 236
Cdd:PRK13637 182 EILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETL 239
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-202 |
1.38e-38 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 136.54 E-value: 1.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYrtADGRlsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRR 80
Cdd:PRK10908 1 MIRFEHVSKAY--LGGR--QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRAIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:PRK10908 77 LRRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1319887251 161 SVLLADEATSGLDPQATASVLALLKRLrDEYQLAIVLITHEM 202
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEF-NRVGVTVLMATHDI 197
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-233 |
4.96e-38 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 139.78 E-value: 4.96e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 18 LSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRERRA-IGTVFQSSALLS 96
Cdd:PRK10070 40 LSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQSFALMP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 97 RRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQA 176
Cdd:PRK10070 120 HMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1319887251 177 TASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARP 233
Cdd:PRK10070 200 RTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNP 256
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
4-242 |
5.18e-38 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 136.51 E-value: 5.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 4 IDDLYKSYRTADGRLSA----VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSalSGEALR 79
Cdd:COG4167 7 VRNLSKTFKYRTGLFRRqqfeAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLE--YGDYKY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 80 RERRaIGTVFQ--SSALLSRRTAWENVALPLAW---LGVVERdiKARVGELLESVGLS--HkADAWPAQLSGGQRQRIGI 152
Cdd:COG4167 85 RCKH-IRMIFQdpNTSLNPRLNIGQILEEPLRLntdLTAEER--EERIFATLRLVGLLpeH-ANFYPHMLSSGQKQRVAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 153 ARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLAR 232
Cdd:COG4167 161 ARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFAN 240
|
250
....*....|
gi 1319887251 233 PDSLLGQQLL 242
Cdd:COG4167 241 PQHEVTKRLI 250
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-235 |
5.78e-38 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 139.20 E-value: 5.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYrtaDGRlsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgealrR 80
Cdd:PRK11607 19 LLEIRNLTKSF---DGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVP-----P 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRAIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:PRK11607 89 YQRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 161 SVLLADEATSGLDpqatasvlallKRLRDEYQLAI-----------VLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDL 229
Cdd:PRK11607 169 KLLLLDEPMGALD-----------KKLRDRMQLEVvdilervgvtcVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
....*.
gi 1319887251 230 LARPDS 235
Cdd:PRK11607 238 YEHPTT 243
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
22-221 |
1.06e-37 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 140.55 E-value: 1.06e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALS-GEALRRerrAIGTVFQSSALLSRRTA 100
Cdd:COG3845 21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSpRDAIAL---GIGMVHQHFMLVPNLTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 WENVAL---PLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQAT 177
Cdd:COG3845 98 AENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1319887251 178 ASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTIV 221
Cdd:COG3845 178 DELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
21-229 |
2.70e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 139.38 E-value: 2.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALS-GEAlrrERRAIGTVFQSSALLSRRT 99
Cdd:COG1129 19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRDA---QAAGIAIIHQELNLVPNLS 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 100 AWENVAL--PLAWLGVV-ERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQA 176
Cdd:COG1129 96 VAENIFLgrEPRRGGLIdWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLTERE 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1319887251 177 TASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDL 229
Cdd:COG1129 176 VERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-232 |
2.84e-37 |
|
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: 140.28 E-value: 2.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLykSYRTADGRlsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALrre 81
Cdd:COG4988 337 IELEDV--SFSYPGGR--PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW--- 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQSSALLSRRTAwENVAlplawLGVVERDiKARVGELLESVGLSHKADAWP-----------AQLSGGQRQRI 150
Cdd:COG4988 410 RRQIAWVPQNPYLFAGTIR-ENLR-----LGRPDAS-DEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 151 GIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEyqLAIVLITHEMDAVRtAADAVAEIRDGTIVQYGRIEDLL 230
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKG--RTVILITHRLALLA-QADRILVLDDGRIVEQGTHEELL 559
|
..
gi 1319887251 231 AR 232
Cdd:COG4988 560 AK 561
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
19-231 |
3.83e-37 |
|
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: 132.94 E-value: 3.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 19 SAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEalRRERRAIGTVFQSSALLSRR 98
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPH--ERARAGIGYVPEGRRIFPEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 99 TAWENvaLPLAWLGVVERDIKARVGELLESVG-----LSHKAdawpAQLSGGQRQRIGIARALALRPSVLLADEATSGLD 173
Cdd:cd03224 91 TVEEN--LLLGAYARRRAKRKARLERVYELFPrlkerRKQLA----GTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1319887251 174 PQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLA 231
Cdd:cd03224 165 PKIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-240 |
1.09e-36 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 132.86 E-value: 1.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 20 AVLKGLSLQVPERSITAVVGPSGAGKSTLARCIS-LLEQPDS-----GSIRINGQDLSALSGEALRRErraIGTVFQSSA 93
Cdd:PRK14246 24 AILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNrLIEIYDSkikvdGKVLYFGKDIFQIDAIKLRKE---VGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 94 LLSRRTAWENVALPLAWLGVVE-RDIKARVGELLESVGL----SHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEA 168
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKSHGIKEkREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1319887251 169 TSGLDPQATASVLALLKRLRDEyqLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSLLGQQ 240
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-234 |
1.80e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 132.55 E-value: 1.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRtaDGrlSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSAlsgEALRRE 81
Cdd:PRK13647 5 IEVEDLHFRYK--DG--TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA---ENEKWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQS--SALLSRrTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALR 159
Cdd:PRK13647 78 RSKVGLVFQDpdDQVFSS-TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1319887251 160 PSVLLADEATSGLDPQATASVLALLKRLRDEYQlAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEdLLARPD 234
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS-LLTDED 229
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-221 |
3.65e-36 |
|
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: 128.32 E-value: 3.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRTAdgrlsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALS-GEALRR 80
Cdd:cd03216 1 LELRGITKRFGGV-----KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 errAIGTVFQssallsrrtawenvalplawlgvverdikarvgellesvglshkadawpaqLSGGQRQRIGIARALALRP 160
Cdd:cd03216 76 ---GIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNA 101
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1319887251 161 SVLLADEATSGLDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTIV 221
Cdd:cd03216 102 RLLILDEPTAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
21-232 |
4.53e-36 |
|
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: 130.35 E-value: 4.53e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTlarCISLLEQ---PDSGSIRINGQDLSALsgeALRRERRAIGTVFQSSALLSR 97
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLERfydPTSGEILLDGVDIRDL---NLRWLRSQIGLVSQEPVLFDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 98 rTAWENVALPLAWLGVVERDIKARVGELLESV-GLSHKAD----AWPAQLSGGQRQRIGIARALALRPSVLLADEATSGL 172
Cdd:cd03249 92 -TIAENIRYGKPDATDEEVEEAAKKANIHDFImSLPDGYDtlvgERGSQLSGGQKQRIAIARALLRNPKILLLDEATSAL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 173 DPQATASVLALLKRLRDEYqlAIVLITHEMDAVRtAADAVAEIRDGTIVQYGRIEDLLAR 232
Cdd:cd03249 171 DAESEKLVQEALDRAMKGR--TTIVIAHRLSTIR-NADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
25-255 |
5.08e-36 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 131.43 E-value: 5.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 25 LSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRERRAIGTVFQSSALLSRRTAWENV 104
Cdd:PRK11831 26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFDNV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 105 ALPL-AWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLAL 183
Cdd:PRK11831 106 AYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLVKL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 184 LKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSLLGQQL-------LPLT-PAAATHSDLL 255
Cdd:PRK11831 186 ISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRVRQFLdgiadgpVPFRyPAGDYHADLL 265
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-230 |
5.36e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 131.27 E-value: 5.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTADgrlSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSAlsgEALRR 80
Cdd:PRK13632 7 MIKVENVSFSYPNSE---NNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK---ENLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRAIGTVFQS------SAllsrrTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIAR 154
Cdd:PRK13632 81 IRKKIGIIFQNpdnqfiGA-----TVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIAS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1319887251 155 ALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVrTAADAVAEIRDGTIVQYGRIEDLL 230
Cdd:PRK13632 156 VLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEIL 230
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-201 |
5.91e-36 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 129.14 E-value: 5.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYrtaDGRLsaVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEAlrr 80
Cdd:COG4133 2 MLEAENLSCRR---GERL--LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDY--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 eRRAIGTVFQSSALLSRRTAWENVALPLAWLGVVERDikARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:COG4133 74 -RRRLAYLGHADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1319887251 161 SVLLADEATSGLDPQATASVLALLKRLRDEyQLAIVLITHE 201
Cdd:COG4133 151 PLWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQ 190
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-234 |
1.76e-35 |
|
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: 128.81 E-value: 1.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRTadgrlSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALsgEALRRE 81
Cdd:cd03218 1 LRAENLSKRYGK-----RKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL--PMHKRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPS 161
Cdd:cd03218 74 RLGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1319887251 162 VLLADEATSGLDPQATASVLALLKRLRDeyqLAI-VLIT-HEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPD 234
Cdd:cd03218 154 FLLLDEPFAGVDPIAVQDIQKIIKILKD---RGIgVLITdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
4-233 |
1.92e-35 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 131.37 E-value: 1.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 4 IDDLYKSYRTADGR---------LSAVlKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALS 74
Cdd:PRK15079 11 VADLKVHFDIKDGKqwfwqppktLKAV-DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 75 GEALRRERRAIGTVFQS--SALLSRRTAWENVALPLA--WLGVVERDIKARVGELLESVGL-SHKADAWPAQLSGGQRQR 149
Cdd:PRK15079 90 DDEWRAVRSDIQMIFQDplASLNPRMTIGEIIAEPLRtyHPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 150 IGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDL 229
Cdd:PRK15079 170 IGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
....
gi 1319887251 230 LARP 233
Cdd:PRK15079 250 YHNP 253
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-233 |
4.18e-35 |
|
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: 134.51 E-value: 4.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYrtaDGRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALrre 81
Cdd:COG4987 334 LELEDVSFRY---PGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL--- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQSSALLSrRTAWENvaLPLAWLGVVERDIKArvgeLLESVGLSHKADAWP-----------AQLSGGQRQRI 150
Cdd:COG4987 408 RRRIAVVPQRPHLFD-TTLREN--LRLARPDATDEELWA----ALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 151 GIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYqlAIVLITHEMDAVRtAADAVAEIRDGTIVQYGRIEDLL 230
Cdd:COG4987 481 ALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLE-RMDRILVLEDGRIVEQGTHEELL 557
|
...
gi 1319887251 231 ARP 233
Cdd:COG4987 558 AQN 560
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
2-224 |
5.41e-35 |
|
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: 126.84 E-value: 5.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRTADGRLSavlkglsLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgealrRE 81
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFD-------LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP-----PA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQSSALLSRRTAWENVALPLA-WLGVVERDiKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:cd03298 69 DRPVSMLFQENNLFAHLTVEQNVGLGLSpGLKLTAED-RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDK 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1319887251 161 SVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYG 224
Cdd:cd03298 148 PVLLLDEPFAALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-232 |
1.37e-34 |
|
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: 126.58 E-value: 1.37e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYrtADGRLsaVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALrre 81
Cdd:cd03253 1 IEFENVTFAY--DPGRP--VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSL--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQSSALLSrRTAWENVAlpLAWLGVVERDI-----KARVGELLESV--GLSHKADAWPAQLSGGQRQRIGIAR 154
Cdd:cd03253 74 RRAIGVVPQDTVLFN-DTIGYNIR--YGRPDATDEEVieaakAAQIHDKIMRFpdGYDTIVGERGLKLSGGEKQRVAIAR 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1319887251 155 ALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLaiVLITHEMDAVrTAADAVAEIRDGTIVQYGRIEDLLAR 232
Cdd:cd03253 151 AILKNPPILLLDEATSALDTHTEREIQAALRDVSKGRTT--IVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELLAK 225
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-234 |
2.93e-34 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 125.53 E-value: 2.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRtadGRlsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgeALRR 80
Cdd:COG1137 3 TLEAENLVKSYG---KR--TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP--MHKR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRAIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:COG1137 76 ARLGIGYLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1319887251 161 SVLLADEATSGLDPQATASVLALLKRLRDEyqlAI-VLIT-HemdAVR-TAA--DAVAEIRDGTIVQYGRIEDLLARPD 234
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRHLKER---GIgVLITdH---NVReTLGicDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-234 |
2.94e-34 |
|
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: 125.48 E-value: 2.94e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYrtadGRlSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEalRR 80
Cdd:COG0410 3 MLEVENLHAGY----GG-IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPH--RI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRAIGTVFQSSALLSRRTAWENVAlplawLGVVERDIKARVGELLESVG-----LSHKADAWPAQLSGGQRQRIGIARA 155
Cdd:COG0410 76 ARLGIGYVPEGRRIFPSLTVEENLL-----LGAYARRDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1319887251 156 LALRPSVLLADEATSGLDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPD 234
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-224 |
3.01e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 126.74 E-value: 3.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDL-YKSYRTADGRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALsgEALR 79
Cdd:PRK13633 4 MIKCKNVsYKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDE--ENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 80 RERRAIGTVFQS-SALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALAL 158
Cdd:PRK13633 82 DIRNKAGMVFQNpDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1319887251 159 RPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVrTAADAVAEIRDGTIVQYG 224
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEG 226
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-233 |
3.18e-34 |
|
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: 125.27 E-value: 3.18e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALrrerraigTVFQSSALLSRRTAW 101
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM--------VVFQNYSLLPWLTVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 102 ENVALP----LAWLGVVERdiKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQAT 177
Cdd:TIGR01184 73 ENIALAvdrvLPDLSKSER--RAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1319887251 178 ASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDL-LARP 233
Cdd:TIGR01184 151 GNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRP 207
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-201 |
3.31e-34 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 125.28 E-value: 3.31e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTADGRLSaVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEAlRR 80
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHELS-ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEA-RA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRA--IGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALAL 158
Cdd:PRK10584 84 KLRAkhVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNG 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1319887251 159 RPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHE 201
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
20-236 |
6.19e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 126.07 E-value: 6.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 20 AVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGS---IRINGQDLSAlsgEALRRERRAIGTVFQS-SALL 95
Cdd:PRK13640 21 PALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTA---KTVWDIREKVGIVFQNpDNQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 96 SRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQ 175
Cdd:PRK13640 98 VGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1319887251 176 ATASVLALLKRLRDEYQLAIVLITHEMDAVrTAADAVAEIRDGTIVQYGRIEDLLARPDSL 236
Cdd:PRK13640 178 GKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEML 237
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-221 |
6.32e-34 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 123.91 E-value: 6.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 4 IDDLYKSYrtadGRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSAlsgealRRERR 83
Cdd:cd03226 2 IENISFSY----KKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA------KERRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 84 AIGTVFQSSAL-LSRRTAWENVALPLAWLGvverDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSV 162
Cdd:cd03226 72 SIGYVMQDVDYqLFTDSVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1319887251 163 LLADEATSGLDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTIV 221
Cdd:cd03226 148 LIFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-232 |
6.73e-34 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 126.38 E-value: 6.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSY--RTAdgrlsavLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSalsgeal 78
Cdd:COG4152 1 MLELKGLTKRFgdKTA-------VDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 79 RRERRAIGTVFQSSALLSRRTAWEnVALPLAWL-GVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALA 157
Cdd:COG4152 67 PEDRRRIGYLPEERGLYPKMKVGE-QLVYLARLkGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1319887251 158 LRPSVLLADEATSGLDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLAR 232
Cdd:COG4152 146 HDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-230 |
7.90e-34 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 125.23 E-value: 7.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLykSYRTADGRLsavLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRR 80
Cdd:COG4559 1 MLEAENL--SVRLGGRTL---LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 eRRAIgtVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALA--- 157
Cdd:COG4559 76 -RRAV--LPQHSSLAFPFTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlw 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1319887251 158 ----LRPSVLLADEATSGLDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLL 230
Cdd:COG4559 153 epvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVL 228
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-236 |
1.15e-33 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 124.43 E-value: 1.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTAdgrlsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRR 80
Cdd:COG4604 1 MIEIKNVSKRYGGK-----VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 eRRAIGTvfQSSALLSRRTAWENVAL---PLAwLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALA 157
Cdd:COG4604 76 -RLAILR--QENHINSRLTVRELVAFgrfPYS-KGRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1319887251 158 LRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLaRPDSL 236
Cdd:COG4604 152 QDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEII-TPEVL 229
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-255 |
1.20e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 125.62 E-value: 1.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTADGRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEA-LR 79
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 80 RERRAIGTVFQ-SSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKA-DAWPAQLSGGQRQRIGIARALA 157
Cdd:PRK13643 81 PVRKKVGVVFQfPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 158 LRPSVLLADEATSGLDPQATASVLALLKRLRDEYQlAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSLL 237
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLK 239
|
250
....*....|....*...
gi 1319887251 238 GQQLlpLTPAAATHSDLL 255
Cdd:PRK13643 240 AHEL--GVPKATHFADQL 255
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-233 |
2.39e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 123.99 E-value: 2.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRTadgrlSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDS-----GSIRINGQDLSALSGE 76
Cdd:PRK14258 8 IKVNNLSFYYDT-----QKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIYERRVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 77 aLRRERRAIGTVFQSSALLSRrTAWENVALPLAWLG---------VVERDIKArvGELLESVglSHKADAWPAQLSGGQR 147
Cdd:PRK14258 83 -LNRLRRQVSMVHPKPNLFPM-SVYDNVAYGVKIVGwrpkleiddIVESALKD--ADLWDEI--KHKIHKSALDLSGGQQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 148 QRIGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVA-----EIRDGTIVQ 222
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAffkgnENRIGQLVE 236
|
250
....*....|.
gi 1319887251 223 YGRIEDLLARP 233
Cdd:PRK14258 237 FGLTKKIFNSP 247
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-219 |
2.83e-33 |
|
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: 122.93 E-value: 2.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYR--TADGRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQD-----LSAL 73
Cdd:COG4778 4 LLEVENLSKTFTlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdlAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 74 SGEALRRERRAIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGL-SHKADAWPAQLSGGQRQRIGI 152
Cdd:COG4778 84 PREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQQRVNI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1319887251 153 ARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGT 219
Cdd:COG4778 164 ARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
1-231 |
3.93e-33 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 122.38 E-value: 3.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTADGRLSavlkgLSLQVPERsiTAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgealrR 80
Cdd:PRK10771 1 MLKLTDITWLYHHLPMRFD-----LTVERGER--VAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP-----P 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRAIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:PRK10771 69 SRRPVSMLFQENNLFSHLTVAQNIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1319887251 161 SVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEM-DAVRTAADAVAeIRDGTIVQYGRIEDLLA 231
Cdd:PRK10771 149 PILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLeDAARIAPRSLV-VADGRIAWDGPTDELLS 219
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
22-241 |
4.90e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 123.70 E-value: 4.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALS-GEALRRERRAIGTVFQ-SSALLSRRT 99
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSkNKDIKQIRKKVGLVFQfPESQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 100 AWENVALPLAWLGVVERDIKARVGELLESVGLSHKA-DAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATA 178
Cdd:PRK13649 103 VLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRK 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1319887251 179 SVLALLKRLRdEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSLLGQQL 241
Cdd:PRK13649 183 ELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDVDFLEEKQL 244
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
21-245 |
4.99e-33 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 128.28 E-value: 4.99e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKST----LARCIslleqPDSGSIRINGQDLSALSGEALRRERRAIGTVFQ--SSAL 94
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQdpNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 95 LSRRTAWENVALPLA----WLGVVERDikARVGELLESVGLS----HKadaWPAQLSGGQRQRIGIARALALRPSVLLAD 166
Cdd:PRK15134 376 NPRLNVLQIIEEGLRvhqpTLSAAQRE--QQVIAVMEEVGLDpetrHR---YPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1319887251 167 EATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSLLGQQLLPLT 245
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLALS 529
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
2-233 |
1.46e-32 |
|
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: 127.77 E-value: 1.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRtADGRLsaVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRE 81
Cdd:TIGR03797 452 IEVDRVTFRYR-PDGPL--ILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAVRRQ 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 rraIGTVFQSSALLSRrTAWENVA------LPLAWlgvverdikarvgELLESVGLSHKADAWP-----------AQLSG 144
Cdd:TIGR03797 529 ---LGVVLQNGRLMSG-SIFENIAggapltLDEAW-------------EAARMAGLAEDIRAMPmgmhtviseggGTLSG 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 145 GQRQRIGIARALALRPSVLLADEATSGLDPQATASVLALLKRLrdeyQLAIVLITHEMDAVRTaADAVAEIRDGTIVQYG 224
Cdd:TIGR03797 592 GQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL----KVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQG 666
|
....*....
gi 1319887251 225 RIEDLLARP 233
Cdd:TIGR03797 667 TYDELMARE 675
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-224 |
1.87e-32 |
|
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: 120.08 E-value: 1.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRTAdgrlsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgealrre 81
Cdd:cd03269 1 LEVENVTKRFGRV-----TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQSSALLSRRTAWEnVALPLAWL-GVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:cd03269 69 RNRIGYLPEERGLYPKMKVID-QLVYLAQLkGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDP 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1319887251 161 SVLLADEATSGLDPQATASVLALLKRLRDEYQlAIVLITHEMDAVRTAADAVAEIRDGTIVQYG 224
Cdd:cd03269 148 ELLILDEPFSGLDPVNVELLKDVIRELARAGK-TVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
21-232 |
3.07e-32 |
|
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: 120.02 E-value: 3.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRErraIGTVFQSSALLSrRTA 100
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSM---IGVVLQDTFLFS-GTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 WENVAL--PLAWLGVVERDIK-ARVGELLESV--GLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQ 175
Cdd:cd03254 94 MENIRLgrPNATDEEVIEAAKeAGAHDFIMKLpnGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTE 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1319887251 176 ATASVLALLKRLRdEYQLAIVlITHEMDAVRTaADAVAEIRDGTIVQYGRIEDLLAR 232
Cdd:cd03254 174 TEKLIQEALEKLM-KGRTSII-IAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLAK 227
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-206 |
7.62e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 119.81 E-value: 7.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTADGRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgealrR 80
Cdd:COG1101 1 MLELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP-----E 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRA--IGTVFQ------SSALlsrrTAWENVAL--------PLAWlGVVERDiKARVGELLESV--GLSHKADAWPAQL 142
Cdd:COG1101 76 YKRAkyIGRVFQdpmmgtAPSM----TIEENLALayrrgkrrGLRR-GLTKKR-RELFRELLATLglGLENRLDTKVGLL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1319887251 143 SGGQRQrigiarALAL------RPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEM-DAVR 206
Cdd:COG1101 150 SGGQRQ------ALSLlmatltKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMeQALD 214
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
22-234 |
9.67e-32 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 119.89 E-value: 9.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQ-----PDSGSIRINGQDLSALSGEALRRERRaIGTVFQSSALLS 96
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYAPDVDPVEVRRR-IGMVFQKPNPFP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 97 RrTAWENVALPLAWLG-------VVERDIKA-----RVGELLESVGLShkadawpaqLSGGQRQRIGIARALALRPSVLL 164
Cdd:PRK14243 105 K-SIYDNIAYGARINGykgdmdeLVERSLRQaalwdEVKDKLKQSGLS---------LSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1319887251 165 ADEATSGLDPQATASVLALLKRLRDEYqlAIVLITHEMDAVRTAADAVA---------EIRDGTIVQYGRIEDLLARPD 234
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAffnveltegGGRYGYLVEFDRTEKIFNSPQ 251
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
21-230 |
1.42e-31 |
|
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: 119.03 E-value: 1.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSG-SIRINGQDLSalsGEALRRERRAIGTVfqSSALLSRRT 99
Cdd:COG1119 18 ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRG---GEDVWELRKRIGLV--SPALQLRFP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 100 AWENValplawLGVV--------------ERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLA 165
Cdd:COG1119 93 RDETV------LDVVlsgffdsiglyrepTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLIL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1319887251 166 DEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLL 230
Cdd:COG1119 167 DEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
22-209 |
1.53e-31 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 117.58 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPD---SGSIRINGQDLSALSGEalrreRRAIGTVFQSSALLSRR 98
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAE-----QRRIGILFQDDLLFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 99 TAWENVALPL-AWLGVVERdiKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQAT 177
Cdd:COG4136 92 SVGENLAFALpPTIGRAQR--RARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALR 169
|
170 180 190
....*....|....*....|....*....|...
gi 1319887251 178 ASVLAL-LKRLRDEyQLAIVLITHEMDAVRTAA 209
Cdd:COG4136 170 AQFREFvFEQIRQR-GIPALLVTHDEEDAPAAG 201
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-232 |
2.11e-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: 117.97 E-value: 2.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRtADGRLsaVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRE 81
Cdd:cd03252 1 ITFEHVRFRYK-PDGPV--ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 rraIGTVFQSSALLSRRTAwENVALPLAWLGVVERDIKARVGELLESV-----GLSHKADAWPAQLSGGQRQRIGIARAL 156
Cdd:cd03252 78 ---VGVVLQENVLFNRSIR-DNIALADPGMSMERVIEAAKLAGAHDFIselpeGYDTIVGEQGAGLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1319887251 157 ALRPSVLLADEATSGLDPQATASVLALLKRLRDEYqlAIVLITHEMDAVRTaADAVAEIRDGTIVQYGRIEDLLAR 232
Cdd:cd03252 154 IHNPRILIFDEATSALDYESEHAIMRNMHDICAGR--TVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAE 226
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
26-224 |
2.25e-31 |
|
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: 117.27 E-value: 2.25e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 26 SLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgealrRERRAIGTVFQSSALLSRRTAWENVA 105
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLA-----PYQRPVSMLFQENNLFAHLTVRQNIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 106 L---PLAWLGVVErdiKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLA 182
Cdd:TIGR01277 93 LglhPGLKLNAEQ---QEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLA 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1319887251 183 LLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYG 224
Cdd:TIGR01277 170 LVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
10-220 |
2.65e-31 |
|
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: 115.78 E-value: 2.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 10 SYRTADGRlSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRErraIGTVF 89
Cdd:cd03246 7 SFRYPGAE-PPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH---VGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 90 QSSALLSrrtawenvalplawlgvverdikarvGELLESVglshkadawpaqLSGGQRQRIGIARALALRPSVLLADEAT 169
Cdd:cd03246 83 QDDELFS--------------------------GSIAENI------------LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1319887251 170 SGLDPQATASVLALLKRLRdEYQLAIVLITHEMDAVRtAADAVAEIRDGTI 220
Cdd:cd03246 125 SHLDVEGERALNQAIAALK-AAGATRIVIAHRPETLA-SADRILVLEDGRV 173
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-237 |
3.21e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 118.66 E-value: 3.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSAlsgEALRRERRAIGTVFQS-SALLSRRTA 100
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA---ENVWNLRRKIGMVFQNpDNQFVGATV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 WENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASV 180
Cdd:PRK13642 100 EDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1319887251 181 LALLKRLRDEYQLAIVLITHEMDAVrTAADAVAEIRDGTIVQYGRIEDLLARPDSLL 237
Cdd:PRK13642 180 MRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELFATSEDMV 235
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-220 |
3.65e-31 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 118.24 E-value: 3.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSY--RTadgrlsaVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIringqdlsaLSGEA-L 78
Cdd:PRK11247 13 LLLNAVSKRYgeRT-------VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL---------LAGTApL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 79 RRERRAIGTVFQSSALLSRRTAWENVALPLawlgvvERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALAL 158
Cdd:PRK11247 77 AEAREDTRLMFQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1319887251 159 RPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTI 220
Cdd:PRK11247 151 RPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-232 |
4.60e-31 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 117.49 E-value: 4.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTADGRLSA-----------------VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSI 63
Cdd:COG1134 4 MIEVENVSKSYRLYHEPSRSlkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 64 RINGQdLSALsgeaLrrerrAIGTVFQSSAllsrrTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAwPAQ-L 142
Cdd:COG1134 84 EVNGR-VSAL----L-----ELGAGFHPEL-----TGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQ-PVKtY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 143 SGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQlAIVLITHEMDAVRTAADAVAEIRDGTIVQ 222
Cdd:COG1134 148 SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSMGAVRRLCDRAIWLEKGRLVM 226
|
250
....*....|
gi 1319887251 223 YGRIEDLLAR 232
Cdd:COG1134 227 DGDPEEVIAA 236
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-236 |
6.59e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 118.01 E-value: 6.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSG-EALRRERRAIGTVFQ-SSALLSRRT 99
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGnKNLKKLRKKVSLVFQfPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 100 AWENVALPLAWLGVVERDIKARVGELLESVGLSHK-ADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATA 178
Cdd:PRK13641 103 VLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRK 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1319887251 179 SVLALLKrlrdEYQLA---IVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSL 236
Cdd:PRK13641 183 EMMQLFK----DYQKAghtVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEWL 239
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-236 |
8.86e-31 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 117.42 E-value: 8.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTAdgrlsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSaLSGEALRR 80
Cdd:PRK13638 1 MLATSDLWFRYQDE-----PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRAIGTVFQSSALLSRRTAWE-NVALPLAWLGVVERDIKARVGELLESVGLSHKADAwPAQ-LSGGQRQRIGIARALAL 158
Cdd:PRK13638 75 LRQQVATVFQDPEQQIFYTDIDsDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQ-PIQcLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1319887251 159 RPSVLLADEATSGLDPQATASVLALLKRLRDEYQlAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSL 236
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEAM 230
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
16-234 |
1.17e-30 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 116.63 E-value: 1.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 16 GRLSAVlKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRErraiGTV--FQSSA 93
Cdd:PRK11300 16 GGLLAV-NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM----GVVrtFQHVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 94 LLSRRTAWEN--VA-------------LPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALAL 158
Cdd:PRK11300 91 LFREMTVIENllVAqhqqlktglfsglLKTPAFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVT 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1319887251 159 RPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPD 234
Cdd:PRK11300 171 QPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPD 246
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
36-248 |
2.33e-30 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 121.50 E-value: 2.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 36 AVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRERRAIGTVFQS--SALLSRRTAWENVALPLAWLGV 113
Cdd:PRK10261 354 SLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDpyASLDPRQTVGDSIMEPLRVHGL 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 114 VERD-IKARVGELLESVGLSHKaDAW--PAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDE 190
Cdd:PRK10261 434 LPGKaAAARVAWLLERVGLLPE-HAWryPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRD 512
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1319887251 191 YQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSLLGQQLLPLTPAA 248
Cdd:PRK10261 513 FGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVPVA 570
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
22-233 |
2.67e-30 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 115.64 E-value: 2.67e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLARCISLL-----EQPDSGSIRINGQDLSALSGEA--LRRErraIGTVFQSSAL 94
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTvdLRKE---IGMVFQQPNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 95 LSRrTAWENVALPLAWLGVVErdiKARVGELLESvglSHK-ADAW----------PAQLSGGQRQRIGIARALALRPSVL 163
Cdd:PRK14239 98 FPM-SIYENVVYGLRLKGIKD---KQVLDEAVEK---SLKgASIWdevkdrlhdsALGLSGGQQQRVCIARVLATSPKII 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 164 LADEATSGLDPQATASVLALLKRLRDEYQLAIVliTHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARP 233
Cdd:PRK14239 171 LLDEPTSALDPISAGKIEETLLGLKDDYTMLLV--TRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNP 238
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
2-232 |
3.12e-30 |
|
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: 115.02 E-value: 3.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYrtaDGRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRE 81
Cdd:cd03251 1 VEFKNVTFRY---PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 rraIGTVFQSSALLSRrTAWENVALplAWLGVVERDIK--ARVGELLESV-----GLSHKADAWPAQLSGGQRQRIGIAR 154
Cdd:cd03251 78 ---IGLVSQDVFLFND-TVAENIAY--GRPGATREEVEeaARAANAHEFImelpeGYDTVIGERGVKLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1319887251 155 ALALRPSVLLADEATSGLDPQATASVLALLKRLRdEYQLAIVlITHEMDAVRTaADAVAEIRDGTIVQYGRIEDLLAR 232
Cdd:cd03251 152 ALLKDPPILILDEATSALDTESERLVQAALERLM-KNRTTFV-IAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQ 226
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
6-225 |
4.41e-30 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 117.82 E-value: 4.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 6 DLYKSYRTAdgrlsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgealrRERRAI 85
Cdd:PRK11000 8 NVTKAYGDV-----VISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVP-----PAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 86 GTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLA 165
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 166 DEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGR 225
Cdd:PRK11000 158 DEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGK 217
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
22-231 |
1.11e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 114.88 E-value: 1.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEA-LRRERRAIGTVFQ--SSALLSRR 98
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKyIRPVRKRIGMVFQfpESQLFEDT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 99 TAWE------NVALPLawlgvveRDIKARVGELLESVGLSHKA-DAWPAQLSGGQRQRIGIARALALRPSVLLADEATSG 171
Cdd:PRK13646 103 VEREiifgpkNFKMNL-------DEVKNYAHRLLMDLGFSRDVmSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 172 LDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLA 231
Cdd:PRK13646 176 LDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-232 |
1.76e-29 |
|
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: 118.77 E-value: 1.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALrreRRAIGTVFQSSALLSrRTA 100
Cdd:COG5265 373 ILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL---RAAIGIVPQDTVLFN-DTI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 WENVAL--PLAWLGVVERDIKA----------------RVGELlesvGLshkadawpaQLSGGQRQRIGIARALALRPSV 162
Cdd:COG5265 449 AYNIAYgrPDASEEEVEAAARAaqihdfieslpdgydtRVGER----GL---------KLSGGEKQRVAIARTLLKNPPI 515
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 163 LLADEATSGLDPQATASVLALLKRLRdEYQLAIVlITHEMDAVrTAADAVAEIRDGTIVQYGRIEDLLAR 232
Cdd:COG5265 516 LIFDEATSALDSRTERAIQAALREVA-RGRTTLV-IAHRLSTI-VDADEILVLEAGRIVERGTHAELLAQ 582
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-247 |
2.92e-29 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 117.50 E-value: 2.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTAdGRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCI-SLLEQPD----SGSIRINGQDLSALSG 75
Cdd:PRK15134 5 LLAIENLSVAFRQQ-QTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSIlRLLPSPPvvypSGDIRFHGESLLHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 76 EALRRER-RAIGTVFQSSalLSRRTAWENVALPLAWLGVVERDI--KARVGEL---LESVGLSHKA---DAWPAQLSGGQ 146
Cdd:PRK15134 84 QTLRGVRgNKIAMIFQEP--MVSLNPLHTLEKQLYEVLSLHRGMrrEAARGEIlncLDRVGIRQAAkrlTDYPHQLSGGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 147 RQRIGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRI 226
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRA 241
|
250 260
....*....|....*....|.
gi 1319887251 227 EDLLARPDSLLGQQLLPLTPA 247
Cdd:PRK15134 242 ATLFSAPTHPYTQKLLNSEPS 262
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-212 |
5.66e-29 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 112.10 E-value: 5.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYrtaDGRlsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEAlrr 80
Cdd:PRK11248 1 MLQISHLYADY---GGK--PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER--- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 erraiGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:PRK11248 73 -----GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1319887251 161 SVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEM-DAVRTAADAV 212
Cdd:PRK11248 148 QLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIeEAVFMATELV 200
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-236 |
8.08e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.79 E-value: 8.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLykSYRTAdGRlsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRR 80
Cdd:PRK13548 2 MLEARNL--SVRLG-GR--TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 eRRAIgtVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALA--- 157
Cdd:PRK13548 77 -RRAV--LPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlw 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 158 ---LRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLaRPD 234
Cdd:PRK13548 154 epdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVL-TPE 232
|
..
gi 1319887251 235 SL 236
Cdd:PRK13548 233 TL 234
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
21-234 |
1.35e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 116.36 E-value: 1.35e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTlarCISLLE---QPDSGSIRINGQDLSALSGEALRRERRAIGtvfqSSALLSR 97
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKST---VAALLQnlyQPTGGQVLLDGVPLVQYDHHYLHRQVALVG----QEPVLFS 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 98 RTAWENVALPLAWLGVVERDIKAR-------VGELLEsvGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATS 170
Cdd:TIGR00958 569 GSVRENIAYGLTDTPDEEIMAAAKaanahdfIMEFPN--GYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1319887251 171 GLDpqatASVLALLKRLRDEYQLAIVLITHEMDAVRTaADAVAEIRDGTIVQYGRIEDLLARPD 234
Cdd:TIGR00958 647 ALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQG 705
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
20-232 |
1.99e-28 |
|
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: 115.23 E-value: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 20 AVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRerrAIGTVFQSSALLSRRT 99
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGR---HIGYLPQDVELFDGTI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 100 AwENVALplawLG------VVERDIKARVGELLESV--GLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSG 171
Cdd:COG4618 423 A-ENIAR----FGdadpekVVAAAKLAGVHEMILRLpdGYDTRIGEGGARLSGGQRQRIGLARALYGDPRLVVLDEPNSN 497
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1319887251 172 LDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRtAADAVAEIRDGTIVQYGRIEDLLAR 232
Cdd:COG4618 498 LDDEGEAALAAAIRALKAR-GATVVVITHRPSLLA-AVDKLLVLRDGRVQAFGPRDEVLAR 556
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
20-200 |
2.16e-28 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 108.79 E-value: 2.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 20 AVLKGLSLQVPERSITAVVGPSGAGKSTLARCIS--LLEQPDSGSIRINGQDLSalsgeaLRRERRAIGTVFQSSALLSR 97
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLD------KRSFRKIIGYVPQDDILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 98 RTAWENvalplawlgvverdikarvgeLLESVGLShkadawpaQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQAT 177
Cdd:cd03213 97 LTVRET---------------------LMFAAKLR--------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180
....*....|....*....|...
gi 1319887251 178 ASVLALLKRLRDEyQLAIVLITH 200
Cdd:cd03213 148 LQVMSLLRRLADT-GRTIICSIH 169
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
27-233 |
3.95e-28 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 111.89 E-value: 3.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 27 LQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLS-ALSGEALRRERRAIGTVFQSSALLSRRTAWENVA 105
Cdd:PRK11144 19 LTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFdAEKGICLPPEKRRIGYVFQDARLFPHYKVRGNLR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 106 LplawlGVVERDiKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLALLK 185
Cdd:PRK11144 99 Y-----GMAKSM-VAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLE 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1319887251 186 RLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARP 233
Cdd:PRK11144 173 RLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
1-231 |
5.11e-28 |
|
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: 114.13 E-value: 5.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTADGRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGS--IRINGQ--DLSALSGE 76
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEvnVRVGDEwvDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 77 ALRRERRAIGTVFQSSALLSRRTAWENVALPLAwLGVVERDIKARVGELLESVGLSHKA-----DAWPAQLSGGQRQRIG 151
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIG-LELPDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHRVA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 152 IARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLA 231
Cdd:TIGR03269 438 LAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
2-221 |
6.14e-28 |
|
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: 108.96 E-value: 6.14e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRTADG----------------RLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRI 65
Cdd:cd03267 1 IEVSNLSKSYRVYSKepgligslkslfkrkyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 66 NGQDLSALSGEALRRerraIGTVF-QSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSG 144
Cdd:cd03267 81 AGLVPWKRRKKFLRR----IGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1319887251 145 GQRQRIGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIV 221
Cdd:cd03267 157 GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
2-243 |
5.08e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 107.79 E-value: 5.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRTADGRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSA--LSGEALR 79
Cdd:PRK13645 7 IILDNVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 80 RERRAIGTVFQ-SSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHK-ADAWPAQLSGGQRQRIGIARALA 157
Cdd:PRK13645 87 RLRKEIGLVFQfPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 158 LRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSLL 237
Cdd:PRK13645 167 MDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQELLT 246
|
....*.
gi 1319887251 238 GQQLLP 243
Cdd:PRK13645 247 KIEIDP 252
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-246 |
5.77e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 107.38 E-value: 5.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLykSYRTADGrlSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgeALRR 80
Cdd:PRK13644 1 MIRLENV--SYSYPDG--TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS--KLQG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRAIGTVFQS-SALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALR 159
Cdd:PRK13644 75 IRKLVGIVFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 160 PSVLLADEATSGLDPQATASVLALLKRLRDEYQlAIVLITHEMDAVRtAADAVAEIRDGTIVQYGRIEDLLARPdSLlgq 239
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHEKGK-TIVYITHNLEELH-DADRIIVMDRGKIVLEGEPENVLSDV-SL--- 228
|
....*..
gi 1319887251 240 QLLPLTP 246
Cdd:PRK13644 229 QTLGLTP 235
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-230 |
7.95e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 108.38 E-value: 7.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAID--DLYKSYRTadgrlSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgeal 78
Cdd:PRK13536 39 TVAIDlaGVSKSYGD-----KAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARA---- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 79 RRERRAIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALAL 158
Cdd:PRK13536 110 RLARARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALIN 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1319887251 159 RPSVLLADEATSGLDPQATASVLALLKRLRDEYQlAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLL 230
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI 260
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-232 |
9.31e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 107.48 E-value: 9.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTA---DGRLSAV-------------LKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIR 64
Cdd:COG4586 1 IIEVENLSKTYRVYekePGLKGALkglfrreyreveaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 65 INGQDLSalsgealrRERRA----IGTVF-QSSALLsrrtaWEnvaLPLA----WLGVV----ERDIKARVGELLESVGL 131
Cdd:COG4586 81 VLGYVPF--------KRRKEfarrIGVVFgQRSQLW-----WD---LPAIdsfrLLKAIyripDAEYKKRLDELVELLDL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 132 SHKADAwPA-QLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAAD 210
Cdd:COG4586 145 GELLDT-PVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCD 223
|
250 260
....*....|....*....|..
gi 1319887251 211 AVAEIRDGTIVQYGRIEDLLAR 232
Cdd:COG4586 224 RVIVIDHGRIIYDGSLEELKER 245
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
21-231 |
2.09e-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: 109.83 E-value: 2.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRErraIGTVFQSSALLSRRTA 100
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQ---MGVVLQENVLFSRSIR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 wENVALPLAWLGVVERDIKARVGELLESV-----GLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQ 175
Cdd:TIGR01846 549 -DNIALCNPGAPFEHVIHAAKLAGAHDFIselpqGYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEATSALDYE 627
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1319887251 176 ATASVLALLKRLRDEYqlAIVLITHEMDAVRtAADAVAEIRDGTIVQYGRIEDLLA 231
Cdd:TIGR01846 628 SEALIMRNMREICRGR--TVIIIAHRLSTVR-ACDRIIVLEKGQIAESGRHEELLA 680
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
21-208 |
2.45e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 103.47 E-value: 2.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRingqdlsalsgealRRERRAIGTVFQSSALLSR--R 98
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR--------------RAGGARVAYVPQRSEVPDSlpL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 99 TAWENVAL----PLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDP 174
Cdd:NF040873 73 TVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDA 152
|
170 180 190
....*....|....*....|....*....|....
gi 1319887251 175 QATASVLALLKRLRDEyQLAIVLITHEMDAVRTA 208
Cdd:NF040873 153 ESRERIIALLAEEHAR-GATVVVVTHDLELVRRA 185
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
13-233 |
2.49e-26 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 106.53 E-value: 2.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 13 TADGRLSAVLKgLSLQVPERSITAVVGPSGAGKSTLARCIsLLEQPDSGSI-----RINGQDLSALSGEAlRRE--RRAI 85
Cdd:COG4170 15 TPQGRVKAVDR-VSLTLNEGEIRGLVGESGSGKSLIAKAI-CGITKDNWHVtadrfRWNGIDLLKLSPRE-RRKiiGREI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 86 GTVFQ--SSALLSRRTAWENV--ALPLA------WLGVVERdiKARVGELLESVGL-SHKA--DAWPAQLSGGQRQRIGI 152
Cdd:COG4170 92 AMIFQepSSCLDPSAKIGDQLieAIPSWtfkgkwWQRFKWR--KKRAIELLHRVGIkDHKDimNSYPHELTEGECQKVMI 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 153 ARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLAR 232
Cdd:COG4170 170 AMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKS 249
|
.
gi 1319887251 233 P 233
Cdd:COG4170 250 P 250
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-233 |
2.82e-26 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 106.73 E-value: 2.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTADGRLSAVLK-GLSLQVPErsITAVVGPSGAGKSTLARCISLLEQPD---SGSIRINGQDLSALSGE 76
Cdd:PRK09473 12 LLDVKDLRVTFSTPDGDVTAVNDlNFSLRAGE--TLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 77 ALRRER-RAIGTVFQSsallsrrtawenvalPLAWLgvverDIKARVGELLESVGLSHK----ADAW------------- 138
Cdd:PRK09473 90 ELNKLRaEQISMIFQD---------------PMTSL-----NPYMRVGEQLMEVLMLHKgmskAEAFeesvrmldavkmp 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 139 ---------PAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAA 209
Cdd:PRK09473 150 earkrmkmyPHEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGIC 229
|
250 260
....*....|....*....|....
gi 1319887251 210 DAVAEIRDGTIVQYGRIEDLLARP 233
Cdd:PRK09473 230 DKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-233 |
3.34e-26 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 104.87 E-value: 3.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTADG-----RLSAVlKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSAlsG 75
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGwfrrqTVEAV-KPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF--G 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 76 EALRRERRaIGTVFQ--SSALLSRRTAWENVALPLAW---LGVVERDikARVGELLESVGL-SHKADAWPAQLSGGQRQR 149
Cdd:PRK15112 81 DYSYRSQR-IRMIFQdpSTSLNPRQRISQILDFPLRLntdLEPEQRE--KQIIETLRQVGLlPDHASYYPHMLAPGQKQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 150 IGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDL 229
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADV 237
|
....
gi 1319887251 230 LARP 233
Cdd:PRK15112 238 LASP 241
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
21-243 |
3.81e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 105.55 E-value: 3.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDlSALSGEALRRE------------------- 81
Cdd:PRK13651 22 ALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKD-EKNKKKTKEKEkvleklviqktrfkkikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 ---RRAIGTVFQ-SSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHK-ADAWPAQLSGGQRQRIGIARAL 156
Cdd:PRK13651 101 keiRRRVGVVFQfAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDESyLQRSPFELSGGQKRRVALAGIL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 157 ALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQlAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSL 236
Cdd:PRK13651 181 AMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSDNKFL 259
|
....*..
gi 1319887251 237 LGQQLLP 243
Cdd:PRK13651 260 IENNMEP 266
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
21-232 |
4.70e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 105.66 E-value: 4.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSalsgEALRRERRAIGTVFQSSALLSRRTA 100
Cdd:PRK13537 22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP----SRARHARQRVGVVPQFDNLDPDFTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 WENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASV 180
Cdd:PRK13537 98 RENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLM 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1319887251 181 LALLKRLRDEYQlAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLAR 232
Cdd:PRK13537 178 WERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIES 228
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-242 |
7.35e-26 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 103.63 E-value: 7.35e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 23 KGLSLQVPERSITAVVGPSGAGKSTlaRCISLLEQPDSGSIRINGQ---DLSALSGEALRRerRAIGTVFQS--SALLSR 97
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKSL--TCAAALGILPAGVRQTAGRvllDGKPVAPCALRG--RKIATIMQNprSAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 98 RTAWENVALPLAWLGVVERDikARVGELLESVGLSHKA---DAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDP 174
Cdd:PRK10418 96 HTMHTHARETCLALGKPADD--ATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1319887251 175 QATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSLLGQQLL 242
Cdd:PRK10418 174 VAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLV 241
|
|
| NHLM_micro_ABC1 |
TIGR03796 |
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ... |
21-233 |
7.44e-26 |
|
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 108.49 E-value: 7.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRerrAIGTVFQSsALLSRRTA 100
Cdd:TIGR03796 494 LIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLAN---SVAMVDQD-IFLFEGTV 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 WENVAL-----PLAWL------GVVERDIKARVG----ELLESvglshkadawPAQLSGGQRQRIGIARALALRPSVLLA 165
Cdd:TIGR03796 570 RDNLTLwdptiPDADLvrackdAAIHDVITSRPGgydaELAEG----------GANLSGGQRQRLEIARALVRNPSILIL 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1319887251 166 DEATSGLDPQATASVLALLKRlrdeYQLAIVLITHEMDAVRTaADAVAEIRDGTIVQYGRIEDLLARP 233
Cdd:TIGR03796 640 DEATSALDPETEKIIDDNLRR----RGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRGTHEELWAVG 702
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-231 |
1.21e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 103.05 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 5 DDLYKSYRtadGRlsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEAlrRERRA 84
Cdd:PRK10895 7 KNLAKAYK---GR--RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 85 IGTVFQSSALLSRRTAWENVALPLAwlgvVERDI-----KARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALR 159
Cdd:PRK10895 80 IGYLPQEASIFRRLSVYDNLMAVLQ----IRDDLsaeqrEDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAAN 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1319887251 160 PSVLLADEATSGLDPQATASVLALLKRLRDeYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLA 231
Cdd:PRK10895 156 PKFILLDEPFAGVDPISVIDIKRIIEHLRD-SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
21-233 |
1.35e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 105.69 E-value: 1.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRErraIGTVFQSSAL---LSR 97
Cdd:PRK09536 18 VLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR---VASVPQDTSLsfeFDV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 98 RTAWENVALP-LAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQA 176
Cdd:PRK09536 95 RQVVEMGRTPhRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINH 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1319887251 177 TASVLALLKRLRDEYQLAIVLItHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARP 233
Cdd:PRK09536 175 QVRTLELVRRLVDDGKTAVAAI-HDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-220 |
1.91e-25 |
|
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: 100.58 E-value: 1.91e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 17 RLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgealRRERRAIGTVF-----QS 91
Cdd:cd03215 11 SVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRS----PRDAIRAGIAYvpedrKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 92 SALLSRRTAWENVALPlawlgvverdikarvgellesvglshkadawpAQLSGGQRQRIGIARALALRPSVLLADEATSG 171
Cdd:cd03215 87 EGLVLDLSVAENIALS--------------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1319887251 172 LDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTI 220
Cdd:cd03215 135 VDVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-282 |
3.67e-25 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 103.77 E-value: 3.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYrtaDGRLsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgealRR 80
Cdd:PRK11650 3 GLKLQAVRKSY---DGKT-QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELE----PA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ErRAIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:PRK11650 75 D-RDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 161 SVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITH-EMDAVrTAADAVAEIRDGTIVQYGRIEDLLARPDSL--- 236
Cdd:PRK11650 154 AVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHdQVEAM-TLADRVVVMNGGVAEQIGTPVEVYEKPASTfva 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1319887251 237 --LGQQLLPLTPAAATHSDLLLRLSYRWDVPVATDWISRLSQQWALQI 282
Cdd:PRK11650 233 sfIGSPAMNLLDGRVSADGAAFELAGGIALPLGGGYRQYAGRKLTLGI 280
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-230 |
7.79e-25 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 100.86 E-value: 7.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTadgrlSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRR 80
Cdd:PRK11231 2 TLRTENLTVGYGT-----KRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 erraigtvfqSSALLSRR-------TAWENVA------LPLaWlGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQR 147
Cdd:PRK11231 77 ----------RLALLPQHhltpegiTVRELVAygrspwLSL-W-GRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 148 QRIGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLItHEMDAVRTAADAVAEIRDGTIVQYGRIE 227
Cdd:PRK11231 145 QRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVL-HDLNQASRYCDHLVVLANGHVMAQGTPE 223
|
...
gi 1319887251 228 DLL 230
Cdd:PRK11231 224 EVM 226
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
36-224 |
7.95e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 101.16 E-value: 7.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 36 AVVGPSGAGKSTLARCISLLEQPDSGSIRINGQ-----DLSALSgEALRRE--RRAIGTVFQSSA--LLSRRTAWENVAL 106
Cdd:PRK11701 36 GIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALS-EAERRRllRTEWGFVHQHPRdgLRMQVSAGGNIGE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 107 PLawLGVVER---DIKARVGELLESVGL-SHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLA 182
Cdd:PRK11701 115 RL--MAVGARhygDIRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLD 192
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1319887251 183 LLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYG 224
Cdd:PRK11701 193 LLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG 234
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-232 |
8.87e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 104.91 E-value: 8.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYrtaDGRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLarcISLLE---QPDSGSIRINGQDLSALSGEAL 78
Cdd:PRK11160 339 LTLNNVSFTY---PDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTL---LQLLTrawDPQQGEILLNGQPIADYSEAAL 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 79 RRerrAIGTVFQSSALLSRrTAWEN--VALPLAwlgvverdIKARVGELLESVGLS------HKADAWPA----QLSGGQ 146
Cdd:PRK11160 413 RQ---AISVVSQRVHLFSA-TLRDNllLAAPNA--------SDEALIEVLQQVGLEklleddKGLNAWLGeggrQLSGGE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 147 RQRIGIARALaLRPS-VLLADEATSGLDPQATASVLALLKRLRDEYQLaiVLITHEMDAVrTAADAVAEIRDGTIVQYGR 225
Cdd:PRK11160 481 QRRLGIARAL-LHDApLLLLDEPTEGLDAETERQILELLAEHAQNKTV--LMITHRLTGL-EQFDRICVMDNGQIIEQGT 556
|
....*..
gi 1319887251 226 IEDLLAR 232
Cdd:PRK11160 557 HQELLAQ 563
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-232 |
9.53e-25 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 104.80 E-value: 9.53e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRtaDGRLsaVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALrre 81
Cdd:PRK10790 341 IDIDNVSFAYR--DDNL--VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL--- 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQSSALLSrRTAWENVALplawlgvvERDI-KARVGELLESVGLSHKADAWPA-----------QLSGGQRQR 149
Cdd:PRK10790 414 RQGVAMVQQDPVVLA-DTFLANVTL--------GRDIsEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQL 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 150 IGIARALALRPSVLLADEATSGLDP---QATASVLALLKRlrdeyQLAIVLITHEMDAVrTAADAVAEIRDGTIVQYGRI 226
Cdd:PRK10790 485 LALARVLVQTPQILILDEATANIDSgteQAIQQALAAVRE-----HTTLVVIAHRLSTI-VEADTILVLHRGQAVEQGTH 558
|
....*.
gi 1319887251 227 EDLLAR 232
Cdd:PRK10790 559 QQLLAA 564
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-224 |
1.04e-24 |
|
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: 99.91 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRTADGRLSA-----------------VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIR 64
Cdd:cd03220 1 IELENVSKSYPTYKGGSSSlkklgilgrkgevgefwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 65 INGQDLSALsgealrrerrAIGTVFQSSAllsrrTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSG 144
Cdd:cd03220 81 VRGRVSSLL----------GLGGGFNPEL-----TGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 145 GQRQRIGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQlAIVLITHEMDAVRTAADAVAEIRDGTIVQYG 224
Cdd:cd03220 146 GMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
16-232 |
1.26e-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: 104.41 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 16 GRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgeaLRRERRAIGTVFQSSALL 95
Cdd:TIGR02203 342 GRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT---LASLRRQVALVSQDVVLF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 96 SRRTAwENVALplawlGVVERDIKARVGELLESVGLSHKADAWP-----------AQLSGGQRQRIGIARALALRPSVLL 164
Cdd:TIGR02203 419 NDTIA-NNIAY-----GRTEQADRAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARALLKDAPILI 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1319887251 165 ADEATSGLDPQATASVLALLKRLRDEYqlAIVLITHEMDAVRTaADAVAEIRDGTIVQYGRIEDLLAR 232
Cdd:TIGR02203 493 LDEATSALDNESERLVQAALERLMQGR--TTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLAR 557
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
15-232 |
1.78e-24 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 103.89 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 15 DGRLSAVlKGLSLQVPERSITAVVGPSGAGKSTLarcISLLEQ---PDSGSIRINGQDLSALSGEALrreRRAIGTVFQs 91
Cdd:PRK13657 345 DNSRQGV-EDVSFEAKPGQTVAIVGPTGAGKSTL---INLLQRvfdPQSGRILIDGTDIRTVTRASL---RRNIAVVFQ- 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 92 SALLSRRTAWEN--VALPLAWLGVVERDIK-ARVGELLE--SVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLAD 166
Cdd:PRK13657 417 DAGLFNRSIEDNirVGRPDATDEEMRAAAErAQAHDFIErkPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILD 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1319887251 167 EATSGLDPQATASVLALLKRLRDEYQLAIvlITHEMDAVRTaADAVAEIRDGTIVQYGRIEDLLAR 232
Cdd:PRK13657 497 EATSALDVETEAKVKAALDELMKGRTTFI--IAHRLSTVRN-ADRILVFDNGRVVESGSFDELVAR 559
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-221 |
6.13e-24 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.03 E-value: 6.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 4 IDDLykSYRTADGRLsaVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgealRRERR 83
Cdd:COG3845 260 VENL--SVRDDRGVP--ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS----PRERR 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 84 AIGTVF-----QSSALLSRRTAWENVAL------PLAWLGVVERD-IKARVGELLE-----SVGLSHKAdawpAQLSGGQ 146
Cdd:COG3845 332 RLGVAYipedrLGRGLVPDMSVAENLILgryrrpPFSRGGFLDRKaIRAFAEELIEefdvrTPGPDTPA----RSLSGGN 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1319887251 147 RQRIGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTIV 221
Cdd:COG3845 408 QQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
10-208 |
7.92e-24 |
|
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: 97.54 E-value: 7.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 10 SYRTADGRLsaVLKGLSLQVPERSITAVVGPSGAGKSTlarCISLLE---QPDSGSIRINGQDLSALSGEALRRErraIG 86
Cdd:cd03248 20 AYPTRPDTL--VLQDVSFTLHPGEVTALVGPSGSGKST---VVALLEnfyQPQGGQVLLDGKPISQYEHKYLHSK---VS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 87 TVFQSSALLSRRTAwENVALPLA---WLGVVERDIKARVGELLESV--GLSHKADAWPAQLSGGQRQRIGIARALALRPS 161
Cdd:cd03248 92 LVGQEPVLFARSLQ-DNIAYGLQscsFECVKEAAQKAHAHSFISELasGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1319887251 162 VLLADEATSGLDpqaTASVLALLKRLRDEYQLAIVL-ITHEMDAVRTA 208
Cdd:cd03248 171 VLILDEATSALD---AESEQQVQQALYDWPERRTVLvIAHRLSTVERA 215
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
21-224 |
7.96e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 99.54 E-value: 7.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRI----NGQDLSALSGEA---------LRRERRAIGT 87
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELITnpyskkiknFKELRRRVSM 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 88 VFQ-SSALLSRRTAWENVAL-PLAwLGVVERDIKARVGELLESVGLSHK-ADAWPAQLSGGQRQRIGIARALALRPSVLL 164
Cdd:PRK13631 121 VFQfPEYQLFKDTIEKDIMFgPVA-LGVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQPEILI 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 165 ADEATSGLDPQATASVLALLKRLRDEYQLAIVlITHEMDAVRTAADAVAEIRDGTIVQYG 224
Cdd:PRK13631 200 FDEPTAGLDPKGEHEMMQLILDAKANNKTVFV-ITHTMEHVLEVADEVIVMDKGKILKTG 258
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-232 |
8.97e-24 |
|
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: 101.80 E-value: 8.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYrtaDGRlsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQ--PDSGSIRIN------------- 66
Cdd:TIGR03269 1 IEVKNLTKKF---DGK--EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHvalcekcgyverp 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 67 ---GQ--------------DLSALSGEALRRERRAIGTVFQSS-ALLSRRTAWENVALPLAWLGVVERDIKARVGELLES 128
Cdd:TIGR03269 76 skvGEpcpvcggtlepeevDFWNLSDKLRRRIRKRIAIMLQRTfALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 129 VGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTA 208
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDL 235
|
250 260
....*....|....*....|....
gi 1319887251 209 ADAVAEIRDGTIVQYGRIEDLLAR 232
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDEVVAV 259
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
19-212 |
1.57e-23 |
|
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: 101.21 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 19 SAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRErraIGTVFQSSALLSRR 98
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQ---IAWVPQHPFLFAGT 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 99 TAwENVALPL---AWLGVVERDIKARVGELLESV--GLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLD 173
Cdd:TIGR02857 412 IA-ENIRLARpdaSDAEIREALERAGLDEFVAALpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLD 490
|
170 180 190
....*....|....*....|....*....|....*....
gi 1319887251 174 PQATASVLALLKRLRDEYqlAIVLITHEmDAVRTAADAV 212
Cdd:TIGR02857 491 AETEAEVLEALRALAQGR--TVLLVTHR-LALAALADRI 526
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
2-224 |
2.05e-23 |
|
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: 96.41 E-value: 2.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRtadGRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgeaLRRE 81
Cdd:cd03244 3 IEFKNVSLRYR---PNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQSSALLSRrTAWENVAlPLA-------WLGVVERDIKARVGELLEsvGLSHKADAWPAQLSGGQRQRIGIAR 154
Cdd:cd03244 77 RSRISIIPQDPVLFSG-TIRSNLD-PFGeysdeelWQALERVGLKEFVESLPG--GLDTVVEEGGENLSVGQRQLLCLAR 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1319887251 155 ALALRPSVLLADEATSGLDPQaTASVLAllKRLRDEYQLAIVL-ITHEMDAVrTAADAVAEIRDGTIVQYG 224
Cdd:cd03244 153 ALLRKSKILVLDEATASVDPE-TDALIQ--KTIREAFKDCTVLtIAHRLDTI-IDSDRILVLDKGRVVEFD 219
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
20-221 |
2.34e-23 |
|
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: 96.12 E-value: 2.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 20 AVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRErraIGTVFQSSALLSRrT 99
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN---IGYVPQDVTLFYG-T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 100 AWENVALplawlGVVERDiKARVGELLESVGLSHKADAWP-----------AQLSGGQRQRIGIARALALRPSVLLADEA 168
Cdd:cd03245 94 LRDNITL-----GAPLAD-DERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1319887251 169 TSGLDPQATASVLALLKRLRDEYqlAIVLITHEMdAVRTAADAVAEIRDGTIV 221
Cdd:cd03245 168 TSAMDMNSEERLKERLRQLLGDK--TLIIITHRP-SLLDLVDRIIVMDSGRIV 217
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
22-229 |
2.60e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 100.24 E-value: 2.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgEALRRErRAIGTVFQSSALLSRRTAW 101
Cdd:PRK09700 21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLD-HKLAAQ-LGIGIIYQELSVIDELTVL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 102 ENV---ALP---LAWLGVVE-RDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDP 174
Cdd:PRK09700 99 ENLyigRHLtkkVCGVNIIDwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTN 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1319887251 175 QATASVLALLKRLRDEYQlAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDL 229
Cdd:PRK09700 179 KEVDYLFLIMNQLRKEGT-AIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
37-212 |
2.93e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 95.94 E-value: 2.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 37 VVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRErraIGTVFQSSALLSRrTAWENVALPlaWLGVVER 116
Cdd:PRK10247 38 ITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQ---VSYCAQTPTLFGD-TVYDNLIFP--WQIRNQQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 117 DIKARVGELLESVGL-SHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAI 195
Cdd:PRK10247 112 PDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAV 191
|
170
....*....|....*..
gi 1319887251 196 VLITHEMDAVRTAADAV 212
Cdd:PRK10247 192 LWVTHDKDEINHADKVI 208
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-232 |
4.27e-23 |
|
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: 100.20 E-value: 4.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYrtadGRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRe 81
Cdd:TIGR01193 474 IVINDVSYSY----GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQ- 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 rrAIGTVFQSSALLSRrTAWENVALPlAWLGVVERDIKARVgELLE--------SVGLSHKADAWPAQLSGGQRQRIGIA 153
Cdd:TIGR01193 549 --FINYLPQEPYIFSG-SILENLLLG-AKENVSQDEIWAAC-EIAEikddienmPLGYQTELSEEGSSISGGQKQRIALA 623
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1319887251 154 RALALRPSVLLADEATSGLDPQATASVLALLKRLRDEyqlAIVLITHEMDaVRTAADAVAEIRDGTIVQYGRIEDLLAR 232
Cdd:TIGR01193 624 RALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLS-VAKQSDKIIVLDHGKIIEQGSHDELLDR 698
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-233 |
4.64e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 96.70 E-value: 4.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGsIRINGQDL----SALSGEALRRERRAIGTVFQSSALLS 96
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSG-YRYSGDVLlggrSIFNYRDVLEFRRRVGMLFQRPNPFP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 97 RRTAWENVALPLAWLGVVERDIKARVGELLESVGL----SHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGL 172
Cdd:PRK14271 115 MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSAL 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1319887251 173 DPQATASVLALLKRLRDeyQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARP 233
Cdd:PRK14271 195 DPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSP 253
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
25-250 |
5.61e-23 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 97.50 E-value: 5.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 25 LSLQVPERSITAVVGPSGAGKSTLARCI-SLLEQPD---SGSIRINGQDLSALSgealRRERRAI-----GTVFQ---SS 92
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAImGLIDYPGrvmAEKLEFNGQDLQRIS----EKERRNLvgaevAMIFQdpmTS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 93 ALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKA---DAWPAQLSGGQRQRIGIARALALRPSVLLADEAT 169
Cdd:PRK11022 102 LNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 170 SGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSLLGQQLLPLTPAAA 249
Cdd:PRK11022 182 TALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRALPEFA 261
|
.
gi 1319887251 250 T 250
Cdd:PRK11022 262 Q 262
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-222 |
7.18e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 98.83 E-value: 7.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLS-ALSGEALRRerrAIGTVFQSSALLSRRTA 100
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAA---GVAIIYQELHLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 WENV---ALPlAWLGVV-ERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQA 176
Cdd:PRK11288 97 AENLylgQLP-HKGGIVnRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSARE 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1319887251 177 TASVLALLKRLRDEYQlAIVLITHEMDAVRTAADAVAEIRDGTIVQ 222
Cdd:PRK11288 176 IEQLFRVIRELRAEGR-VILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
22-220 |
2.18e-22 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 94.69 E-value: 2.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGS---IRING---QDLSALSGEaLRRERRAIGTVFQSSALL 95
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAgshIELLGrtvQREGRLARD-IRKSRANTGYIFQQFNLV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 96 SRRTAWENVAL------PLaW---LGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLAD 166
Cdd:PRK09984 99 NRLSVLENVLIgalgstPF-WrtcFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1319887251 167 EATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTI 220
Cdd:PRK09984 178 EPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
21-227 |
2.27e-22 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 92.98 E-value: 2.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLE--QPDSGSIRINGQDLSALSGEalRRERRAIGTVFQSsallsrr 98
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPE--ERARLGIFLAFQY------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 99 tawenvalPLAWLGVverdikaRVGELLESVGLShkadawpaqLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATA 178
Cdd:cd03217 86 --------PPEIPGV-------KNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1319887251 179 SVLALLKRLRDEYQlAIVLITHE---MDAVRtaADAVAEIRDGTIVQYGRIE 227
Cdd:cd03217 142 LVAEVINKLREEGK-SVLIITHYqrlLDYIK--PDRVHVLYDGRIVKSGDKE 190
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-229 |
2.73e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 97.43 E-value: 2.73e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTAdgrlsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgeALRR 80
Cdd:PRK15439 11 LLCARSISKQYSGV-----EVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLT--PAKA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRAIGTVFQSSALLSRRTAWENVALPLAwlgvVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:PRK15439 84 HQLGIYLVPQEPLLFPNLSVKENILFGLP----KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDS 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1319887251 161 SVLLADEATSGLDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDL 229
Cdd:PRK15439 160 RILILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-223 |
3.77e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.06 E-value: 3.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 4 IDDLYKSYrtaDGRLsaVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRING--------QDLSALSG 75
Cdd:COG0488 1 LENLSKSF---GGRP--LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKglrigylpQEPPLDDD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 76 E--------------ALRRERRAIGTVF-QSSALLSRRTAWENVALPL-AWlgvverDIKARVGELLESVGLSHKADAWP 139
Cdd:COG0488 76 LtvldtvldgdaelrALEAELEELEAKLaEPDEDLERLAELQEEFEALgGW------EAEARAEEILSGLGFPEEDLDRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 140 -AQLSGGQRQRIGIARALALRPSVLLADEATSGLDpqaTASVLALLKRLRDeYQLAIVLITHE---MDAVrtaADAVAEI 215
Cdd:COG0488 150 vSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD---LESIEWLEEFLKN-YPGTVLVVSHDryfLDRV---ATRILEL 222
|
....*...
gi 1319887251 216 RDGTIVQY 223
Cdd:COG0488 223 DRGKLTLY 230
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-224 |
4.57e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 93.21 E-value: 4.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLE--QPDSGSIRINGQDLSALSGEAlrRERRAIGTVFQS------- 91
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGEDILELSPDE--RARAGIFLAFQYpveipgv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 92 --SALLsrRTAWENVALPLawlgVVERDIKARVGELLESVGLSHKAdawpAQ------LSGGQRQRIGIARALALRPSVL 163
Cdd:COG0396 93 svSNFL--RTALNARRGEE----LSAREFLKLLKEKMKELGLDEDF----LDryvnegFSGGEKKRNEILQMLLLEPKLA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1319887251 164 LADEATSGLDPQATASVLALLKRLRDEyQLAIVLITHE---MDAVRtaADAVAEIRDGTIVQYG 224
Cdd:COG0396 163 ILDETDSGLDIDALRIVAEGVNKLRSP-DRGILIITHYqriLDYIK--PDFVHVLVDGRIVKSG 223
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
21-224 |
6.06e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 93.51 E-value: 6.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSAL-SGEALRRerraIGTVFQSSALLSRRT 99
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYaSKEVARR----IGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 100 AWENVA--------LPLAWlgvvERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSG 171
Cdd:PRK10253 98 VQELVArgryphqpLFTRW----RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTW 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1319887251 172 LDPQATASVLALLKRLRDE--YQLAIVLitHEMD-AVRTAADAVAeIRDGTIVQYG 224
Cdd:PRK10253 174 LDISHQIDLLELLSELNREkgYTLAAVL--HDLNqACRYASHLIA-LREGKIVAQG 226
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
21-231 |
6.46e-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: 96.26 E-value: 6.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRErraIGTVFQSSALLSRRTA 100
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKH---IGYLPQDVELFPGTVA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 wENVAL---PLAWLGVVERDIKARVGELLESVGLSHKADAWP--AQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQ 175
Cdd:TIGR01842 410 -ENIARfgeNADPEKIIEAAKLAGVHELILRLPDGYDTVIGPggATLSGGQRQRIALARALYGDPKLVVLDEPNSNLDEE 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1319887251 176 ATASVLALLKRLRDEyQLAIVLITHEMdAVRTAADAVAEIRDGTIVQYGRIEDLLA 231
Cdd:TIGR01842 489 GEQALANAIKALKAR-GITVVVITHRP-SLLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-224 |
6.62e-22 |
|
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: 90.84 E-value: 6.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYrtaDGRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEAlrre 81
Cdd:cd03247 1 LSINNVSFSY---PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKAL---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQSSALLSrrtawenvalplawlgvverdikarvGELLESVGlshkadawpAQLSGGQRQRIGIARALALRPS 161
Cdd:cd03247 74 SSLISVLNQRPYLFD--------------------------TTLRNNLG---------RRFSGGERQRLALARILLQDAP 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1319887251 162 VLLADEATSGLDPQATASVLALL-KRLRDEyqlAIVLITHEMDAVRtAADAVAEIRDGTIVQYG 224
Cdd:cd03247 119 IVLLDEPTVGLDPITERQLLSLIfEVLKDK---TLIWITHHLTGIE-HMDKILFLENGKIIMQG 178
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-246 |
7.02e-22 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 96.46 E-value: 7.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTADGRLSAVlKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSI--------RINGQ--DL 70
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAV-RNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrRRSRQviEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 71 SALSGEALRRERRA-IGTVFQS--SALLSRRTAWENVALPLAW-LGVVERDIKARVGELLESVGLSHKADA---WPAQLS 143
Cdd:PRK10261 91 SEQSAAQMRHVRGAdMAMIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQTIlsrYPHQLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 144 GGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQY 223
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVET 250
|
250 260
....*....|....*....|...
gi 1319887251 224 GRIEDLLARPDSLLGQQLLPLTP 246
Cdd:PRK10261 251 GSVEQIFHAPQHPYTRALLAAVP 273
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
21-203 |
1.18e-21 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 91.56 E-value: 1.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCI--SLLEQPDSGSIRINGQDLSalsgealrrerraigtvfQSSALLsrr 98
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQFG------------------REASLI--- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 99 tawENVALplawlgvvERDIKARVgELLESVGLShkaDAW-----PAQLSGGQRQRIGIARALALRPSVLLADEATSGLD 173
Cdd:COG2401 104 ---DAIGR--------KGDFKDAV-ELLNAVGLS---DAVlwlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180 190
....*....|....*....|....*....|.
gi 1319887251 174 PQaTASVLAL-LKRLRDEYQLAIVLITHEMD 203
Cdd:COG2401 169 RQ-TAKRVARnLQKLARRAGITLVVATHHYD 198
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-225 |
1.48e-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: 90.93 E-value: 1.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRTadgRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgeaLRRE 81
Cdd:cd03369 7 IEVENLSVRYAP---DLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIP---LEDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQSSALLSrRTAWENValplawlgvverDIKARVG--ELLESVGLSHKADawpaQLSGGQRQRIGIARALALR 159
Cdd:cd03369 81 RSSLTIIPQDPTLFS-GTIRSNL------------DPFDEYSdeEIYGALRVSEGGL----NLSQGQRQLLCLARALLKR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1319887251 160 PSVLLADEATSGLDPQATAsvlALLKRLRDEYQLA-IVLITHEMdavRTAA--DAVAEIRDGTIVQYGR 225
Cdd:cd03369 144 PRVLVLDEATASIDYATDA---LIQKTIREEFTNStILTIAHRL---RTIIdyDKILVMDAGEVKEYDH 206
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-232 |
2.44e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 94.75 E-value: 2.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYrtaDGRLsaVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRIngqdlsalsGEALRr 80
Cdd:COG0488 315 VLELEGLSKSY---GDKT--LLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL---------GETVK- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 erraIGTVFQSSALL-SRRTAWENVAlplawlGVVERDIKARVGELLESVGLS-HKADAWPAQLSGGQRQRIGIARALAL 158
Cdd:COG0488 380 ----IGYFDQHQEELdPDKTVLDELR------DGAPGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLS 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1319887251 159 RPSVLLADEATSGLDPQAtasvLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQY-GRIEDLLAR 232
Cdd:COG0488 450 PPNVLLLDEPTNHLDIET----LEALEEALDDFPGTVLLVSHDRYFLDRVATRILEFEDGGVREYpGGYDDYLEK 520
|
|
| MsbA_rel |
TIGR02204 |
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ... |
21-231 |
5.52e-21 |
|
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: 93.61 E-value: 5.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRErraIGTVFQSSALLSRrTA 100
Cdd:TIGR02204 355 ALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRAR---MALVPQDPVLFAA-SV 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 WENVAL--PLAWLGVVERD-IKARVGELLEsvGLSHKADAWPAQ----LSGGQRQRIGIARALALRPSVLLADEATSGLD 173
Cdd:TIGR02204 431 MENIRYgrPDATDEEVEAAaRAAHAHEFIS--ALPEGYDTYLGErgvtLSGGQRQRIAIARAILKDAPILLLDEATSALD 508
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1319887251 174 PQATASVLALLKRLRDEYQLAIvlITHEMDAVRTaADAVAEIRDGTIVQYGRIEDLLA 231
Cdd:TIGR02204 509 AESEQLVQQALETLMKGRTTLI--IAHRLATVLK-ADRIVVMDQGRIVAQGTHAELIA 563
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
13-232 |
2.57e-20 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 91.62 E-value: 2.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 13 TADGRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRErraIGTVFQSS 92
Cdd:PRK11176 350 TYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQ---VALVSQNV 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 93 ALLSRRTAwENVALplAWLGVVER-DIK--ARVGELLESV-GLSHKADAW----PAQLSGGQRQRIGIARALaLRPS-VL 163
Cdd:PRK11176 427 HLFNDTIA-NNIAY--ARTEQYSReQIEeaARMAYAMDFInKMDNGLDTVigenGVLLSGGQRQRIAIARAL-LRDSpIL 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1319887251 164 LADEATSGLDpqaTASVLALLKRLrDEYQ--LAIVLITHEMDAVRTaADAVAEIRDGTIVQYGRIEDLLAR 232
Cdd:PRK11176 503 ILDEATSALD---TESERAIQAAL-DELQknRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLAQ 568
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-229 |
2.64e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 91.83 E-value: 2.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 25 LSLQVPERSITAVVGPSGAGKSTLarcISLLEQ--PDSGSIRINGQDLSALSgeaLRRERRAIGTVFQSSALLsRRTAWE 102
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSL---LNALLGflPYQGSLKINGIELRELD---PESWRKHLSWVGQNPQLP-HGTLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 103 NVALplAWLGVVERDI-----KARVGELLESV--GLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQ 175
Cdd:PRK11174 442 NVLL--GNPDASDEQLqqaleNAWVSEFLPLLpqGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1319887251 176 ATASVLALLKRLRDeyQLAIVLITHEMDAVrTAADAVAEIRDGTIVQYGRIEDL 229
Cdd:PRK11174 520 SEQLVMQALNAASR--RQTTLMVTHQLEDL-AQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-227 |
2.90e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 86.09 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRTAdgrlSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSalsgEALRRE 81
Cdd:PRK15056 7 IVVNDVTVTWRNG----HTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 rrAIGTVFQSSAL-LSRRTAWENVAL-----PLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARA 155
Cdd:PRK15056 79 --LVAYVPQSEEVdWSFPVLVEDVVMmgrygHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1319887251 156 LALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVlITHEMDAVRTAADAVAEIRdGTIVQYGRIE 227
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLV-STHNLGSVTEFCDYTVMVK-GTVLASGPTE 226
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-200 |
3.06e-19 |
|
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: 84.33 E-value: 3.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 20 AVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEAlrreRRAIGTVFQSSALLSRRT 99
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEP----HENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 100 AWENvalpLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATAs 179
Cdd:TIGR01189 90 ALEN----LHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA- 164
|
170 180
....*....|....*....|.
gi 1319887251 180 VLALLKRLRDEYQLAIVLITH 200
Cdd:TIGR01189 165 LLAGLLRAHLARGGIVLLTTH 185
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
25-220 |
3.23e-19 |
|
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: 88.92 E-value: 3.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 25 LSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSAlsgeALRRERRAIGTVFQSSALLSRRTAWENV 104
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVRQSLGMCPQHNILFHHLTVAEHI 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 105 ALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLALL 184
Cdd:TIGR01257 1025 LFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104
|
170 180 190
....*....|....*....|....*....|....*.
gi 1319887251 185 KRLRDEYqlAIVLITHEMDAVRTAADAVAEIRDGTI 220
Cdd:TIGR01257 1105 LKYRSGR--TIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-200 |
3.24e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 88.33 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLykSYRTADGRlsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRI-NGQDLSALSgealr 79
Cdd:COG4178 362 ALALEDL--TLRTPDGR--PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLP----- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 80 reRRA---IGTVfqssallsrRTAwenVALPLAwlgvvERDIK-ARVGELLESVGLSHKAD------AWPAQLSGGQRQR 149
Cdd:COG4178 433 --QRPylpLGTL---------REA---LLYPAT-----AEAFSdAELREALEAVGLGHLAErldeeaDWDQVLSLGEQQR 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1319887251 150 IGIARALALRPSVLLADEATSGLDPQATASVLALLK-RLRDeyqLAIVLITH 200
Cdd:COG4178 494 LAFARLLLHKPDWLFLDEATSALDEENEAALYQLLReELPG---TTVISVGH 542
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
21-236 |
3.76e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 85.61 E-value: 3.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRErraIGTVFQSSALLSRRTA 100
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK---VAYLPQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 WENVAL-PLAWLGVVER---DIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQA 176
Cdd:PRK10575 103 RELVAIgRYPWHGALGRfgaADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAH 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 177 TASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLaRPDSL 236
Cdd:PRK10575 183 QVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM-RGETL 241
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-246 |
4.02e-19 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 86.78 E-value: 4.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTADGRLSAVLKgLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPD----SGSIRINGQDLSALSge 76
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDR-VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvtADRMRFDDIDLLRLS-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 77 aLRRERRAIG----TVFQSSAllSRRTAWENVALPLA------------WLGVVERdiKARVGELLESVGLSHKADA--- 137
Cdd:PRK15093 80 -PRERRKLVGhnvsMIFQEPQ--SCLDPSERVGRQLMqnipgwtykgrwWQRFGWR--KRRAIELLHRVGIKDHKDAmrs 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 138 WPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRD 217
Cdd:PRK15093 155 FPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYC 234
|
250 260
....*....|....*....|....*....
gi 1319887251 218 GTIVQYGRIEDLLARPDSLLGQQLLPLTP 246
Cdd:PRK15093 235 GQTVETAPSKELVTTPHHPYTQALIRAIP 263
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-221 |
5.46e-19 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.38 E-value: 5.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 3 AIDDLYKSYRTADGR-------LSA--VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSAL 73
Cdd:COG1129 240 ELEDLFPKRAAAPGEvvlevegLSVggVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIR 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 74 S-GEALRR-------ERRAIGtvfqssaLLSRRTAWENVALP----LAWLGVV-ERDIKARVGELLESVGL---SHKADA 137
Cdd:COG1129 320 SpRDAIRAgiayvpeDRKGEG-------LVLDLSIRENITLAsldrLSRGGLLdRRRERALAEEYIKRLRIktpSPEQPV 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 138 wpAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRD 217
Cdd:COG1129 393 --GNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMRE 469
|
....
gi 1319887251 218 GTIV 221
Cdd:COG1129 470 GRIV 473
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-218 |
1.23e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 86.52 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLARCISLLeQPD---SGSIRINGQDLSALSgeaLR-RERRAIGTVFQSSALLSR 97
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQASN---IRdTERAGIAIIHQELALVKE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 98 RTAWENVALPLAWL--GVVERD-IKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDP 174
Cdd:PRK13549 97 LSVLENIFLGNEITpgGIMDYDaMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLTE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1319887251 175 QATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDG 218
Cdd:PRK13549 177 SETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-173 |
2.00e-18 |
|
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: 86.14 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYrtaDGRLsaVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRIngqdlsalsGEALRre 81
Cdd:TIGR03719 323 IEAENLTKAF---GDKL--LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI---------GETVK-- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 rraIGTVFQS-SALLSRRTAWENVALPLAWLGVVERDIKARV---------GELLESVGlshkadawpaQLSGGQRQRIG 151
Cdd:TIGR03719 387 ---LAYVDQSrDALDPNKTVWEEISGGLDIIKLGKREIPSRAyvgrfnfkgSDQQKKVG----------QLSGGERNRVH 453
|
170 180
....*....|....*....|..
gi 1319887251 152 IARALALRPSVLLADEATSGLD 173
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLD 475
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-229 |
3.78e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 85.06 E-value: 3.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLS----ALSGEAlrrerrAIGTVFQSSALLSR 97
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpKSSQEA------GIGIIHQELNLIPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 98 RTAWENVAL----PLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLD 173
Cdd:PRK10762 94 LTIAENIFLgrefVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1319887251 174 PQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDL 229
Cdd:PRK10762 174 DTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADL 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
19-200 |
7.10e-18 |
|
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: 84.33 E-value: 7.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 19 SAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRerraIGTVFQSSALLSRR 98
Cdd:TIGR02868 348 PPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRR----RVSVCAQDAHLFDT 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 99 TAWENVAlpLAWLGVVERDikarVGELLESVGLSHKADAWP-----------AQLSGGQRQRIGIARALALRPSVLLADE 167
Cdd:TIGR02868 424 TVRENLR--LARPDATDEE----LWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDE 497
|
170 180 190
....*....|....*....|....*....|...
gi 1319887251 168 ATSGLDPQATASVLALLKRLRDEYqlAIVLITH 200
Cdd:TIGR02868 498 PTEHLDAETADELLEDLLAALSGR--TVVLITH 528
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
19-212 |
1.52e-17 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.93 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 19 SAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRingqdlsalsgealRRERRAIGTVFQSSALlsrr 98
Cdd:PRK09544 17 RRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------------RNGKLRIGYVPQKLYL---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 99 taweNVALPLAwlgvVERDI-------KARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSG 171
Cdd:PRK09544 79 ----DTTLPLT----VNRFLrlrpgtkKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1319887251 172 LDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAV 212
Cdd:PRK09544 151 VDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEV 191
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-219 |
2.72e-17 |
|
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: 77.49 E-value: 2.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYrtaDGRLsaVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIringqdlsalsgealrre 81
Cdd:cd03221 1 IELENLSKTY---GGKL--LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 rraigtvfqssallsrrtawenvalplawlgvvERDIKARVGELlesvglshkadawpAQLSGGQRQRIGIARALALRPS 161
Cdd:cd03221 58 ---------------------------------TWGSTVKIGYF--------------EQLSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1319887251 162 VLLADEATSGLDPQATASVLALLKrlrdEYQLAIVLITHEMDAVRTAADAVAEIRDGT 219
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEEALK----EYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
21-198 |
3.14e-17 |
|
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: 79.24 E-value: 3.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPD---SGSIRINGQDLSAlsgeALRRERraIGTVFQSSALLSR 97
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKP----DQFQKC--VAYVRQDDILLPG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 98 RTAWENVALPLAWLGVVERDIKARVgELLESVGLSHKADAWPA-----QLSGGQRQRIGIARALALRPSVLLADEATSGL 172
Cdd:cd03234 96 LTVRETLTYTAILRLPRKSSDAIRK-KRVEDVLLRDLALTRIGgnlvkGISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180
....*....|....*....|....*.
gi 1319887251 173 DPQATASVLALLKRLRDEYQLAIVLI 198
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILTI 200
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-229 |
6.82e-17 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 81.31 E-value: 6.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLS-ALSGEALrreRRAIGTVFQSSALLSRRTA 100
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEAL---ENGISMVHQELNLVLQRSV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 WENVAL---PLAWLGVVE----RDIKARVGELLESVGLSHKAdawpAQLSGGQRQRIGIARALALRPSVLLADEATSGLD 173
Cdd:PRK10982 91 MDNMWLgryPTKGMFVDQdkmyRDTKAIFDELDIDIDPRAKV----ATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1319887251 174 PQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDL 229
Cdd:PRK10982 167 EKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
16-256 |
1.52e-16 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 79.39 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 16 GRLSAVlKGLSLQVPERSITAVVGPSGAGKSTLArCISLLEQPDSGSiringQDLSALSGEALRRE-RRAIGTvfQSSAL 94
Cdd:NF000106 24 GEVKAV-DGVDLDVREGTVLGVLGP*GAA**RGA-LPAHV*GPDAGR-----RPWRF*TWCANRRAlRRTIG*--HRPVR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 95 LSRRTAW---ENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSG 171
Cdd:NF000106 95 *GRRESFsgrENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 172 LDPQATASVLALLKRL-RDeyQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARpdslLGQQLLPLTPAAAT 250
Cdd:NF000106 175 LDPRTRNEVWDEVRSMvRD--GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTK----VGGRTLQIRPAHAA 248
|
....*.
gi 1319887251 251 HSDLLL 256
Cdd:NF000106 249 ELDRMV 254
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
24-184 |
4.30e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 75.61 E-value: 4.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 24 GLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALsGEALRRERRAIGtvfQSSALLSRRTAWEN 103
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ-RDEYHQDLLYLG---HQPGIKTELTALEN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 104 VALPLAWLGVVERDikaRVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLAL 183
Cdd:PRK13538 95 LRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARLEAL 171
|
.
gi 1319887251 184 L 184
Cdd:PRK13538 172 L 172
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
36-198 |
4.72e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.94 E-value: 4.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 36 AVVGPSGAGKSTLARCISLLEQPD---SGSIRINGQDLSAlsgealrRERRAI-GTVFQSSALLSRRTAWEN------VA 105
Cdd:TIGR00955 55 AVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDA-------KEMRAIsAYVQQDDLFIPTLTVREHlmfqahLR 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 106 LPlAWLGVVERdiKARVGELLESVGLSHKAD---AWPAQ---LSGGQRQRIGIARALALRPSVLLADEATSGLDPQATAS 179
Cdd:TIGR00955 128 MP-RRVTKKEK--RERVDEVLQALGLRKCANtriGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFMAYS 204
|
170
....*....|....*....
gi 1319887251 180 VLALLKRLRDEYQLAIVLI 198
Cdd:TIGR00955 205 VVQVLKGLAQKGKTIICTI 223
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
15-230 |
7.39e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 76.03 E-value: 7.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 15 DGRLSavlkGLSLQVPERSITAVVGPSGAGKSTLARCISLLeQPDSGSIRINGQDLSALSGEALRReRRAIGTvfQSSAL 94
Cdd:COG4138 9 AGRLG----PISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELAR-HRAYLS--QQQSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 95 LSRRTAWENVALPLAWLGVVERDIKArVGELLESVGLSHKADAWPAQLSGGQRQRIGIARAL-----ALRPS--VLLADE 167
Cdd:COG4138 81 PFAMPVFQYLALHQPAGASSEAVEQL-LAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1319887251 168 ATSGLDPQATASVLALLKRLRDEyQLAIVLITHemDAVRTA--ADAVAEIRDGTIVQYGRIEDLL 230
Cdd:COG4138 160 PMNSLDVAQQAALDRLLRELCQQ-GITVVMSSH--DLNHTLrhADRVWLLKQGKLVASGETAEVM 221
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-219 |
1.52e-15 |
|
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: 74.04 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRTADGRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCIsLLE-QPDSGSIRINGQdlsalsgealrr 80
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-LGElEKLSGSVSVPGS------------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 erraIGTVFQSSALLSRrTAWENValplawLGVVERDiKARVGELLESVGLSHKADAWPAQ-----------LSGGQRQR 149
Cdd:cd03250 68 ----IAYVSQEPWIQNG-TIRENI------LFGKPFD-EERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQR 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1319887251 150 IGIARALALRPSVLLADEATSGLDPQaTASVL---ALLKRLRDEYqlAIVLITHEMDAVRtAADAVAEIRDGT 219
Cdd:cd03250 136 ISLARAVYSDADIYLLDDPLSAVDAH-VGRHIfenCILGLLLNNK--TRILVTHQLQLLP-HADQIVVLDNGR 204
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-173 |
1.94e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 77.08 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYrtaDGRLsaVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRIngqdlsalsGEALRre 81
Cdd:PRK11819 325 IEAENLSKSF---GDRL--LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI---------GETVK-- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 rraIGTVFQS-SALLSRRTAWENVALPLAWLGVVERDIKARV---------GELLESVGlshkadawpaQLSGGQRQRIG 151
Cdd:PRK11819 389 ---LAYVDQSrDALDPNKTVWEEISGGLDIIKVGNREIPSRAyvgrfnfkgGDQQKKVG----------VLSGGERNRLH 455
|
170 180
....*....|....*....|..
gi 1319887251 152 IARALALRPSVLLADEATSGLD 173
Cdd:PRK11819 456 LAKTLKQGGNVLLLDEPTNDLD 477
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-186 |
2.46e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 73.75 E-value: 2.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 20 AVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDlsalsgEALRRERRAIGTVFQSSALLSRRT 99
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD------IDDPDVAEACHYLGHRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 100 AWENVALPLAWLGVVERDIKArvgeLLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATAS 179
Cdd:PRK13539 90 VAENLEFWAAFLGGEELDIAA----ALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
....*..
gi 1319887251 180 VLALLKR 186
Cdd:PRK13539 166 FAELIRA 172
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
1-251 |
4.27e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 76.55 E-value: 4.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTAdgrLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALsgeALRR 80
Cdd:PLN03232 1234 SIKFEDVHLRYRPG---LPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKF---GLTD 1307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 ERRAIGTVFQSSALLSrRTAWENVAlPLA-------WLGVVERDIKARVGEllESVGLSHKADAWPAQLSGGQRQRIGIA 153
Cdd:PLN03232 1308 LRRVLSIIPQSPVLFS-GTVRFNID-PFSehndadlWEALERAHIKDVIDR--NPFGLDAEVSEGGENFSVGQRQLLSLA 1383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 154 RALALRPSVLLADEATSGLDPQATasvlALLKR-LRDEYQ-LAIVLITHEMDAVrTAADAVAEIRDGTIVQYGRIEDLLA 231
Cdd:PLN03232 1384 RALLRRSKILVLDEATASVDVRTD----SLIQRtIREEFKsCTMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQELLS 1458
|
250 260
....*....|....*....|
gi 1319887251 232 RPDSLLGQQLLPLTPAAATH 251
Cdd:PLN03232 1459 RDTSAFFRMVHSTGPANAQY 1478
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
15-200 |
6.91e-15 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 72.14 E-value: 6.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 15 DGRlsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEAlrreRRAIGTVFQSSAL 94
Cdd:cd03231 11 DGR--ALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSI----ARGLLYLGHAPGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 95 LSRRTAWENvalpLAWLGVVERDikARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDp 174
Cdd:cd03231 85 KTTLSVLEN----LRFWHADHSD--EQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD- 157
|
170 180
....*....|....*....|....*...
gi 1319887251 175 qaTASVLALLKRLRDEYQL--AIVLITH 200
Cdd:cd03231 158 --KAGVARFAEAMAGHCARggMVVLTTH 183
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
21-233 |
1.08e-14 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 74.75 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRReRRAIgtVFQSSALLSRRTA 100
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRS-RLAV--VSQTPFLFSDTVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 wENVAL--PLAWLGVVERdiKARVGELLESV-----GLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLD 173
Cdd:PRK10789 407 -NNIALgrPDATQQEIEH--VARLASVHDDIlrlpqGYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVD 483
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 174 PQATASVLALLKRLRDeyQLAIVLITHEMDAVrTAADAVAEIRDGTIVQYGRIEDLLARP 233
Cdd:PRK10789 484 GRTEHQILHNLRQWGE--GRTVIISAHRLSAL-TEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-218 |
1.22e-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: 74.48 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDS--GSIRINGQDLSALSgeALRRERRAIGTVFQSSALLSRRT 99
Cdd:TIGR02633 17 LDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASN--IRDTERAGIVIIHQELTLVPELS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 100 AWENVAL--PLAWLGVVERD--IKARVGELLESVGLSHKADAWP-AQLSGGQRQRIGIARALALRPSVLLADEATSGLDP 174
Cdd:TIGR02633 95 VAENIFLgnEITLPGGRMAYnaMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILDEPSSSLTE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1319887251 175 QATASVLALLKRLRdEYQLAIVLITHEMDAVRTAADAVAEIRDG 218
Cdd:TIGR02633 175 KETEILLDIIRDLK-AHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
4-237 |
1.40e-14 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 74.54 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 4 IDDLYksYRTADGRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQdlSALSgealrrerr 83
Cdd:PRK13545 24 LKDLF--FRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS--AALI--------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 84 AIgtvfqSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVL 163
Cdd:PRK13545 91 AI-----SSGLNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDIL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1319887251 164 LADEATSGLDPQATASVLALLKRLRDEYQlAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSLL 237
Cdd:PRK13545 166 VIDEALSVGDQTFTKKCLDKMNEFKEQGK-TIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHYDEFL 238
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-222 |
2.13e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 73.67 E-value: 2.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDS--GSIRINGQ-----DLSAlsgealrRERRAIGTVFQSSAL 94
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEvcrfkDIRD-------SEALGIVIIHQELAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 95 LSRRTAWENVAL--PLAWLGVVERD-IKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSG 171
Cdd:NF040905 90 IPYLSIAENIFLgnERAKRGVIDWNeTNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1319887251 172 LDPQATASVLALLKRLRDEYQLAIvLITHEMDAVRTAADAVAEIRDGTIVQ 222
Cdd:NF040905 170 LNEEDSAALLDLLLELKAQGITSI-IISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
21-259 |
4.74e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.99 E-value: 4.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDS--GSIRINGQDLSAlsgEALRRerraIGTVFQSSALLSRR 98
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK---QILKR----TGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 99 TAWENVA------LPLAwlgvVERDIKARVGE-LLESVGLSH-----KADAWPAQLSGGQRQRIGIARALALRPSVLLAD 166
Cdd:PLN03211 156 TVRETLVfcsllrLPKS----LTKQEKILVAEsVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILD 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 167 EATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDSLLGQQLLPLTP 246
Cdd:PLN03211 232 EPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSDAMAYFESVGFSPSFPMNP 311
|
250
....*....|...
gi 1319887251 247 AaathsDLLLRLS 259
Cdd:PLN03211 312 A-----DFLLDLA 319
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-219 |
5.00e-14 |
|
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: 70.05 E-value: 5.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 20 AVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALR-RERRAIGTVFQSSALLSRr 98
Cdd:cd03290 15 ATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsRNRYSVAYAAQKPWLLNA- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 99 TAWENVAL--PLAwlgvverdiKARVGELLESVGLSHKADAWP-----------AQLSGGQRQRIGIARALALRPSVLLA 165
Cdd:cd03290 94 TVEENITFgsPFN---------KQRYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARALYQNTNIVFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1319887251 166 DEATSGLDPQATASVL--ALLKRLRDEYQlAIVLITHEMDAVrTAADAVAEIRDGT 219
Cdd:cd03290 165 DDPFSALDIHLSDHLMqeGILKFLQDDKR-TLVLVTHKLQYL-PHADWIIAMKDGS 218
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
21-227 |
9.01e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 70.06 E-value: 9.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISllEQPD----SGSIRINGQDLSALSGEAlrRERRAIGTVFQ------ 90
Cdd:CHL00131 22 ILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIA--GHPAykilEGDILFKGESILDLEPEE--RAHLGIFLAFQypieip 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 91 --------SSALLSRRTAWENVAL-PLAWLGVVErdikarvgELLESVGLShkadawPAQL--------SGGQRQRIGIA 153
Cdd:CHL00131 98 gvsnadflRLAYNSKRKFQGLPELdPLEFLEIIN--------EKLKLVGMD------PSFLsrnvnegfSGGEKKRNEIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1319887251 154 RALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQlAIVLITHE---MDAVRtaADAVAEIRDGTIVQYGRIE 227
Cdd:CHL00131 164 QMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITHYqrlLDYIK--PDYVHVMQNGKIIKTGDAE 237
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-236 |
1.07e-13 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 72.37 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLarcISLL------------------------EQPDSGSIRIN---------- 66
Cdd:PTZ00265 1183 IYKDLTFSCDSKKTTAIVGETGSGKSTV---MSLLmrfydlkndhhivfknehtndmtnEQDYQGDEEQNvgmknvnefs 1259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 67 -------GQDLSAL--SGEALR----------RERRAIGTVFQSSALLSRRTAWENVALPL--AWLGVVERDIK-ARVGE 124
Cdd:PTZ00265 1260 ltkeggsGEDSTVFknSGKILLdgvdicdynlKDLRNLFSIVSQEPMLFNMSIYENIKFGKedATREDVKRACKfAAIDE 1339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 125 LLESVGLSHKADAWP--AQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEM 202
Cdd:PTZ00265 1340 FIESLPNKYDTNVGPygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRI 1419
|
250 260 270
....*....|....*....|....*....|....*...
gi 1319887251 203 DAVRTAADAVA---EIRDGTIVQ-YGRIEDLLARPDSL 236
Cdd:PTZ00265 1420 ASIKRSDKIVVfnnPDRTGSFVQaHGTHEELLSVQDGV 1457
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
33-201 |
1.10e-13 |
|
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: 68.81 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 33 SITAVVGPSGAGKSTLARCISLLEQPD--SGSIRINGQDLsalsGEALRRErraIGTVFQSSALLSRRTawenvalplaw 110
Cdd:cd03232 34 TLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPL----DKNFQRS---TGYVEQQDVHSPNLT----------- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 111 lgvverdikarVGELLEsvgLShkadAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDE 190
Cdd:cd03232 96 -----------VREALR---FS----ALLRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS 157
|
170
....*....|.
gi 1319887251 191 YQlAIVLITHE 201
Cdd:cd03232 158 GQ-AILCTIHQ 167
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
13-230 |
1.15e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 69.58 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 13 TADGRLSAvlkgLSLQVPERSITAVVGPSGAGKSTLARCISLLeQPDSGSIRINGQDLSALSGEALRRERraiGTVFQSS 92
Cdd:PRK03695 7 AVSTRLGP----LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHR---AYLSQQQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 93 ALLSRRTAWENVALPLAwLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARAL-----ALRPS--VLLA 165
Cdd:PRK03695 79 TPPFAMPVFQYLTLHQP-DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqLLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1319887251 166 DEATSGLDPQATASVLALLKRLRdEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLL 230
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVL 221
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
25-220 |
3.80e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 70.08 E-value: 3.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 25 LSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgealRRERRAIGTVF-----QSSAL-LSRR 98
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS----TAQRLARGLVYlpedrQSSGLyLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 99 TAWENVALPLAWLGVVERDIK--ARVGELLESVG--LSHkADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDP 174
Cdd:PRK15439 358 LAWNVCALTHNRRGFWIKPARenAVLERYRRALNikFNH-AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1319887251 175 QATASVLALLKRLRdEYQLAIVLITHEMDAVRTAADAVAEIRDGTI 220
Cdd:PRK15439 437 SARNDIYQLIRSIA-AQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
22-224 |
8.88e-13 |
|
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: 66.13 E-value: 8.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPD---SGSIRINGQDlsalSGEALRRERRAIgtVFqssallsrr 98
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIP----YKEFAEKYPGEI--IY--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 99 tawenvalplawlgVVERDIKAR---VGELLESVgLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDpq 175
Cdd:cd03233 88 --------------VSEEDVHFPtltVRETLDFA-LRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD-- 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1319887251 176 aTASVLALLKRLRdeyqlaivLITHEMDAVRTAA------------DAVAEIRDGTIVQYG 224
Cdd:cd03233 151 -SSTALEILKCIR--------TMADVLKTTTFVSlyqasdeiydlfDKVLVLYEGRQIYYG 202
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
8-237 |
1.62e-12 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 66.76 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 8 YKSYRTADGRLSAV------------LKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGqDLSALsg 75
Cdd:PRK13546 14 YRIYRTNKERMKDAlipkhknktffaLDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVI-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 76 ealrrerrAIgtvfqSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARA 155
Cdd:PRK13546 91 --------AI-----SAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSIN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 156 LALRPSVLLADEATSGLDPQATASVLALLKRLRdEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLARPDS 235
Cdd:PRK13546 158 ITVNPDILVIDEALSVGDQTFAQKCLDKIYEFK-EQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPKYEA 236
|
..
gi 1319887251 236 LL 237
Cdd:PRK13546 237 FL 238
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
21-221 |
2.93e-12 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 65.67 E-value: 2.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRErrAIGTVFQSSALLSRRTA 100
Cdd:PRK11614 20 ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMRE--AVAIVPEGRRVFSRMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 WENVALP--LAWLGVVERDIKaRVGELLESvgLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATA 178
Cdd:PRK11614 98 EENLAMGgfFAERDQFQERIK-WVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1319887251 179 SVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTIV 221
Cdd:PRK11614 175 QIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
21-208 |
2.95e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 67.75 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINgqDLSALSGEALRRERRAIGTVFQSSALLSRRTA 100
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWRSKIGVVSQDPLLFSNSIK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 wENVALPLAWLGVVE--------------RDIKARVG-------------------ELLES------------VGLSHKA 135
Cdd:PTZ00265 478 -NNIKYSLYSLKDLEalsnyynedgndsqENKNKRNScrakcagdlndmsnttdsnELIEMrknyqtikdsevVDVSKKV 556
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 136 ------DAWP-----------AQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLI 198
Cdd:PTZ00265 557 lihdfvSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIII 636
|
250
....*....|
gi 1319887251 199 THEMDAVRTA 208
Cdd:PTZ00265 637 AHRLSTIRYA 646
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
21-214 |
1.06e-11 |
|
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: 65.73 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQ-VPERSItAVVGPSGAGKSTLARCISLLEQPdsgsiringqdlsaLSGEALRRERRAIGTVFQSSALLSRRT 99
Cdd:TIGR03719 20 ILKDISLSfFPGAKI-GVLGLNGAGKSTLLRIMAGVDKD--------------FNGEARPQPGIKVGYLPQEPQLDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 100 AWENVALPLA-WLGVVER--DIKARVGE-------LLESVG-LSHKADAWPA------------------------QLSG 144
Cdd:TIGR03719 85 VRENVEEGVAeIKDALDRfnEISAKYAEpdadfdkLAAEQAeLQEIIDAADAwdldsqleiamdalrcppwdadvtKLSG 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 145 GQRQRIGIARALALRPSVLLADEATSGLDpqatASVLALLKRLRDEYQLAIVLITHEmdavRTAADAVAE 214
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTHD----RYFLDNVAG 226
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-288 |
1.19e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.91 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRTadgRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALsgeALRRE 81
Cdd:PLN03130 1238 IKFEDVVLRYRP---ELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKF---GLMDL 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQSSALLSRRTA--------------WEnvALPLAWL-GVVERDikarvgelleSVGLSHKADAWPAQLSGGQ 146
Cdd:PLN03130 1312 RKVLGIIPQAPVLFSGTVRfnldpfnehndadlWE--SLERAHLkDVIRRN----------SLGLDAEVSEAGENFSVGQ 1379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 147 RQRIGIARALALRPSVLLADEATSGLDPQATASVlalLKRLRDEYQLAIVL-ITHEMDAVrTAADAVAEIRDGTIVQYGR 225
Cdd:PLN03130 1380 RQLLSLARALLRRSKILVLDEATAAVDVRTDALI---QKTIREEFKSCTMLiIAHRLNTI-IDCDRILVLDAGRVVEFDT 1455
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1319887251 226 IEDLLARPDSLLGQQLLPLTPAAATHsdlLLRLSYRWDVPVATD-----------WI--SR--LSQQWALQIDLLGGH 288
Cdd:PLN03130 1456 PENLLSNEGSAFSKMVQSTGAANAQY---LRSLVFGGDEDRLAReeskaldgqrkWLasSRwaAAAQFALAVSLTSSQ 1530
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-200 |
1.22e-11 |
|
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: 62.17 E-value: 1.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLykSYRTADGRLsaVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRIngqdlsalsgeaLRRE 81
Cdd:cd03223 1 IELENL--SLATPDGRV--LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM------------PEGE 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RraigtvfqsSALLSRRTAwenvaLPLawlgvverdikarvGELLESVglshkADAWPAQLSGGQRQRIGIARALALRPS 161
Cdd:cd03223 65 D---------LLFLPQRPY-----LPL--------------GTLREQL-----IYPWDDVLSGGEQQRLAFARLLLHKPK 111
|
170 180 190
....*....|....*....|....*....|....*....
gi 1319887251 162 VLLADEATSGLDPQATASVLALLKRLRdeyqLAIVLITH 200
Cdd:cd03223 112 FVFLDEATSALDEESEDRLYQLLKELG----ITVISVGH 146
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-238 |
1.90e-11 |
|
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: 63.39 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYrtaDGRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLA----RCISLLEqpdsGSIRINGQDLSALSGEA 77
Cdd:cd03288 20 IKIHDLCVRY---ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSlaffRMVDIFD----GKIVIDGIDISKLPLHT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 78 LRrERRAIgtVFQSSALLS--------------RRTAWEnvALPLAWLGVVerdIKARVGellesvGLSHKADAWPAQLS 143
Cdd:cd03288 93 LR-SRLSI--ILQDPILFSgsirfnldpeckctDDRLWE--ALEIAQLKNM---VKSLPG------GLDAVVTEGGENFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 144 GGQRQRIGIARALALRPSVLLADEATSGLDpQATASVL--ALLKRLRDEyqlAIVLITHEMDAVRTaADAVAEIRDGTIV 221
Cdd:cd03288 159 VGQRQLFCLARAFVRKSSILIMDEATASID-MATENILqkVVMTAFADR---TVVTIAHRVSTILD-ADLVLVLSRGILV 233
|
250
....*....|....*..
gi 1319887251 222 QYGRIEDLLARPDSLLG 238
Cdd:cd03288 234 ECDTPENLLAQEDGVFA 250
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
39-202 |
2.47e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 64.76 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 39 GPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEAlrreRRAIGTVFQSSALLSRRTAWENVALPLAWLGVVERDI 118
Cdd:NF033858 299 GSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIAT----RRRVGYMSQAFSLYGELTVRQNLELHARLFHLPAAEI 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 119 KARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLI 198
Cdd:NF033858 375 AARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFIS 454
|
....
gi 1319887251 199 THEM 202
Cdd:NF033858 455 THFM 458
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
18-251 |
4.94e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.03 E-value: 4.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 18 LSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRERRAI--------GTVF 89
Cdd:PTZ00243 1322 LPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIpqdpvlfdGTVR 1401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 90 QSSALLSRRTAWEnVALPLAWLGVVErdikaRVGEllESVGLSHKADAWPAQLSGGQRQRIGIARALALRPS-VLLADEA 168
Cdd:PTZ00243 1402 QNVDPFLEASSAE-VWAALELVGLRE-----RVAS--ESEGIDSRVLEGGSNYSVGQRQLMCMARALLKKGSgFILMDEA 1473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 169 TSGLDP----QATASVLALLKrlrdeyQLAIVLITHEMDAVrTAADAVAEIRDGTIVQYGRIEDLLARPDSLLGQQLLPL 244
Cdd:PTZ00243 1474 TANIDPaldrQIQATVMSAFS------AYTVITIAHRLHTV-AQYDKIIVMDHGAVAEMGSPRELVMNRQSIFHSMVEAL 1546
|
....*..
gi 1319887251 245 TPAAATH 251
Cdd:PTZ00243 1547 GRSEAKR 1553
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
17-230 |
5.43e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 62.15 E-value: 5.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 17 RLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCIS--LLEQPDSGSIRI------NGQDLSALSGEALRRERRAIGTV 88
Cdd:PRK13547 12 RHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdLTGGGAPRGARVtgdvtlNGEPLAAIDAPRLARLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 89 FQSSALLSRRtawENVAL---PLAW----LGVVERDIKARVGELLESVGLSHKAdawPAQLSGGQRQRIGIARALA---- 157
Cdd:PRK13547 92 AQPAFAFSAR---EIVLLgryPHARragaLTHRDGEIAWQALALAGATALVGRD---VTTLSGGELARVQFARVLAqlwp 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1319887251 158 -----LRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLL 230
Cdd:PRK13547 166 phdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVL 243
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-229 |
7.60e-11 |
|
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: 63.49 E-value: 7.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYrtaDGRLSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEAlrr 80
Cdd:TIGR01257 1937 ILRLNELTKVY---SGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDV--- 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 eRRAIGTVFQSSALLSRRTAWENVALPLAWLGVVERDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRP 160
Cdd:TIGR01257 2011 -HQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCP 2089
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1319887251 161 SVLLADEATSGLDPQATA----SVLALLKRLRdeyqlAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDL 229
Cdd:TIGR01257 2090 PLVLLDEPTTGMDPQARRmlwnTIVSIIREGR-----AVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
58-241 |
8.33e-11 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 63.11 E-value: 8.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 58 PDSGSIRINGQDLSALSGEALRRERRaigtVFQSSALLSRRtawENVALPlawlgvVERDIKARVGELLEsVGLSHKADA 137
Cdd:TIGR00630 418 PEALAVTVGGKSIADVSELSIREAHE----FFNQLTLTPEE---KKIAEE------VLKEIRERLGFLID-VGLDYLSLS 483
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 138 WPAQ-LSGGQRQRIGIARAL--ALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVlITHEMDAVRtAADAV-- 212
Cdd:TIGR00630 484 RAAGtLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIV-VEHDEDTIR-AADYVid 561
|
170 180 190
....*....|....*....|....*....|...
gi 1319887251 213 ----AEIRDGTIVQYGRIEDLLARPDSLLGQQL 241
Cdd:TIGR00630 562 igpgAGEHGGEVVASGTPEEILANPDSLTGQYL 594
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-224 |
9.75e-11 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 61.35 E-value: 9.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 1 MIAIDDLYKSYRTadgrlSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLE--QPDSGSIRINGQDLSALSGEal 78
Cdd:PRK09580 1 MLSIKDLHVSVED-----KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPE-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 79 RRERRAIGTVFQ--------------SSALLSRRTAWENVALP-LAWLGVVERDI---KARVGELLESVGLShkadawpa 140
Cdd:PRK09580 74 DRAGEGIFMAFQypveipgvsnqfflQTALNAVRSYRGQEPLDrFDFQDLMEEKIallKMPEDLLTRSVNVG-------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 141 qLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQlAIVLITHE---MDAVRtaADAVAEIRD 217
Cdd:PRK09580 146 -FSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKR-SFIIVTHYqriLDYIK--PDYVHVLYQ 221
|
....*..
gi 1319887251 218 GTIVQYG 224
Cdd:PRK09580 222 GRIVKSG 228
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
23-222 |
9.85e-11 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 62.49 E-value: 9.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 23 KGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSgeALRRERRAIGTVFQS---SALLSRRT 99
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRS--PLDAVKKGMAYITESrrdNGFFPNFS 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 100 AWENVAlplawlgvVERDIKarVGELLESVGL-SHKADAWPAQ-------------------LSGGQRQRIGIARALALR 159
Cdd:PRK09700 358 IAQNMA--------ISRSLK--DGGYKGAMGLfHEVDEQRTAEnqrellalkchsvnqniteLSGGNQQKVLISKWLCCC 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1319887251 160 PSVLLADEATSGLDPQATASVLALLKRLRDEYQlAIVLITHEMDAVRTAADAVAEIRDGTIVQ 222
Cdd:PRK09700 428 PEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGK-VILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
34-205 |
1.01e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 63.20 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 34 ITAVVGPSGAGKSTLARCISllEQPDSGSIR-----INGQDLSAlsgealrRERRAIGTVFQSSALLSRRTAWENVALPl 108
Cdd:TIGR00956 791 LTALMGASGAGKTTLLNVLA--ERVTTGVITggdrlVNGRPLDS-------SFQRSIGYVQQQDLHLPTSTVRESLRFS- 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 109 AWL---GVVERDIKAR-VGELLESVGLSHKADAW---PAQ-LSGGQRQRIGIARALALRPSVLL-ADEATSGLDPQATAS 179
Cdd:TIGR00956 861 AYLrqpKSVSKSEKMEyVEEVIKLLEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWS 940
|
170 180
....*....|....*....|....*.
gi 1319887251 180 VLALLKRLRDEYQlAIVLITHEMDAV 205
Cdd:TIGR00956 941 ICKLMRKLADHGQ-AILCTIHQPSAI 965
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-231 |
1.25e-10 |
|
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: 62.66 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 18 LSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRERRAI--GTVFQSSALL 95
Cdd:TIGR00957 1298 LDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIpqDPVLFSGSLR 1377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 96 SRRTAWENVALPLAWLGVVERDIKARVGELLEsvGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQ 175
Cdd:TIGR00957 1378 MNLDPFSQYSDEEVWWALELAHLKTFVSALPD--KLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVDLE 1455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1319887251 176 ATASVLAllkRLRDEYQLAIVL-ITHE----MDAVRtaadaVAEIRDGTIVQYGRIEDLLA 231
Cdd:TIGR00957 1456 TDNLIQS---TIRTQFEDCTVLtIAHRlntiMDYTR-----VIVLDKGEVAEFGAPSNLLQ 1508
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
30-216 |
3.00e-10 |
|
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: 58.14 E-value: 3.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 30 PERSITAVVGPSGAGKSTLARCISLleqpdsgsiringqdlsALSGEALRRERRaigtvfqssallsrrtawenvalpla 109
Cdd:cd03227 19 GEGSLTIITGPNGSGKSTILDAIGL-----------------ALGGAQSATRRR-------------------------- 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 110 wLGVVERDIKARVGelLESVGLSHkadawpaQLSGGQRQRIGIARALAL-----RPSVLLaDEATSGLDPQATASVLALL 184
Cdd:cd03227 56 -SGVKAGCIVAAVS--AELIFTRL-------QLSGGEKELSALALILALaslkpRPLYIL-DEIDRGLDPRDGQALAEAI 124
|
170 180 190
....*....|....*....|....*....|..
gi 1319887251 185 KRLRDEYQLAIVlITHEMDavrTAADAVAEIR 216
Cdd:cd03227 125 LEHLVKGAQVIV-ITHLPE---LAELADKLIH 152
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
22-190 |
4.59e-10 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 60.91 E-value: 4.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLarcISLLeqpdSGSIRINGQDLSALSGE-ALRRERRAIGtvfqssallsRRTA 100
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSL---LSLI----AGARKIQQGRVEVLGGDmADARHRRAVC----------PRIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 W----------------ENVAL--PLAWLGVVERDikARVGELLESVGLSHKADAwPA-QLSGGQRQRIGIARALALRPS 161
Cdd:NF033858 80 YmpqglgknlyptlsvfENLDFfgRLFGQDAAERR--RRIDELLRATGLAPFADR-PAgKLSGGMKQKLGLCCALIHDPD 156
|
170 180
....*....|....*....|....*....
gi 1319887251 162 VLLADEATSGLDPQATASVLALLKRLRDE 190
Cdd:NF033858 157 LLILDEPTTGVDPLSRRQFWELIDRIRAE 185
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
37-232 |
7.13e-10 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 59.99 E-value: 7.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 37 VVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSAlsgEALRRERRAIGTVFQSSALLSRRTAWENVALPlawlgvver 116
Cdd:PRK10522 354 LIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTA---EQPEDYRKLFSAVFTDFHLFDQLLGPEGKPAN--------- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 117 diKARVGELLESVGLSHKAD-----AWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASV-LALLKRLRDE 190
Cdd:PRK10522 422 --PALVEKWLERLKMAHKLEledgrISNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREFyQVLLPLLQEM 499
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1319887251 191 YQlAIVLITHEmDAVRTAADAVAEIRDGTIVQ-YGRIEDLLAR 232
Cdd:PRK10522 500 GK-TIFAISHD-DHYFIHADRLLEMRNGQLSElTGEERDAASR 540
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
38-223 |
7.20e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.96 E-value: 7.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 38 VGPSGAGKSTLARCISLLEQPDSGSIRINgQDL--SALSGEALRRERraiGTVF---------QSSAL-----LSRRTAW 101
Cdd:PRK11147 35 VGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLivARLQQDPPRNVE---GTVYdfvaegieeQAEYLkryhdISHLVET 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 102 ENVALPLAWLGVVERDI--------KARVGELLESVGLShkADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLD 173
Cdd:PRK11147 111 DPSEKNLNELAKLQEQLdhhnlwqlENRINEVLAQLGLD--PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1319887251 174 PQATASVLALLKrlrdEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQY 223
Cdd:PRK11147 189 IETIEWLEGFLK----TFQGSIIFISHDRSFIRNMATRIVDLDRGKLVSY 234
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-227 |
8.12e-10 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 56.61 E-value: 8.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 32 RSITAVVGPSGAGKSTLARCIS-LLEQPDSGSIRINGQDLSALSGEALRRERRAIGtvfqssallsrrtawenvalplaw 110
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALArELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGK------------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 111 lgvverdikarvgellesvglshkadawPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLAL-----LK 185
Cdd:smart00382 58 ----------------------------KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLL 109
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1319887251 186 RLRDEYQLAIVLITHEMDAVRtaaDAVAEIRDGTIVQYGRIE 227
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLG---PALLRRRFDRRIVLLLIL 148
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
37-175 |
9.34e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 57.94 E-value: 9.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 37 VVGPSGAGKSTLARCISLLEQPDSGSIRINGQdlsalsgEALRRER-RAIGTVFQSSALLSRRTAWENVALPLAWLGvve 115
Cdd:PRK13543 42 VQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK-------TATRGDRsRFMAYLGHLPGLKADLSTLENLHFLCGLHG--- 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1319887251 116 RDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARaLALRPSVL-LADEATSGLDPQ 175
Cdd:PRK13543 112 RRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPAPLwLLDEPYANLDLE 171
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
22-226 |
3.82e-09 |
|
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: 56.11 E-value: 3.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLA---------------------RCISLLEQPD-------SGSIRINGQDLSal 73
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDvdsieglSPAIAIDQKTTS-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 74 sgealRRERRAIGTVFQSSALLsrRTAWENVAlplawlgvverdIKARVGELLEsVGLSH-KADAWPAQLSGGQRQRIGI 152
Cdd:cd03270 89 -----RNPRSTVGTVTEIYDYL--RLLFARVG------------IRERLGFLVD-VGLGYlTLSRSAPTLSGGEAQRIRL 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1319887251 153 ARAL--ALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQlAIVLITHEMDAVRtAADAVAEIRDGTIVQYGRI 226
Cdd:cd03270 149 ATQIgsGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHDEDTIR-AADHVIDIGPGAGVHGGEI 222
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
22-226 |
7.18e-09 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 54.64 E-value: 7.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLArcislleqpdsgsiringqdlsaLSGEALRRERRAIGTvfqssallsrrtaw 101
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV-----------------------NEGLYASGKARLISF-------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 102 envaLPLAwlgvvERDIKARVGEL--LESVGLSHKADAWPAQ-LSGGQRQRIGIARALALRP--SVLLADEATSGLDPQA 176
Cdd:cd03238 54 ----LPKF-----SRNKLIFIDQLqfLIDVGLGYLTLGQKLStLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQD 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1319887251 177 TASVLALLKRLRDEYQlAIVLITHEMDAVRTaADAVAEIRDGTIVQYGRI 226
Cdd:cd03238 125 INQLLEVIKGLIDLGN-TVILIEHNLDVLSS-ADWIIDFGPGSGKSGGKV 172
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
37-223 |
1.15e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.33 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 37 VVGPSGAGKSTLarcISLLE---QPDSGSIRING--------QDLSALSGEALR------RERRAIGTVFQSSALLSRRT 99
Cdd:PRK10636 32 LVGKNGCGKSTL---LALLKneiSADGGSYTFPGnwqlawvnQETPALPQPALEyvidgdREYRQLEAQLHDANERNDGH 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 100 AWENVALPL----AWlgvverDIKARVGELLESVGLSHKADAWPAQ-LSGGQRQRIGIARALALRPSVLLADEATSGLDP 174
Cdd:PRK10636 109 AIATIHGKLdaidAW------TIRSRAASLLHGLGFSNEQLERPVSdFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1319887251 175 QAtasVLALLKRLRDeYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQY 223
Cdd:PRK10636 183 DA---VIWLEKWLKS-YQGTLILISHDRDFLDPIVDKIIHIEQQSLFEY 227
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-244 |
1.17e-08 |
|
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: 56.84 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 4 IDDLYKSYrTADGRlsAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDsGSIRINGQDLSALSgeaLRRERR 83
Cdd:TIGR01271 1220 VQGLTAKY-TEAGR--AVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVT---LQTWRK 1292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 84 AIGTVFQSSALLSRrTAWENvalplawLGVVERDIKARVGELLESVGLSHKADAWPAQL-----------SGGQRQRIGI 152
Cdd:TIGR01271 1293 AFGVIPQKVFIFSG-TFRKN-------LDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCL 1364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 153 ARALALRPSVLLADEATSGLDPqatASVLALLKRLRDEY-QLAIVLITHEMDAVRTAADAVAeIRDGTIVQYGRIEDLLA 231
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDP---VTLQIIRKTLKQSFsNCTVILSEHRVEALLECQQFLV-IEGSSVKQYDSIQKLLN 1440
|
250
....*....|...
gi 1319887251 232 RPdSLLGQQLLPL 244
Cdd:TIGR01271 1441 ET-SLFKQAMSAA 1452
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-231 |
1.47e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.05 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 4 IDDLYKSYrtaDGRLsaVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINgqdlsalsgealrrERR 83
Cdd:PRK15064 322 VENLTKGF---DNGP--LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS--------------ENA 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 84 AIGTVFQSSAllsrrTAWENVALPLAWLGV--VERD----IKARVGELLES---VGLSHKAdawpaqLSGGQRQRIGIAR 154
Cdd:PRK15064 383 NIGYYAQDHA-----YDFENDLTLFDWMSQwrQEGDdeqaVRGTLGRLLFSqddIKKSVKV------LSGGEKGRMLFGK 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1319887251 155 ALALRPSVLLADEATSGLDPQATASV-LALlkrlrDEYQLAIVLITHEMDAVRTAADAVAEIRDGTIVQY-GRIEDLLA 231
Cdd:PRK15064 452 LMMQKPNVLVMDEPTNHMDMESIESLnMAL-----EKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDFsGTYEEYLR 525
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
27-239 |
1.70e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.79 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 27 LQVPERSIT-----AVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALSGEALRRerrAIGTVFQ--SSALLSR-- 97
Cdd:PRK10938 19 LQLPSLTLNagdswAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQK---LVSDEWQrnNTDMLSPge 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 98 ----RTAWEnvalplawlgVVERDIK--ARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSG 171
Cdd:PRK10938 96 ddtgRTTAE----------IIQDEVKdpARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDG 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1319887251 172 LDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTIVQYGRIEDLLArpDSLLGQ 239
Cdd:PRK10938 166 LDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQ--QALVAQ 230
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
142-220 |
2.92e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 55.01 E-value: 2.92e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1319887251 142 LSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTI 220
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
21-200 |
3.97e-08 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 3.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQ-VPERSItAVVGPSGAGKSTLARCISLLEQPdsgsiringqdlsaLSGEALRRERRAIGTVFQSSALLSRRT 99
Cdd:PRK11819 22 ILKDISLSfFPGAKI-GVLGLNGAGKSTLLRIMAGVDKE--------------FEGEARPAPGIKVGYLPQEPQLDPEKT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 100 AWENVALplawlGVVE-RDIKARVGE--------------LLESVG-----LSHkADAW---------------P----- 139
Cdd:PRK11819 87 VRENVEE-----GVAEvKAALDRFNEiyaayaepdadfdaLAAEQGelqeiIDA-ADAWdldsqleiamdalrcPpwdak 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1319887251 140 -AQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQataSVLALLKRLRDeYQLAIVLITH 200
Cdd:PRK11819 161 vTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE---SVAWLEQFLHD-YPGTVVAVTH 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-232 |
4.59e-08 |
|
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: 54.95 E-value: 4.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTLARciSLLEQPD--SGSIRINGQ-----DLSALSGEALRrERRAIGTVFQSSAL 94
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLS--ALLAEMDkvEGHVHMKGSvayvpQQAWIQNDSLR-ENILFGKALNEKYY 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 95 lsrRTAWENVALpLAWLGVVERDIKARVGEllesVGLShkadawpaqLSGGQRQRIGIARALALRPSVLLADEATSGLDP 174
Cdd:TIGR00957 731 ---QQVLEACAL-LPDLEILPSGDRTEIGE----KGVN---------LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA 793
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1319887251 175 QATA----SVLALLKRLRDEYQlaiVLITHEMDAVrTAADAVAEIRDGTIVQYGRIEDLLAR 232
Cdd:TIGR00957 794 HVGKhifeHVIGPEGVLKNKTR---ILVTHGISYL-PQVDVIIVMSGGKISEMGSYQELLQR 851
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
17-201 |
5.48e-08 |
|
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: 53.18 E-value: 5.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 17 RLSAVLKGLSLQVPERSIT-----AVVGPSGAGKSTLARCISLLEQPDSGSIrinGQDLSALSGEALRRERRAIGTVfqs 91
Cdd:cd03237 5 TMKKTLGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDTVSYKPQYIKADYEGTV--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 92 SALLSRRTA-------WEN-VALPLAWLGVVERdikarvgELLEsvglshkadawpaqLSGGQRQRIGIARALALRPSVL 163
Cdd:cd03237 79 RDLLSSITKdfythpyFKTeIAKPLQIEQILDR-------EVPE--------------LSGGELQRVAIAACLSKDADIY 137
|
170 180 190
....*....|....*....|....*....|....*...
gi 1319887251 164 LADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHE 201
Cdd:cd03237 138 LLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHD 175
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
21-220 |
7.60e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 54.10 E-value: 7.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRingqdLSALSGEALRRERRAIGTVFQSSALLSRRTA 100
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF-----RSAKVRMAVFSQHHVDGLDLSSNPLLYMMRC 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 WEnvalplawlGVVERDIKARVGelleSVGLSHKADAWPA-QLSGGQRQRIGIARALALRPSVLLADEATSGLDPQAtas 179
Cdd:PLN03073 599 FP---------GVPEQKLRAHLG----SFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDA--- 662
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1319887251 180 VLALLKRLRdEYQLAIVLITHEMDAVRTAADAVAEIRDGTI 220
Cdd:PLN03073 663 VEALIQGLV-LFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
25-220 |
2.50e-07 |
|
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: 52.13 E-value: 2.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 25 LSLQVPERSITAVVGPSGAGKSTLARCI-SLLEQPDSGSIRINGQDLSALS-GEALRRERRAIGTVFQSSALLSRRTAWE 102
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIRNpAQAIRAGIAMVPEDRKRHGIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 103 NVALPL--AWLGVVERDIKARVGELLESVGLSHKADAWP----AQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQA 176
Cdd:TIGR02633 359 NITLSVlkSFCFKMRIDAAAELQIIGSAIQRLKVKTASPflpiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1319887251 177 TASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTI 220
Cdd:TIGR02633 439 KYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-243 |
3.85e-07 |
|
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: 50.62 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYrTADGrlSAVLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDsGSIRINGQDLSALSgeaLRRE 81
Cdd:cd03289 3 MTVKDLTAKY-TEGG--NAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVP---LQKW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 RRAIGTVFQSSALLSRrTAWENVALPLAWlgvverdIKARVGELLESVGLSHKADAWPAQL-----------SGGQRQRI 150
Cdd:cd03289 76 RKAFGVIPQKVFIFSG-TFRKNLDPYGKW-------SDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 151 GIARALALRPSVLLADEATSGLDPqATASVLAllKRLRDEYQ-LAIVLITHEMDAVRTAADAVAeIRDGTIVQYGRIEDL 229
Cdd:cd03289 148 CLARSVLSKAKILLLDEPSAHLDP-ITYQVIR--KTLKQAFAdCTVILSEHRIEAMLECQRFLV-IEENKVRQYDSIQKL 223
|
250
....*....|....
gi 1319887251 230 LARpDSLLGQQLLP 243
Cdd:cd03289 224 LNE-KSHFKQAISP 236
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
34-219 |
4.08e-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: 49.91 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 34 ITAVVGPSGAGKSTLARCISLleqpdsgsiringqdlsALSGEALRRERraiGTVFQSSALlsrRTAWENVALPLAWLGV 113
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEALKY-----------------ALTGELPPNSK---GGAHDPKLI---REGEVRAQVKLAFENA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 114 VERDIKA-RVGELLESVGLSHKAD-AWP-----AQLSGGQRQ------RIGIARALALRPSVLLADEATSGLDPQATASV 180
Cdd:cd03240 81 NGKKYTItRSLAILENVIFCHQGEsNWPlldmrGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEES 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1319887251 181 LA-LLKRLRDEYQLAIVLITHEMDaVRTAADAVAEI-RDGT 219
Cdd:cd03240 161 LAeIIEERKSQKNFQLIVITHDEE-LVDAADHIYRVeKDGR 200
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
16-202 |
4.09e-07 |
|
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: 51.32 E-value: 4.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 16 GRLSAVLKGLSLQVPERSI-----TAVVGPSGAGKSTLARCISLLEQPDSGSIRIN----------GQDLSALSGEALrr 80
Cdd:COG1245 345 PDLTKSYGGFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykpqyiSPDYDGTVEEFL-- 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 81 eRRAIGTVFQSSALlsrrtaWENVALPLawlgvverdikaRVGELLES-VglshkadawpAQLSGGQRQRIGIARALALR 159
Cdd:COG1245 423 -RSANTDDFGSSYY------KTEIIKPL------------GLEKLLDKnV----------KDLSGGELQRVAIAACLSRD 473
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1319887251 160 PSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEM 202
Cdd:COG1245 474 ADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDI 516
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-201 |
5.41e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 49.56 E-value: 5.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSalsgEALRRERRAIGTVFQSSALLSRRTA 100
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLCTYQKQLCFVGHRSGINPYLTL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 WENVALPLAWlgvveRDIKARVGELLESVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASV 180
Cdd:PRK13540 92 RENCLYDIHF-----SPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
|
170 180
....*....|....*....|.
gi 1319887251 181 LALLKRLRDEYQlAIVLITHE 201
Cdd:PRK13540 167 ITKIQEHRAKGG-AVLLTSHQ 186
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
140-241 |
5.70e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.37 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 140 AQLSGGQRQRIGIARALA--LRPSVLLADEATSGLDPQATASVLALLKRLRDEYQlAIVLITHEmDAVRTAADAV----- 212
Cdd:PRK00635 475 ATLSGGEQERTALAKHLGaeLIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHD-EQMISLADRIidigp 552
|
90 100 110
....*....|....*....|....*....|
gi 1319887251 213 -AEIRDGTIVQYGRIEDLLARPDSLLGQQL 241
Cdd:PRK00635 553 gAGIFGGEVLFNGSPREFLAKSDSLTAKYL 582
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
25-200 |
7.04e-07 |
|
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: 50.90 E-value: 7.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 25 LSLQVPERSITAVVGPSGAGKSTLARCISlleqpdsgsiringqDLSALSGEALRRERRaiGTVF--QSSALLSRRTAWE 102
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRILG---------------ELWPVYGGRLTKPAK--GKLFyvPQRPYMTLGTLRD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 103 NVALPLAWLGVVERDIKARVGE-----------LLESVGLSHKADaWPAQLSGGQRQRIGIARALALRPSVLLADEATSG 171
Cdd:TIGR00954 534 QIIYPDSSEDMKRRGLSDKDLEqildnvqlthiLEREGGWSAVQD-WMDVLSGGEKQRIAMARLFYHKPQFAILDECTSA 612
|
170 180
....*....|....*....|....*....
gi 1319887251 172 LDPQATASVLALLKrlrdEYQLAIVLITH 200
Cdd:TIGR00954 613 VSVDVEGYMYRLCR----EFGITLFSVSH 637
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
10-201 |
7.09e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 50.72 E-value: 7.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 10 SYRTADGRLsavLKGLSLQVPERSITAVVGPSGAGKSTLARCisLLEQ--PDSGSIRInGQDLSAlsgeALRRERRAigt 87
Cdd:PRK11147 326 NYQIDGKQL---VKDFSAQVQRGDKIALIGPNGCGKTTLLKL--MLGQlqADSGRIHC-GTKLEV----AYFDQHRA--- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 88 vfqssALLSRRTAWENVALplawlGVVERDIKAR---VGELLESVGLSHKADAWPAQ-LSGGQRQRIGIARaLALRPSVL 163
Cdd:PRK11147 393 -----ELDPEKTVMDNLAE-----GKQEVMVNGRprhVLGYLQDFLFHPKRAMTPVKaLSGGERNRLLLAR-LFLKPSNL 461
|
170 180 190
....*....|....*....|....*....|....*....
gi 1319887251 164 LA-DEATSGLDPQAtasvLALLKRLRDEYQLAIVLITHE 201
Cdd:PRK11147 462 LIlDEPTNDLDVET----LELLEELLDSYQGTVLLVSHD 496
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
34-181 |
8.83e-07 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 50.61 E-value: 8.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 34 ITAVVGPSGAGKSTLARCIS------LLEqpdsGSIRING----QDLSA-LSGEAlrrERRAIG----TVFQS---SALL 95
Cdd:PLN03140 908 LTALMGVSGAGKTTLMDVLAgrktggYIE----GDIRISGfpkkQETFArISGYC---EQNDIHspqvTVRESliySAFL 980
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 96 srRTAWEnvalplawlgvVERDIKAR-VGELLESVGLSHKADA---WPA--QLSGGQRQRIGIARALALRPSVLLADEAT 169
Cdd:PLN03140 981 --RLPKE-----------VSKEEKMMfVDEVMELVELDNLKDAivgLPGvtGLSTEQRKRLTIAVELVANPSIIFMDEPT 1047
|
170
....*....|..
gi 1319887251 170 SGLDPQATASVL 181
Cdd:PLN03140 1048 SGLDARAAAIVM 1059
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
58-241 |
1.12e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 50.41 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 58 PDSGSIRINGQ---DLSALS-GEALRRerraigtvFQSSALlsrrTAWENVALPLAWlgvveRDIKARVGELLEsVGLSH 133
Cdd:COG0178 415 PEALAVKIGGKniaELTALSiDEALEF--------FENLEL----TEREAEIAERIL-----KEIRSRLGFLVD-VGLDY 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 134 -----KADAwpaqLSGGQRQRIGIARALAlrpS-------VLlaDEATSGLDPQATASVLALLKRLRDeyqL---AIVlI 198
Cdd:COG0178 477 ltldrSAGT----LSGGEAQRIRLATQIG---SglvgvlyVL--DEPSIGLHQRDNDRLIETLKRLRD---LgntVIV-V 543
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1319887251 199 THEMDAVRtAADAVAEI------RDGTIVQYGRIEDLLARPDSLLGQQL 241
Cdd:COG0178 544 EHDEDTIR-AADYIIDIgpgageHGGEVVAQGTPEEILKNPDSLTGQYL 591
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
124-229 |
3.31e-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: 48.86 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 124 ELLESVGLSHKADAWPA-QLSGGQRQRIGIARALALR---PSVLLADEATSGLDPQATASVLALLKRLRDEYQlAIVLIT 199
Cdd:TIGR00630 811 QTLCDVGLGYIRLGQPAtTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIE 889
|
90 100 110
....*....|....*....|....*....|....*.
gi 1319887251 200 HEMDAVRTaADAVAEI------RDGTIVQYGRIEDL 229
Cdd:TIGR00630 890 HNLDVIKT-ADYIIDLgpeggdGGGTVVASGTPEEV 924
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
21-174 |
4.69e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.09 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLarcISLL--EQPDSGSiringQDLSAL-----SGEALRRERRAIGTVfqSSA 93
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTL---LSLItgDHPQGYS-----NDLTLFgrrrgSGETIWDIKKHIGYV--SSS 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 94 L-LSRR--TAWENVALP--LAWLGV---VERDIKARVGELLESVGLSHK-ADAWPAQLSGGQRQRIGIARALALRPSVLL 164
Cdd:PRK10938 345 LhLDYRvsTSVRNVILSgfFDSIGIyqaVSDRQQKLAQQWLDILGIDKRtADAPFHSLSWGQQRLALIVRALVKHPTLLI 424
|
170
....*....|
gi 1319887251 165 ADEATSGLDP 174
Cdd:PRK10938 425 LDEPLQGLDP 434
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-250 |
5.00e-06 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 47.98 E-value: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 26 SLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALS-GEALRR-------ERRAIGTVFQSSA---- 93
Cdd:PRK11288 273 SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSpRDAIRAgimlcpeDRKAEGIIPVHSVadni 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 94 -------------LLSRRTAWENVALPLAWLGVVERDIKARVGellesvglshkadawpaQLSGGQRQRIGIARALALRP 160
Cdd:PRK11288 353 nisarrhhlragcLINNRWEAENADRFIRSLNIKTPSREQLIM-----------------NLSGGNQQKAILGRWLSEDM 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 161 SVLLADEATSGLDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGTIVqyGRIEDLLARPDSLLgQQ 240
Cdd:PRK11288 416 KVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIA--GELAREQATERQAL-SL 491
|
250
....*....|
gi 1319887251 241 LLPLTPAAAT 250
Cdd:PRK11288 492 ALPRTSAAVA 501
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
140-220 |
5.28e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.00 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 140 AQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEyQLAIVLITHEMDAVRTAADAVAEIRDGT 219
Cdd:PRK13549 404 ARLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGK 482
|
.
gi 1319887251 220 I 220
Cdd:PRK13549 483 L 483
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
120-224 |
5.81e-06 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 46.84 E-value: 5.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 120 ARVGELLESVGLSHKADAWPA-QLSGGQRQRIGIARALALR---PSVLLADEATSGLDPQATASVLALLKRLRDEYQLAI 195
Cdd:cd03271 147 ARKLQTLCDVGLGYIKLGQPAtTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVV 226
|
90 100 110
....*....|....*....|....*....|....*
gi 1319887251 196 VlITHEMDAVRTaADAVAEI------RDGTIVQYG 224
Cdd:cd03271 227 V-IEHNLDVIKC-ADWIIDLgpeggdGGGQVVASG 259
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
34-178 |
6.09e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 6.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 34 ITAVVGPSGAGKSTLARCI-SLLEQ---PDSGSIRINGqdlsaLSGEALRRERRA----IG---------TVFQSSALLS 96
Cdd:TIGR00956 89 LTVVLGRPGSGCSTLLKTIaSNTDGfhiGVEGVITYDG-----ITPEEIKKHYRGdvvyNAetdvhfphlTVGETLDFAA 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 97 R-RTAWENValplawLGVVERDIKARVGEL-LESVGLSHKADAWPAQ-----LSGGQRQRIGIARALALRPSVLLADEAT 169
Cdd:TIGR00956 164 RcKTPQNRP------DGVSREEYAKHIADVyMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGGAKIQCWDNAT 237
|
....*....
gi 1319887251 170 SGLDpQATA 178
Cdd:TIGR00956 238 RGLD-SATA 245
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-238 |
6.26e-06 |
|
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: 47.98 E-value: 6.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQdlsalsgealrrerraIGTVFQSSALLSRrTA 100
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR----------------ISFSPQTSWIMPG-TI 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 WENVALPLAWLGVVERDIkARVGELLESVGLSHKADAWP-----AQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQ 175
Cdd:TIGR01271 504 KDNIIFGLSYDEYRYTSV-IKACQLEEDIALFPEKDKTVlgeggITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1319887251 176 ATASVL--ALLKRLRDEYQlaiVLITHEMDAVRTaADAVAEIRDGTIVQYGRIEDLLA-RPD---SLLG 238
Cdd:TIGR01271 583 TEKEIFesCLCKLMSNKTR---ILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSELQAkRPDfssLLLG 647
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-202 |
1.66e-05 |
|
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: 45.44 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 27 LQVP-ERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGqdlsalsgealrrERRAIGTVFQSSALLSRRTAWEN-- 103
Cdd:cd03236 20 LPVPrEGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPP-------------DWDEILDEFRGSELQNYFTKLLEgd 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 104 --VALPLAWLGVVERDIKARVGELLESV-------------GLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEA 168
Cdd:cd03236 87 vkVIVKPQYVDLIPKAVKGKVGELLKKKdergkldelvdqlELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190
....*....|....*....|....*....|....
gi 1319887251 169 TSGLDPQATASVLALLKRLRDEYQlAIVLITHEM 202
Cdd:cd03236 167 SSYLDIKQRLNAARLIRELAEDDN-YVLVVEHDL 199
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
116-241 |
2.04e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.22 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 116 RDIKARVGELLEsVGL-----SHKAdawpAQLSGGQRQRIGIAralalrpS-----------VLlaDEATSGLDPQATAS 179
Cdd:PRK00349 464 KEIRERLKFLVD-VGLdyltlSRSA----GTLSGGEAQRIRLA-------TqigsgltgvlyVL--DEPSIGLHQRDNDR 529
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 180 VLALLKRLRDeyqLAIVLIT--HEMDAVRtAADAV------AEIRDGTIVQYGRIEDLLARPDSLLGQQL 241
Cdd:PRK00349 530 LIETLKHLRD---LGNTLIVveHDEDTIR-AADYIvdigpgAGVHGGEVVASGTPEEIMKNPNSLTGQYL 595
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-233 |
2.35e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.31 E-value: 2.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARciSLLEQPDSGSIRINGQdlsalsgealrrerRAIGTVFQSsALLSRRTA 100
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQ--SLLSQFEISEGRVWAE--------------RSIAYVPQQ-AWIMNATV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 WENVAL----PLAWLGVVER--DIKARVGELleSVGLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADEATSGLDP 174
Cdd:PTZ00243 738 RGNILFfdeeDAARLADAVRvsQLEADLAQL--GGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDA 815
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1319887251 175 QATASVL--ALLKRLRDEYQlaiVLITHEMDAVrTAADAVAEIRDGTIVQYGRIEDLLARP 233
Cdd:PTZ00243 816 HVGERVVeeCFLGALAGKTR---VLATHQVHVV-PRADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
2-229 |
3.22e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 45.74 E-value: 3.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYrtaDGRLS-AVLKGLSLQVPERSITAVVGPSGAGKSTL-ARCISLLEQPDSGSIRINGQDLSALS----G 75
Cdd:PLN03232 615 ISIKNGYFSW---DSKTSkPTLSDINLEIPVGSLVAIVGGTGEGKTSLiSAMLGELSHAETSSVVIRGSVAYVPQvswiF 691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 76 EALRRERRAIGTVFQSSallsrrtawenvalplawlgvverdikaRVGELLESVGLSHKADAWPAQ-----------LSG 144
Cdd:PLN03232 692 NATVRENILFGSDFESE----------------------------RYWRAIDVTALQHDLDLLPGRdlteigergvnISG 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 145 GQRQRIGIARALALRPSVLLADEATSGLDPQATASVLAllKRLRDEYQLAI-VLITHEMDAVrTAADAVAEIRDGTIVQY 223
Cdd:PLN03232 744 GQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVFD--SCMKDELKGKTrVLVTNQLHFL-PLMDRIILVSEGMIKEE 820
|
....*.
gi 1319887251 224 GRIEDL 229
Cdd:PLN03232 821 GTFAEL 826
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
2-242 |
4.21e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.50 E-value: 4.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 2 IAIDDLYKSYRTADGRlsAVLKGLSLQVPERSITAVVGPSGAGKSTLarcislleqpdsgsiringqdLSALSGEALRRE 81
Cdd:PLN03130 615 ISIKNGYFSWDSKAER--PTLSNINLDVPVGSLVAIVGSTGEGKTSL---------------------ISAMLGELPPRS 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 82 ------RRAIGTVFQSSALLSRrTAWENVALPLAWlgvverdIKARVGELLESVGLSHKADAWPA-----------QLSG 144
Cdd:PLN03130 672 dasvviRGTVAYVPQVSWIFNA-TVRDNILFGSPF-------DPERYERAIDVTALQHDLDLLPGgdlteigergvNISG 743
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 145 GQRQRIGIARALALRPSVLLADEATSGLDPQATASVLAllKRLRDEYQLAI-VLITHEMDAVrTAADAVAEIRDGTIVQY 223
Cdd:PLN03130 744 GQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDELRGKTrVLVTNQLHFL-SQVDRIILVHEGMIKEE 820
|
250
....*....|....*....
gi 1319887251 224 GRIEDLLArpDSLLGQQLL 242
Cdd:PLN03130 821 GTYEELSN--NGPLFQKLM 837
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
26-173 |
8.41e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.41 E-value: 8.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 26 SLQVPER-SITAVVGPSGAGKSTLARCISlleqpdsGSIRIN-GQDLSALSGEA-LRRERraiGTVFQS--SALLSRRTa 100
Cdd:PRK13409 92 GLPIPKEgKVTGILGPNGIGKTTAVKILS-------GELIPNlGDYEEEPSWDEvLKRFR---GTELQNyfKKLYNGEI- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 weNVALPLAWLGVVERDIKARVGELLESV-------------GLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADE 167
Cdd:PRK13409 161 --KVVHKPQYVDLIPKVFKGKVRELLKKVdergkldevverlGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
....*.
gi 1319887251 168 ATSGLD 173
Cdd:PRK13409 239 PTSYLD 244
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
142-244 |
1.25e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.86 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 142 LSGGQRQRIGIARALALR---PSVLLADEATSGLDPQATASVLALLKRLRDeyqlA---IVLITHEMDAVRTaADAVAEI 215
Cdd:COG0178 827 LSGGEAQRVKLASELSKRstgKTLYILDEPTTGLHFHDIRKLLEVLHRLVD----KgntVVVIEHNLDVIKT-ADWIIDL 901
|
90 100 110
....*....|....*....|....*....|....*
gi 1319887251 216 ------RDGTIVQYGRIEDLLARPDSLLGQQLLPL 244
Cdd:COG0178 902 gpeggdGGGEIVAEGTPEEVAKVKASYTGRYLKEY 936
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-173 |
1.41e-04 |
|
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: 43.62 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 26 SLQVPER-SITAVVGPSGAGKSTlarCISLLeqpdSGSIRIN-GQDLSALS-GEALRRERraiGTVFQS--SALLSRRTa 100
Cdd:COG1245 92 GLPVPKKgKVTGILGPNGIGKST---ALKIL----SGELKPNlGDYDEEPSwDEVLKRFR---GTELQDyfKKLANGEI- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 weNVALPLAWLGVVERDIKARVGELLESV-------------GLSHKADAWPAQLSGGQRQRIGIARALALRPSVLLADE 167
Cdd:COG1245 161 --KVAHKPQYVDLIPKVFKGTVRELLEKVdergkldelaeklGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
....*.
gi 1319887251 168 ATSGLD 173
Cdd:COG1245 239 PSSYLD 244
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
119-176 |
2.29e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.92 E-value: 2.29e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1319887251 119 KARVGELLesVGLSHKADAW---PAQLSGGQRQRIGIARALALRPSVLLADEATSGLDPQA 176
Cdd:PLN03073 321 EARAASIL--AGLSFTPEMQvkaTKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA 379
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
142-202 |
3.50e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 42.02 E-value: 3.50e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1319887251 142 LSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQlAIVLITHEM 202
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEM 451
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
124-244 |
4.69e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 41.98 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 124 ELLESVGLSHKADAWPA-QLSGGQRQRIGIARALALRP---SVLLADEATSGLDPQATASVLALLKRLRDEYQlAIVLIT 199
Cdd:PRK00349 812 QTLVDVGLGYIKLGQPAtTLSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLHFEDIRKLLEVLHRLVDKGN-TVVVIE 890
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1319887251 200 HEMDAVRTaADAVAEI------RDGTIVQYGRIEDLLARPDSLLGQQLLPL 244
Cdd:PRK00349 891 HNLDVIKT-ADWIIDLgpeggdGGGEIVATGTPEEVAKVEASYTGRYLKPV 940
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
28-216 |
9.78e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 39.94 E-value: 9.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 28 QVPERSITAVVGPSGAGKSTLARCISLleqpdsgsiringqdlsALSGEALR-RERRAIGTVFQSSAllsrRTAWENVAL 106
Cdd:cd03279 24 GLDNNGLFLICGPTGAGKSTILDAITY-----------------ALYGKTPRyGRQENLRSVFAPGE----DTAEVSFTF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 107 PLAW-LGVVERDIKARVGELLESVGLSH-KADAWPAQ----LSGGQRQRIGIARALALRPSV----------LLADEATS 170
Cdd:cd03279 83 QLGGkKYRVERSRGLDYDQFTRIVLLPQgEFDRFLARpvstLSGGETFLASLSLALALSEVLqnrggarleaLFIDEGFG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1319887251 171 GLDPQATASVLALLKRLRDEYQLaIVLITHeMDAVRTAADAVAEIR 216
Cdd:cd03279 163 TLDPEALEAVATALELIRTENRM-VGVISH-VEELKERIPQRLEVI 206
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
21-173 |
1.29e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 39.47 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 21 VLKGLSLQVPERSITAVVGPSGAGKSTLARCISLLEQPDSGSIRINGQDLSALsgealrrERRAIGTVFQSSALLSRRTA 100
Cdd:PRK13541 15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-------AKPYCTYIGHNLGLKLEMTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 101 WENVALplaWlgvverdikarvGELLESVGLSHKA----------DAWPAQLSGGQRQRIGIARALALRPSVLLADEATS 170
Cdd:PRK13541 88 FENLKF---W------------SEIYNSAETLYAAihyfklhdllDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVET 152
|
...
gi 1319887251 171 GLD 173
Cdd:PRK13541 153 NLS 155
|
|
| ABC_SMC3_euk |
cd03272 |
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ... |
119-192 |
2.68e-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: 38.78 E-value: 2.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1319887251 119 KARVGELLESVGLSH------------------KADAWPA--QLSGGQRQRIGIARALALR-----PSVLLaDEATSGLD 173
Cdd:cd03272 116 KNDVMNLLESAGFSRsnpyyivpqgkinsltnmKQDEQQEmqQLSGGQKSLVALALIFAIQkcdpaPFYLF-DEIDAALD 194
|
90
....*....|....*....
gi 1319887251 174 PQATASVLALLKRLRDEYQ 192
Cdd:cd03272 195 AQYRTAVANMIKELSDGAQ 213
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
22-48 |
7.43e-03 |
|
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: 38.07 E-value: 7.43e-03
10 20
....*....|....*....|....*..
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKSTL 48
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTL 650
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
22-73 |
8.36e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.27 E-value: 8.36e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1319887251 22 LKGLSLQVPERSITAVVGPSGAGKS-----TLARCI-SLLEQPDSGSIRINGQDLSAL 73
Cdd:PRK00635 611 LKDLTISLPLGRLTVVTGVSGSGKSslindTLVPAVeEFIEQGFCSNLSIQWGAISRL 668
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
142-212 |
8.55e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 36.78 E-value: 8.55e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1319887251 142 LSGGQRQRIGIARALALRPSVLLADEATSGLDPQATASVLALLKRLRDEYQLAIVLITHEMDAVRTAADAV 212
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRI 142
|
|
| |
