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Conserved domains on  [gi|495128541|ref|WP_007853352|]
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MULTISPECIES: AAA family ATPase [Enterobacteriaceae]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RloC super family cl44110
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
3-489 1.95e-21

Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];


The actual alignment was detected with superfamily member COG4694:

Pssm-ID: 443729 [Multi-domain]  Cd Length: 692  Bit Score: 99.43  E-value: 1.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128541   3 IEIRHCNNIVRARITLTADKLNIKFAPNGTGKSTLSRAISCAARDDTQGLQALMPFRLRGDNPDNAgpivigaegigDVM 82
Cdd:COG4694    6 KKLKNVGAFKDFGWLAFFKKLNLIYGENGSGKSTLSRILRSLELGDTSSEVIAEFEIEAGGSAPNP-----------SVR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128541  83 CFNEEYV-----------GQFTFQPDEL-INDSFNILIR----------------NEAHAEREREIEEMTQTIRAVFTDH 134
Cdd:COG4694   75 VFNRDFVeenlrsgeeikGIFTLGEENIeLEEEIEELEKeiedlkkeldklekelKEAKKALEKLLEDLAKSIKDDLKKL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128541 135 ----------------------AELNSLIDHLQELSNAFKSTSSGISRSSTGMRGLSGGNKI-HHIPVG-----LENYQP 186
Cdd:COG4694  155 fassgrnyrkanlekklsalksSSEDELKEKLKLLKEEEPEPIAPITPLPDLKALLSEAETLlEKSAVSsaieeLAALIQ 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128541 187 YIRSErrvewiDWQTKGLEFSPLSDGC-CPFCTGDIreKEGQIRKVSEEYDKSTIKNLTAIIRLVENLgnyltEDARERL 265
Cdd:COG4694  235 NPGNS------DWVEQGLAYHKEEEDDtCPFCQQEL--AAERIEALEAYFDDEYEKLLAALKDLLEEL-----ESAINAL 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128541 266 LAITLLQNGpeaehiEYLVALKRQTDTLTEKLTALRGLNVFSLQEQQNVrEVLTARLIDLQFFPDLQCELT--QGITDRL 343
Cdd:COG4694  302 SALLLEILR------TLLPSAKEDLKAALEALNALLETLLAALEEKIAN-PSTSIDLDDQELLDELNDLIAalNALIEEH 374
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128541 344 NAALQDLINLAGP------------LQGRINRHRDSMVRLIAQHKT------------------------------NINN 381
Cdd:COG4694  375 NAKIANLKAEKEEarkkleahelaeLKEDLSRYKAEVEELIEELKTikalkkaledlkteiseleaelssvdeaadEINE 454
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128541 382 FLTYAGYK-YRVDIAGEGEQR-KLRLRHMDFDGYvsggSQHLSYGERNAFAIVLFMYECLSKNP----GLIILDDPISSF 455
Cdd:COG4694  455 ELKALGFDeFSLEAVEDGRSSyRLKRNGENDAKP----AKTLSEGEKTAIALAYFLAELEGDENdlkkKIVVIDDPVSSL 530
                        570       580       590
                 ....*....|....*....|....*....|....
gi 495128541 456 DKNKKFAILEMLFRrasgECLKNRTVLMLTHDVE 489
Cdd:COG4694  531 DSNHRFAVASLLKE----LSKKAKQVIVLTHNLY 560
 
Name Accession Description Interval E-value
RloC COG4694
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
3-489 1.95e-21

Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 443729 [Multi-domain]  Cd Length: 692  Bit Score: 99.43  E-value: 1.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128541   3 IEIRHCNNIVRARITLTADKLNIKFAPNGTGKSTLSRAISCAARDDTQGLQALMPFRLRGDNPDNAgpivigaegigDVM 82
Cdd:COG4694    6 KKLKNVGAFKDFGWLAFFKKLNLIYGENGSGKSTLSRILRSLELGDTSSEVIAEFEIEAGGSAPNP-----------SVR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128541  83 CFNEEYV-----------GQFTFQPDEL-INDSFNILIR----------------NEAHAEREREIEEMTQTIRAVFTDH 134
Cdd:COG4694   75 VFNRDFVeenlrsgeeikGIFTLGEENIeLEEEIEELEKeiedlkkeldklekelKEAKKALEKLLEDLAKSIKDDLKKL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128541 135 ----------------------AELNSLIDHLQELSNAFKSTSSGISRSSTGMRGLSGGNKI-HHIPVG-----LENYQP 186
Cdd:COG4694  155 fassgrnyrkanlekklsalksSSEDELKEKLKLLKEEEPEPIAPITPLPDLKALLSEAETLlEKSAVSsaieeLAALIQ 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128541 187 YIRSErrvewiDWQTKGLEFSPLSDGC-CPFCTGDIreKEGQIRKVSEEYDKSTIKNLTAIIRLVENLgnyltEDARERL 265
Cdd:COG4694  235 NPGNS------DWVEQGLAYHKEEEDDtCPFCQQEL--AAERIEALEAYFDDEYEKLLAALKDLLEEL-----ESAINAL 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128541 266 LAITLLQNGpeaehiEYLVALKRQTDTLTEKLTALRGLNVFSLQEQQNVrEVLTARLIDLQFFPDLQCELT--QGITDRL 343
Cdd:COG4694  302 SALLLEILR------TLLPSAKEDLKAALEALNALLETLLAALEEKIAN-PSTSIDLDDQELLDELNDLIAalNALIEEH 374
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128541 344 NAALQDLINLAGP------------LQGRINRHRDSMVRLIAQHKT------------------------------NINN 381
Cdd:COG4694  375 NAKIANLKAEKEEarkkleahelaeLKEDLSRYKAEVEELIEELKTikalkkaledlkteiseleaelssvdeaadEINE 454
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128541 382 FLTYAGYK-YRVDIAGEGEQR-KLRLRHMDFDGYvsggSQHLSYGERNAFAIVLFMYECLSKNP----GLIILDDPISSF 455
Cdd:COG4694  455 ELKALGFDeFSLEAVEDGRSSyRLKRNGENDAKP----AKTLSEGEKTAIALAYFLAELEGDENdlkkKIVVIDDPVSSL 530
                        570       580       590
                 ....*....|....*....|....*....|....
gi 495128541 456 DKNKKFAILEMLFRrasgECLKNRTVLMLTHDVE 489
Cdd:COG4694  531 DSNHRFAVASLLKE----LSKKAKQVIVLTHNLY 560
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
438-493 5.79e-06

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: 47.91  E-value: 5.79e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 495128541 438 CLSKNPGLIILDDPISSFDKNKKFAILEMLfRRAsgeCLKNRTVLMLTHDVEPVID 493
Cdd:cd03235  146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELL-REL---RREGMTILVVTHDLGLVLE 197
AAA_13 pfam13166
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
416-504 1.18e-04

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.


Pssm-ID: 463796 [Multi-domain]  Cd Length: 712  Bit Score: 45.44  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128541  416 GGSQ---HLSYGERNAFAIVLFmYECLSKN------PGLIILDDPISSFDKNKKFAILEMLFRRASGECLKNrtVLMLTH 486
Cdd:pfam13166 492 GGSQaaeTLSEGERTAIAFLYF-LKSLKDSdndigkDKIVVIDDPVSSLDSNHLFIVFSLIRTRTEKTNAKQ--VFILTH 568
                          90
                  ....*....|....*...
gi 495128541  487 DVEpvidTLKSVRKLFSN 504
Cdd:pfam13166 569 NFY----FFKEVTNWFDN 582
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
420-489 2.44e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 43.57  E-value: 2.44e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495128541 420 HLSYGE--RNAFAIVLFMyeclskNPGLIILDDPISSFDKNKKFAILEMLFRrasgecLKNR--TVLMLTHDVE 489
Cdd:PRK13647 138 HLSYGQkkRVAIAGVLAM------DPDVIVLDEPMAYLDPRGQETLMEILDR------LHNQgkTVIVATHDVD 199
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
421-489 9.16e-03

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: 39.19  E-value: 9.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495128541  421 LSYGERNAFAIVLFMYeclsKNPGLIILDDPISSFDknkkfAILEMLFRRASGECLKNRTVLMLTHDVE 489
Cdd:TIGR02857 459 LSGGQAQRLALARAFL----RDAPLLLLDEPTAHLD-----AETEAEVLEALRALAQGRTVLLVTHRLA 518
 
Name Accession Description Interval E-value
RloC COG4694
Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];
3-489 1.95e-21

Wobble nucleotide-excising tRNase [Translation, ribosomal structure and biogenesis];


Pssm-ID: 443729 [Multi-domain]  Cd Length: 692  Bit Score: 99.43  E-value: 1.95e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128541   3 IEIRHCNNIVRARITLTADKLNIKFAPNGTGKSTLSRAISCAARDDTQGLQALMPFRLRGDNPDNAgpivigaegigDVM 82
Cdd:COG4694    6 KKLKNVGAFKDFGWLAFFKKLNLIYGENGSGKSTLSRILRSLELGDTSSEVIAEFEIEAGGSAPNP-----------SVR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128541  83 CFNEEYV-----------GQFTFQPDEL-INDSFNILIR----------------NEAHAEREREIEEMTQTIRAVFTDH 134
Cdd:COG4694   75 VFNRDFVeenlrsgeeikGIFTLGEENIeLEEEIEELEKeiedlkkeldklekelKEAKKALEKLLEDLAKSIKDDLKKL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128541 135 ----------------------AELNSLIDHLQELSNAFKSTSSGISRSSTGMRGLSGGNKI-HHIPVG-----LENYQP 186
Cdd:COG4694  155 fassgrnyrkanlekklsalksSSEDELKEKLKLLKEEEPEPIAPITPLPDLKALLSEAETLlEKSAVSsaieeLAALIQ 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128541 187 YIRSErrvewiDWQTKGLEFSPLSDGC-CPFCTGDIreKEGQIRKVSEEYDKSTIKNLTAIIRLVENLgnyltEDARERL 265
Cdd:COG4694  235 NPGNS------DWVEQGLAYHKEEEDDtCPFCQQEL--AAERIEALEAYFDDEYEKLLAALKDLLEEL-----ESAINAL 301
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128541 266 LAITLLQNGpeaehiEYLVALKRQTDTLTEKLTALRGLNVFSLQEQQNVrEVLTARLIDLQFFPDLQCELT--QGITDRL 343
Cdd:COG4694  302 SALLLEILR------TLLPSAKEDLKAALEALNALLETLLAALEEKIAN-PSTSIDLDDQELLDELNDLIAalNALIEEH 374
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128541 344 NAALQDLINLAGP------------LQGRINRHRDSMVRLIAQHKT------------------------------NINN 381
Cdd:COG4694  375 NAKIANLKAEKEEarkkleahelaeLKEDLSRYKAEVEELIEELKTikalkkaledlkteiseleaelssvdeaadEINE 454
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128541 382 FLTYAGYK-YRVDIAGEGEQR-KLRLRHMDFDGYvsggSQHLSYGERNAFAIVLFMYECLSKNP----GLIILDDPISSF 455
Cdd:COG4694  455 ELKALGFDeFSLEAVEDGRSSyRLKRNGENDAKP----AKTLSEGEKTAIALAYFLAELEGDENdlkkKIVVIDDPVSSL 530
                        570       580       590
                 ....*....|....*....|....*....|....
gi 495128541 456 DKNKKFAILEMLFRrasgECLKNRTVLMLTHDVE 489
Cdd:COG4694  531 DSNHRFAVASLLKE----LSKKAKQVIVLTHNLY 560
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
438-493 5.79e-06

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: 47.91  E-value: 5.79e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 495128541 438 CLSKNPGLIILDDPISSFDKNKKFAILEMLfRRAsgeCLKNRTVLMLTHDVEPVID 493
Cdd:cd03235  146 ALVQDPDLLLLDEPFAGVDPKTQEDIYELL-REL---RREGMTILVVTHDLGLVLE 197
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
391-489 1.21e-05

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: 46.08  E-value: 1.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128541 391 RVDIAGEGEQRKLRLRHMDFDGYVSGgsqhLSYGERNAFAIVLfmyeCLSKNPGLIILDDPISSFDKNKKFAILEMLFRR 470
Cdd:cd00267   55 EILIDGKDIAKLPLEELRRRIGYVPQ----LSGGQRQRVALAR----ALLLNPDLLLLDEPTSGLDPASRERLLELLREL 126
                         90
                 ....*....|....*....
gi 495128541 471 ASgeclKNRTVLMLTHDVE 489
Cdd:cd00267  127 AE----EGRTVIIVTHDPE 141
AAA_13 pfam13166
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ...
416-504 1.18e-04

AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.


Pssm-ID: 463796 [Multi-domain]  Cd Length: 712  Bit Score: 45.44  E-value: 1.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128541  416 GGSQ---HLSYGERNAFAIVLFmYECLSKN------PGLIILDDPISSFDKNKKFAILEMLFRRASGECLKNrtVLMLTH 486
Cdd:pfam13166 492 GGSQaaeTLSEGERTAIAFLYF-LKSLKDSdndigkDKIVVIDDPVSSLDSNHLFIVFSLIRTRTEKTNAKQ--VFILTH 568
                          90
                  ....*....|....*...
gi 495128541  487 DVEpvidTLKSVRKLFSN 504
Cdd:pfam13166 569 NFY----FFKEVTNWFDN 582
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
398-489 1.86e-04

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 43.36  E-value: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128541 398 GEQRKLRLRHMdfdGYVSGGSQHLSygernAFAIVLFMYECLSKNPGLIILDDPISSFDKNKKFAILEMLFRRASGEclK 477
Cdd:cd03240  103 GESNWPLLDMR---GRCSGGEKVLA-----SLIIRLALAETFGSNCGILALDEPTTNLDEENIEESLAEIIEERKSQ--K 172
                         90
                 ....*....|..
gi 495128541 478 NRTVLMLTHDVE 489
Cdd:cd03240  173 NFQLIVITHDEE 184
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
420-489 2.44e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 43.57  E-value: 2.44e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495128541 420 HLSYGE--RNAFAIVLFMyeclskNPGLIILDDPISSFDKNKKFAILEMLFRrasgecLKNR--TVLMLTHDVE 489
Cdd:PRK13647 138 HLSYGQkkRVAIAGVLAM------DPDVIVLDEPMAYLDPRGQETLMEILDR------LHNQgkTVIVATHDVD 199
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
408-487 3.69e-04

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: 43.67  E-value: 3.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128541 408 MDFDGYVSGGSQHLSYGERNAFAIVlfmyECLSKNPGLIILDDPISSFDKNKKFAILEMLFRRasgecLKNRTVLMLTHD 487
Cdd:COG2274  599 MGYDTVVGEGGSNLSGGQRQRLAIA----RALLRNPRILILDEATSALDAETEAIILENLRRL-----LKGRTVIIIAHR 669
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
417-491 1.02e-03

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: 41.30  E-value: 1.02e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495128541 417 GSQhLSYGERNAFAIVlfmyECLSKNPGLIILDDPISSFDKNKKFAILEMLFrrasgECLKNRTVLMLTHDVEPV 491
Cdd:cd03248  148 GSQ-LSGGQKQRVAIA----RALIRNPQVLILDEATSALDAESEQQVQQALY-----DWPERRTVLVIAHRLSTV 212
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
411-493 2.23e-03

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: 40.17  E-value: 2.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495128541 411 DGYVSGGSQHLSYGERNAFAIVlfmyECLSKNPGLIILDDPISSFDKnkkfaILEMLFRRASGECLKNRTVLMLTHDVEP 490
Cdd:cd03244  130 DTVVEEGGENLSVGQRQLLCLA----RALLRKSKILVLDEATASVDP-----ETDALIQKTIREAFKDCTVLTIAHRLDT 200

                 ...
gi 495128541 491 VID 493
Cdd:cd03244  201 IID 203
cbiO PRK13646
energy-coupling factor transporter ATPase;
421-491 2.43e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 40.53  E-value: 2.43e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495128541 421 LSYGERNAFAIVlfmyECLSKNPGLIILDDPISSFDKNKKFAILEmLFRRASGEclKNRTVLMLTHDVEPV 491
Cdd:PRK13646 146 MSGGQMRKIAIV----SILAMNPDIIVLDEPTAGLDPQSKRQVMR-LLKSLQTD--ENKTIILVSHDMNEV 209
cbiO PRK13640
energy-coupling factor transporter ATPase;
413-489 4.54e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 39.78  E-value: 4.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495128541 413 YVSGGSQHLSYGERNAFAIVlfmyECLSKNPGLIILDDPISSFDKNKKFAILEmLFRRASGEclKNRTVLMLTHDVE 489
Cdd:PRK13640 136 YIDSEPANLSGGQKQRVAIA----GILAVEPKIIILDESTSMLDPAGKEQILK-LIRKLKKK--NNLTVISITHDID 205
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
421-489 9.16e-03

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: 39.19  E-value: 9.16e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495128541  421 LSYGERNAFAIVLFMYeclsKNPGLIILDDPISSFDknkkfAILEMLFRRASGECLKNRTVLMLTHDVE 489
Cdd:TIGR02857 459 LSGGQAQRLALARAFL----RDAPLLLLDEPTAHLD-----AETEAEVLEALRALAQGRTVLLVTHRLA 518
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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