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Conserved domains on  [gi|446634871|ref|WP_000712217|]
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MULTISPECIES: substrate-binding domain-containing protein [Bacillus]

Protein Classification

excise and PBP_like domain-containing protein( domain architecture ID 10019979)

excise and PBP_like domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
YvgK COG1910
Periplasmic molybdate-binding protein/domain [Inorganic ion transport and metabolism];
1-313 3.37e-106

Periplasmic molybdate-binding protein/domain [Inorganic ion transport and metabolism];


:

Pssm-ID: 441514 [Multi-domain]  Cd Length: 328  Bit Score: 312.71  E-value: 3.37e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446634871   1 MKKESEESSMDHHSYTTEEVAKRLKVSKLTVYDLIKKGELPSYRVGRQMRIDAADLEQYIKQMKTGKVQVTPvkndsnsI 80
Cdd:COG1910   22 SRKLVSSLGVLEFLRVKLGLVGGLRVAEPLVRGAGVITSLVAADGLLKIPEPSEGLEAGLEVEVELLRPELP-------L 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446634871  81 SNTCIISGQELTLDMLAKRIENRLPSSNILRAYQGSLTSLVKMYQGEGSIVSLHLFDGETGTYNVPYVKRILVGQPCTMI 160
Cdd:COG1910   95 LTLVIIGSHDPLLDILLRLLEKRESGAGLASSYVGSLGGLEALARGEADIAGIHLLDEETGEYNIPYVRRYLPGRPAVLI 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446634871 161 NLLSRNVGFYVQKGNPKNIKTWADLSQSSIRFVNREKGSGIRVLVDEQLRIQNLNKERISGYEWEESNHLGVATQVANEK 240
Cdd:COG1910  175 NLARREQGLIVAKGNPKGIKGLEDLARPDLRFVNRQKGSGTRVLLDELLRRLGIDPEDINGYEREEYTHLAVAAAVASGE 254
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446634871 241 ADVGVGSEKFSQIVNVDFIPIMKEQYDLVILKNKENEELIEVVKDILQSEEFHNELKAIGGYDMTKTGQIIYE 313
Cdd:COG1910  255 ADVGLGIEAAARAFGLDFIPLAEERYDLVIPREALFDPPVQALLEILRSPEFRERAAALGGYDLSDTGKVIYE 327
 
Name Accession Description Interval E-value
YvgK COG1910
Periplasmic molybdate-binding protein/domain [Inorganic ion transport and metabolism];
1-313 3.37e-106

Periplasmic molybdate-binding protein/domain [Inorganic ion transport and metabolism];


Pssm-ID: 441514 [Multi-domain]  Cd Length: 328  Bit Score: 312.71  E-value: 3.37e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446634871   1 MKKESEESSMDHHSYTTEEVAKRLKVSKLTVYDLIKKGELPSYRVGRQMRIDAADLEQYIKQMKTGKVQVTPvkndsnsI 80
Cdd:COG1910   22 SRKLVSSLGVLEFLRVKLGLVGGLRVAEPLVRGAGVITSLVAADGLLKIPEPSEGLEAGLEVEVELLRPELP-------L 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446634871  81 SNTCIISGQELTLDMLAKRIENRLPSSNILRAYQGSLTSLVKMYQGEGSIVSLHLFDGETGTYNVPYVKRILVGQPCTMI 160
Cdd:COG1910   95 LTLVIIGSHDPLLDILLRLLEKRESGAGLASSYVGSLGGLEALARGEADIAGIHLLDEETGEYNIPYVRRYLPGRPAVLI 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446634871 161 NLLSRNVGFYVQKGNPKNIKTWADLSQSSIRFVNREKGSGIRVLVDEQLRIQNLNKERISGYEWEESNHLGVATQVANEK 240
Cdd:COG1910  175 NLARREQGLIVAKGNPKGIKGLEDLARPDLRFVNRQKGSGTRVLLDELLRRLGIDPEDINGYEREEYTHLAVAAAVASGE 254
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446634871 241 ADVGVGSEKFSQIVNVDFIPIMKEQYDLVILKNKENEELIEVVKDILQSEEFHNELKAIGGYDMTKTGQIIYE 313
Cdd:COG1910  255 ADVGLGIEAAARAFGLDFIPLAEERYDLVIPREALFDPPVQALLEILRSPEFRERAAALGGYDLSDTGKVIYE 327
PBP_like pfam12727
PBP superfamily domain; This family belongs to the periplasmic binding domain superfamily. It ...
97-287 9.22e-78

PBP superfamily domain; This family belongs to the periplasmic binding domain superfamily. It is often associated with a helix-turn-helix domain.


Pssm-ID: 463683 [Multi-domain]  Cd Length: 192  Bit Score: 235.55  E-value: 9.22e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446634871   97 AKRIENRLPSSNILRAYQGSLTSLVKMYQGEGSIVSLHLFDGETGTYNVPYVKRILVGQPCTMINLLSRNVGFYVQKGNP 176
Cdd:pfam12727   1 AEELARKHPGVRLAVAYVGSLGGLAALRRGEAHIAGIHLLDPETGEYNLPFLRRLLPGIPVVLINLAYREQGLVVAPGNP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446634871  177 KNIKTWADLSQSSIRFVNREKGSGIRVLVDEQLRIQNLNKERISGYEWEESNHLGVATQVANEKADVGVGSEKFS-QIVN 255
Cdd:pfam12727  81 KGITGWEDLARPGLRFVNRQRGSGTRVLLDELLRKAGIDPSDINGYDREERSHLAVAAAVASGRADAGLGIEAAArALGG 160
                         170       180       190
                  ....*....|....*....|....*....|..
gi 446634871  256 VDFIPIMKEQYDLVILKNKENEELIEVVKDIL 287
Cdd:pfam12727 161 LDFIPLARERYDLVIPKEALDDPAVQALLEVL 192
PRK14498 PRK14498
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ...
85-299 1.01e-54

putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional


Pssm-ID: 237732 [Multi-domain]  Cd Length: 633  Bit Score: 188.11  E-value: 1.01e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446634871  85 IISGQELTLDMLAKRIenRLPSSNILRAYQGSLTSLVKMYQGEGSIVSLHLFDGETGTYNVPYVKRILVGQPCTMINLLS 164
Cdd:PRK14498 421 IIGSHDPGLDLLLDLL--ARRGLRLRSLHVGSMGGLMALKRGEADIAGIHLLDPETGEYNIPYIKKYLLGEDAVLVKGYR 498
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446634871 165 RNVGFYVQKGNPKNIKTWADLSQSSIRFVNREKGSGIRVLVDEQLRIQNLNKERISGYEWEESNHLGVATQVANEKADVG 244
Cdd:PRK14498 499 REQGLVVRKGNPKGIEGIEDLVRKDVRFVNRQRGSGTRILLDYHLKELAIDPERINGYDREEKTHMAVAAAVAQGRADAG 578
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446634871 245 VGSEKFSQIVNVDFIPIMKEQYDLVILKNKENEELIEVVKDILQSEEFHNELKAI 299
Cdd:PRK14498 579 LGIRAAAKALGLDFIPLAEEEYDLLIPKERLEKPAVRAFLEALKSPEFKAALEEL 633
excise TIGR01764
DNA binding domain, excisionase family; An excisionase, or Xis protein, is a small protein ...
15-62 3.59e-15

DNA binding domain, excisionase family; An excisionase, or Xis protein, is a small protein that binds and promotes excisive recombination; it is not enzymatically active. This model represents a number of putative excisionases and related proteins from temperate phage, plasmids, and transposons, as well as DNA binding domains of other proteins, such as a DNA modification methylase. This model identifies mostly small proteins and N-terminal regions of large proteins, but some proteins appear to have two copies. This domain appears similar, in both sequence and predicted secondary structure (PSIPRED) to the MerR family of transcriptional regulators (pfam00376). [Unknown function, General]


Pssm-ID: 200128  Cd Length: 49  Bit Score: 68.40  E-value: 3.59e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 446634871   15 YTTEEVAKRLKVSKLTVYDLIKKGELPSYRVGRQMRIDAADLEQYIKQ 62
Cdd:TIGR01764   2 LTVEEAAEYLGVSKSTVYRLIEEGELPAYRVGRHYRIPREDVDEYLEQ 49
PBP2_CysP cd01005
Substrate binding domain of an active sulfate transporter, a member of the type 2 periplasmic ...
167-193 8.00e-04

Substrate binding domain of an active sulfate transporter, a member of the type 2 periplasmic binding fold superfamily; This family contains sulfate binding domain of CysP proteins that serve as initial receptors in the ABC transport of sulfate and thiosulfate in eubacteria. After binding the ligand, CysP interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The CysP proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270226  Cd Length: 307  Bit Score: 40.37  E-value: 8.00e-04
                         10        20
                 ....*....|....*....|....*..
gi 446634871 167 VGFYVQKGNPKNIKTWADLSQSSIRFV 193
Cdd:cd01005   97 IVFLVRKGNPKGIRDWDDLVKPGVSVI 123
 
Name Accession Description Interval E-value
YvgK COG1910
Periplasmic molybdate-binding protein/domain [Inorganic ion transport and metabolism];
1-313 3.37e-106

Periplasmic molybdate-binding protein/domain [Inorganic ion transport and metabolism];


Pssm-ID: 441514 [Multi-domain]  Cd Length: 328  Bit Score: 312.71  E-value: 3.37e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446634871   1 MKKESEESSMDHHSYTTEEVAKRLKVSKLTVYDLIKKGELPSYRVGRQMRIDAADLEQYIKQMKTGKVQVTPvkndsnsI 80
Cdd:COG1910   22 SRKLVSSLGVLEFLRVKLGLVGGLRVAEPLVRGAGVITSLVAADGLLKIPEPSEGLEAGLEVEVELLRPELP-------L 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446634871  81 SNTCIISGQELTLDMLAKRIENRLPSSNILRAYQGSLTSLVKMYQGEGSIVSLHLFDGETGTYNVPYVKRILVGQPCTMI 160
Cdd:COG1910   95 LTLVIIGSHDPLLDILLRLLEKRESGAGLASSYVGSLGGLEALARGEADIAGIHLLDEETGEYNIPYVRRYLPGRPAVLI 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446634871 161 NLLSRNVGFYVQKGNPKNIKTWADLSQSSIRFVNREKGSGIRVLVDEQLRIQNLNKERISGYEWEESNHLGVATQVANEK 240
Cdd:COG1910  175 NLARREQGLIVAKGNPKGIKGLEDLARPDLRFVNRQKGSGTRVLLDELLRRLGIDPEDINGYEREEYTHLAVAAAVASGE 254
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446634871 241 ADVGVGSEKFSQIVNVDFIPIMKEQYDLVILKNKENEELIEVVKDILQSEEFHNELKAIGGYDMTKTGQIIYE 313
Cdd:COG1910  255 ADVGLGIEAAARAFGLDFIPLAEERYDLVIPREALFDPPVQALLEILRSPEFRERAAALGGYDLSDTGKVIYE 327
PBP_like pfam12727
PBP superfamily domain; This family belongs to the periplasmic binding domain superfamily. It ...
97-287 9.22e-78

PBP superfamily domain; This family belongs to the periplasmic binding domain superfamily. It is often associated with a helix-turn-helix domain.


Pssm-ID: 463683 [Multi-domain]  Cd Length: 192  Bit Score: 235.55  E-value: 9.22e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446634871   97 AKRIENRLPSSNILRAYQGSLTSLVKMYQGEGSIVSLHLFDGETGTYNVPYVKRILVGQPCTMINLLSRNVGFYVQKGNP 176
Cdd:pfam12727   1 AEELARKHPGVRLAVAYVGSLGGLAALRRGEAHIAGIHLLDPETGEYNLPFLRRLLPGIPVVLINLAYREQGLVVAPGNP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446634871  177 KNIKTWADLSQSSIRFVNREKGSGIRVLVDEQLRIQNLNKERISGYEWEESNHLGVATQVANEKADVGVGSEKFS-QIVN 255
Cdd:pfam12727  81 KGITGWEDLARPGLRFVNRQRGSGTRVLLDELLRKAGIDPSDINGYDREERSHLAVAAAVASGRADAGLGIEAAArALGG 160
                         170       180       190
                  ....*....|....*....|....*....|..
gi 446634871  256 VDFIPIMKEQYDLVILKNKENEELIEVVKDIL 287
Cdd:pfam12727 161 LDFIPLARERYDLVIPKEALDDPAVQALLEVL 192
PRK14498 PRK14498
putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing ...
85-299 1.01e-54

putative molybdopterin biosynthesis protein MoeA/LysR substrate binding-domain-containing protein; Provisional


Pssm-ID: 237732 [Multi-domain]  Cd Length: 633  Bit Score: 188.11  E-value: 1.01e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446634871  85 IISGQELTLDMLAKRIenRLPSSNILRAYQGSLTSLVKMYQGEGSIVSLHLFDGETGTYNVPYVKRILVGQPCTMINLLS 164
Cdd:PRK14498 421 IIGSHDPGLDLLLDLL--ARRGLRLRSLHVGSMGGLMALKRGEADIAGIHLLDPETGEYNIPYIKKYLLGEDAVLVKGYR 498
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446634871 165 RNVGFYVQKGNPKNIKTWADLSQSSIRFVNREKGSGIRVLVDEQLRIQNLNKERISGYEWEESNHLGVATQVANEKADVG 244
Cdd:PRK14498 499 REQGLVVRKGNPKGIEGIEDLVRKDVRFVNRQRGSGTRILLDYHLKELAIDPERINGYDREEKTHMAVAAAVAQGRADAG 578
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446634871 245 VGSEKFSQIVNVDFIPIMKEQYDLVILKNKENEELIEVVKDILQSEEFHNELKAI 299
Cdd:PRK14498 579 LGIRAAAKALGLDFIPLAEEEYDLLIPKERLEKPAVRAFLEALKSPEFKAALEEL 633
excise TIGR01764
DNA binding domain, excisionase family; An excisionase, or Xis protein, is a small protein ...
15-62 3.59e-15

DNA binding domain, excisionase family; An excisionase, or Xis protein, is a small protein that binds and promotes excisive recombination; it is not enzymatically active. This model represents a number of putative excisionases and related proteins from temperate phage, plasmids, and transposons, as well as DNA binding domains of other proteins, such as a DNA modification methylase. This model identifies mostly small proteins and N-terminal regions of large proteins, but some proteins appear to have two copies. This domain appears similar, in both sequence and predicted secondary structure (PSIPRED) to the MerR family of transcriptional regulators (pfam00376). [Unknown function, General]


Pssm-ID: 200128  Cd Length: 49  Bit Score: 68.40  E-value: 3.59e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 446634871   15 YTTEEVAKRLKVSKLTVYDLIKKGELPSYRVGRQMRIDAADLEQYIKQ 62
Cdd:TIGR01764   2 LTVEEAAEYLGVSKSTVYRLIEEGELPAYRVGRHYRIPREDVDEYLEQ 49
HTH_17 pfam12728
Helix-turn-helix domain; This domain is a DNA-binding helix-turn-helix domain.
15-64 7.01e-15

Helix-turn-helix domain; This domain is a DNA-binding helix-turn-helix domain.


Pssm-ID: 463684 [Multi-domain]  Cd Length: 51  Bit Score: 67.87  E-value: 7.01e-15
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 446634871   15 YTTEEVAKRLKVSKLTVYDLIKKGELPSYRVGRQMRIDAADLEQYIKQMK 64
Cdd:pfam12728   2 LTVEEAAELLGVSRRTVYRLIRSGELPAAKIGRRWRIRKSDLEEWLERRR 51
AlpA COG3311
DNA-binding transcriptional regulator AlpA [Transcription, Mobilome: prophages, transposons];
15-67 8.69e-10

DNA-binding transcriptional regulator AlpA [Transcription, Mobilome: prophages, transposons];


Pssm-ID: 442540 [Multi-domain]  Cd Length: 64  Bit Score: 54.16  E-value: 8.69e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446634871  15 YTTEEVAKRLKVSKLTVYDLIKKGELP-SYRVG-RQMRIDAADLEQYIKQMKTGK 67
Cdd:COG3311    9 LRLKEVAELLGVSRSTIYRLIKKGEFPkPVKLGgRSVRWRESEVEAWLAARIAAS 63
Sbp COG1613
ABC-type sulfate transport system, periplasmic component [Inorganic ion transport and ...
169-185 4.92e-04

ABC-type sulfate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 441221  Cd Length: 340  Bit Score: 41.27  E-value: 4.92e-04
                         10
                 ....*....|....*..
gi 446634871 169 FYVQKGNPKNIKTWADL 185
Cdd:COG1613  129 FLVRKGNPKGIKDWDDL 145
PBP2_CysP cd01005
Substrate binding domain of an active sulfate transporter, a member of the type 2 periplasmic ...
167-193 8.00e-04

Substrate binding domain of an active sulfate transporter, a member of the type 2 periplasmic binding fold superfamily; This family contains sulfate binding domain of CysP proteins that serve as initial receptors in the ABC transport of sulfate and thiosulfate in eubacteria. After binding the ligand, CysP interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The CysP proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270226  Cd Length: 307  Bit Score: 40.37  E-value: 8.00e-04
                         10        20
                 ....*....|....*....|....*..
gi 446634871 167 VGFYVQKGNPKNIKTWADLSQSSIRFV 193
Cdd:cd01005   97 IVFLVRKGNPKGIRDWDDLVKPGVSVI 123
HTH_MerR-trunc cd04762
Helix-Turn-Helix DNA binding domain of truncated MerR-like proteins; Proteins in this family ...
15-57 1.72e-03

Helix-Turn-Helix DNA binding domain of truncated MerR-like proteins; Proteins in this family mostly have a truncated helix-turn-helix (HTH) MerR-like domain. They lack a portion of the C-terminal region, called Wing 2 and the long dimerization helix that is typically present in MerR-like proteins. These truncated domains are found in response regulator receiver (REC) domain proteins (i.e., CheY), cytosine-C5 specific DNA methylases, IS607 transposase-like proteins, and RacA, a bacterial protein that anchors chromosomes to cell poles.


Pssm-ID: 133390 [Multi-domain]  Cd Length: 49  Bit Score: 35.64  E-value: 1.72e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 446634871  15 YTTEEVAKRLKVSKLTVYDLIKKGELPSYR-VGRQMRIDAADLE 57
Cdd:cd04762    1 LTTKEAAELLGVSPSTLRRWVKEGKLKAIRtPGGHRRFPEEDLE 44
PBP2_ModA3_like cd13517
Substrate binding domain of molybdate binding protein-like (ModA3), a member of the type 2 ...
171-291 3.75e-03

Substrate binding domain of molybdate binding protein-like (ModA3), a member of the type 2 periplasmic binding fold superfamily; This subfamily contains molybdate binding protein-like (ModA3) domain of an ABC-type transporter. Molybdate transport system is comprised of a periplasmic binding protein, an integral membrane protein, and an energizer protein. These three proteins are coded by modA, modB, and modC genes, respectively. ModA proteins serve as initial receptors in the ABC transport of molybdate mostly in eubacteria and archaea. ModA transporters import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. In contrast to the structure of the two ModA homologs from Escherichia coli and Azotobacter vinelandii, where the oxygen atoms are tetrahedrally arrangted around the metal center, the structure of Pyrococcus furiosus ModA/WtpA (PfModA) has shown that a binding site for molybdate and tungstate where the central metal atom is in a hexacoordinate configuration. The ModA proteins belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap.


Pssm-ID: 270235 [Multi-domain]  Cd Length: 223  Bit Score: 37.97  E-value: 3.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446634871 171 VQKGNPKNIKTWADLSQSSIRFV-NREKGSGI---RVLVDEQLRIQNLNKERISGYEwEESNHLgvATQVANEKADVGVG 246
Cdd:cd13517   84 VPKGNPKNITSLEDLAKPGVKVAlGDPKAAAIgkyAKKILEKNGLWEKVKKNVVVYT-ATVNQL--LTYVLLGQVDAAIV 160
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 446634871 247 SE--KFSQIVNVDFIPIMKEQ-YDLVI----LKNKENEELIEVVKDILQSEE 291
Cdd:cd13517  161 WEdfAYWNPGKVEVIPIPKEQnRIKTIpiavLKSSKNKELAKKFVDFVTSDE 212
3a0106s03 TIGR00971
sulfate/thiosulfate-binding protein; This model describes binding proteins functionally ...
167-200 3.98e-03

sulfate/thiosulfate-binding protein; This model describes binding proteins functionally associated with the sulfate ABC transporter. In the model bacterium E. coli, two different members work with the same transporter; mutation analysis says each enables the uptake of both sulfate and thiosulfate. In many species, a single binding protein is found, and may be referred to in general terms as a sulfate ABC transporter sulfate-binding protein. [Transport and binding proteins, Anions]


Pssm-ID: 130044  Cd Length: 315  Bit Score: 38.41  E-value: 3.98e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 446634871  167 VGFYVQKGNPKNIKTWADLSQSSIRFVN-REKGSG 200
Cdd:TIGR00971 105 IVFLVRKGNPKQIHDWNDLIKPGVSVITpNPKSSG 139
PRK10852 PRK10852
thiosulfate ABC transporter substrate-binding protein CysP;
168-193 4.18e-03

thiosulfate ABC transporter substrate-binding protein CysP;


Pssm-ID: 236775  Cd Length: 338  Bit Score: 38.58  E-value: 4.18e-03
                         10        20
                 ....*....|....*....|....*.
gi 446634871 168 GFYVQKGNPKNIKTWADLSQSSIRFV 193
Cdd:PRK10852 123 AFLVRKGNPKNIHDWNDLVRSDVKLI 148
ModA COG0725
ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion ...
171-291 8.23e-03

ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, periplasmic Mo-binding protein ModA is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440489 [Multi-domain]  Cd Length: 253  Bit Score: 37.16  E-value: 8.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446634871 171 VQKGNPKNIKTWADLSQSSIRFV--NREKG-SGIR---VLvdEQLRIQNLNKERISGYEweesNHLGVATQVANEKADVG 244
Cdd:COG0725  112 VPKGNPADISSLEDLAKPGVRIAigDPKTVpYGKYakeAL--EKAGLWDALKPKLVLGE----NVRQVLAYVESGEADAG 185
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446634871 245 VG--SEKFSQIVNVDFIPIMKEQ-----YDLVILKNKENEELIEVVKDILQSEE 291
Cdd:COG0725  186 IVylSDALAAKGVLVVVELPAELyapivYPAAVLKGAKNPEAAKAFLDFLLSPE 239
 
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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