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Conserved domains on  [gi|1080617793|gb|OFN93548|]
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zinc-binding protein [Streptococcus sp. HMSC074F05]

Protein Classification

zinc ABC transporter substrate-binding protein AdcA( domain architecture ID 10099085)

zinc ABC transporter substrate-binding protein AdcA functions as the initial receptor in the ATP-driven transport of zinc and/or manganese

Gene Ontology:  GO:0140359|GO:0042626|GO:0055052
PubMed:  26517916|24638992|25750732
TCDB:  3.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AdcA cd01017
Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of ...
 28-308 8.14e-121

Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of Zn2+ and Mn2+ and in competence for genetic transformation and adhesion. The AdcA proteins belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. They are comprised of two globular subdomains connected by a long alpha helix and they bind their ligand in the cleft between these domains. In addition, many of these proteins have a low complexity region containing metal binding histidine-rich motif (repetitive HDH sequence).


:

Pssm-ID: 238499 [Multi-domain]  Cd Length: 282  Bit Score: 355.45  E-value: 8.14e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793  28 NGKLKVMTTFYPVYDFTKNIVGDEGTVDLLIGAGSEPHEYELSAKGRAMIQDSDVFVYENENMETWVPNLLKSMKDKKTK 107
Cdd:cd01017     1 SGKLKVVTTFYPLYEFTKAIGGDKADVKLIIPAGTEPHDFEPSPKDIARIADADVFVYNGLGMETWAEKVLKSLQNKKLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 108 VIDATKGMVLLPGLEEEHEHEGGEEHH-HEYDPHLWLSPHRAMKMVESIRDQLVAAYPDKKKTFEKNAQAYLKKLQALDQ 186
Cdd:cd01017    81 VVEASKGIKLLKAGGAEHDHDHSHSHHhGDYDPHVWLSPVLAIQQVENIKDALIKLDPDNKEYYEKNAAAYAKKLEALDQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 187 AYQDGLKDAKQKNFVTQHAAFRYLALDYGLNQVAISGISPDSEPSAARLRELTEYIKKNEIKVIYFEENASKSLAKTLSS 266
Cdd:cd01017   161 EYRAKLAKAKGKTFVTQHAAFGYLARRYGLKQIAIVGVSPEVEPSPKQLAELVEFVKKSDVKYIFFEENASSKIAETLAK 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1080617793 267 EAGVELAVLNPLESLTDQEMKDGEDYVSVMKENLKALEKTTS 308
Cdd:cd01017   241 ETGAKLLVLNPLETLTKEEIDDGKDYFSLMKENLETLKRALK 282
ZinT pfam09223
ZinT (YodA) periplasmic lipocalin-like zinc-recruitment; ZinT plays a critical role in ...
 321-501 4.20e-114

ZinT (YodA) periplasmic lipocalin-like zinc-recruitment; ZinT plays a critical role in recruiting periplasmic zinc to the bacterial zinc-uptake complex ZnuABC, consisting of families pfam01297,pfam00950, pfam00005, regulated by the transcription-regulator FUR, pfam01475. ZinT acts as a Zn2+-buffering protein that delivers Zn2+ to ZnuA (TroA), pfam01297. Members of this family of prokaryotic domains were first identified as part of the response of bacteria to a challenge with the toxic heavy metal cadmium. They are able to bind to cadmium, and ensure its subsequent elimination.


:

Pssm-ID: 430470  Cd Length: 181  Bit Score: 334.21  E-value: 4.20e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 321 DAKTVQKGYFEDSQVKDRSLANYAGDWKSVYPYLQDGTLDQVFDYKAKLNPTMTAAEYKEYYTKGYQTDIDRIKIDKDSM 400
Cdd:pfam09223   1 EEKTVYNGYFEDSQVKDRTLSDWAGDWQSVYPYLLDGTLDPVFEHKAKEKGDKTAEEYKAYYTKGYKTDVDRIVIDGDTI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 401 EFYQKGSSKKYTYKYVGKHILTYKKGNRGVRYLFEAKESDAGDFKYVQFSDHEITPVKAAHFHIFHGGKSQEALYDELEN 480
Cdd:pfam09223  81 TFTKNGKKKSGTYKYDGYKILTYEKGNRGVRYLFEAKDKDAGAPKYIQFSDHIIAPTKAEHFHIYWGNDSQEALLEEMDN 160

                         170       180
                  ....*....|....*....|.
gi 1080617793 481 WPTYYPSNLSGLEVAQEMLAH 501
Cdd:pfam09223 161 WPTYYPSSLSGEEIVQEMLAH 181
 
Name Accession Description Interval E-value
AdcA cd01017
Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of ...
 28-308 8.14e-121

Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of Zn2+ and Mn2+ and in competence for genetic transformation and adhesion. The AdcA proteins belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. They are comprised of two globular subdomains connected by a long alpha helix and they bind their ligand in the cleft between these domains. In addition, many of these proteins have a low complexity region containing metal binding histidine-rich motif (repetitive HDH sequence).


Pssm-ID: 238499 [Multi-domain]  Cd Length: 282  Bit Score: 355.45  E-value: 8.14e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793  28 NGKLKVMTTFYPVYDFTKNIVGDEGTVDLLIGAGSEPHEYELSAKGRAMIQDSDVFVYENENMETWVPNLLKSMKDKKTK 107
Cdd:cd01017     1 SGKLKVVTTFYPLYEFTKAIGGDKADVKLIIPAGTEPHDFEPSPKDIARIADADVFVYNGLGMETWAEKVLKSLQNKKLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 108 VIDATKGMVLLPGLEEEHEHEGGEEHH-HEYDPHLWLSPHRAMKMVESIRDQLVAAYPDKKKTFEKNAQAYLKKLQALDQ 186
Cdd:cd01017    81 VVEASKGIKLLKAGGAEHDHDHSHSHHhGDYDPHVWLSPVLAIQQVENIKDALIKLDPDNKEYYEKNAAAYAKKLEALDQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 187 AYQDGLKDAKQKNFVTQHAAFRYLALDYGLNQVAISGISPDSEPSAARLRELTEYIKKNEIKVIYFEENASKSLAKTLSS 266
Cdd:cd01017   161 EYRAKLAKAKGKTFVTQHAAFGYLARRYGLKQIAIVGVSPEVEPSPKQLAELVEFVKKSDVKYIFFEENASSKIAETLAK 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1080617793 267 EAGVELAVLNPLESLTDQEMKDGEDYVSVMKENLKALEKTTS 308
Cdd:cd01017   241 ETGAKLLVLNPLETLTKEEIDDGKDYFSLMKENLETLKRALK 282
ZinT pfam09223
ZinT (YodA) periplasmic lipocalin-like zinc-recruitment; ZinT plays a critical role in ...
 321-501 4.20e-114

ZinT (YodA) periplasmic lipocalin-like zinc-recruitment; ZinT plays a critical role in recruiting periplasmic zinc to the bacterial zinc-uptake complex ZnuABC, consisting of families pfam01297,pfam00950, pfam00005, regulated by the transcription-regulator FUR, pfam01475. ZinT acts as a Zn2+-buffering protein that delivers Zn2+ to ZnuA (TroA), pfam01297. Members of this family of prokaryotic domains were first identified as part of the response of bacteria to a challenge with the toxic heavy metal cadmium. They are able to bind to cadmium, and ensure its subsequent elimination.


Pssm-ID: 430470  Cd Length: 181  Bit Score: 334.21  E-value: 4.20e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 321 DAKTVQKGYFEDSQVKDRSLANYAGDWKSVYPYLQDGTLDQVFDYKAKLNPTMTAAEYKEYYTKGYQTDIDRIKIDKDSM 400
Cdd:pfam09223   1 EEKTVYNGYFEDSQVKDRTLSDWAGDWQSVYPYLLDGTLDPVFEHKAKEKGDKTAEEYKAYYTKGYKTDVDRIVIDGDTI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 401 EFYQKGSSKKYTYKYVGKHILTYKKGNRGVRYLFEAKESDAGDFKYVQFSDHEITPVKAAHFHIFHGGKSQEALYDELEN 480
Cdd:pfam09223  81 TFTKNGKKKSGTYKYDGYKILTYEKGNRGVRYLFEAKDKDAGAPKYIQFSDHIIAPTKAEHFHIYWGNDSQEALLEEMDN 160

                         170       180
                  ....*....|....*....|.
gi 1080617793 481 WPTYYPSNLSGLEVAQEMLAH 501
Cdd:pfam09223 161 WPTYYPSSLSGEEIVQEMLAH 181
Zn_bnd_ABC_AdcA NF033605
zinc ABC transporter substrate-binding lipoprotein AdcA;
21-501 2.21e-112

zinc ABC transporter substrate-binding lipoprotein AdcA;


Pssm-ID: 468109 [Multi-domain]  Cd Length: 516  Bit Score: 342.14  E-value: 2.21e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793  21 CSKSQSQNG---KLKVMTTFYPVYDFTKNIVGDEGTVDLLIGAGSEPHEYELSAKGRAMIQDSDVFVYENENMETWVPNL 97
Cdd:NF033605   21 CGKGDSKNKdndKIKINTTVFPLKSFAEQIGGKHVEVESIYPAGTDLHSYEPTQKDILNASKADLFVYTGDDLDPVAKKV 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793  98 LKSMKDKKTKV-----IDATKgmvLLPGLEEEHEHEGGEEHHHE---------YDPHLWLSPHRAMKMVESIRDQLVAAY 163
Cdd:NF033605  101 ASTIKKDDKKLsledkLDKST---LLTDQHEHGEEHEHEEEGHEhehhhhhggYDPHVWLDPKFDQTFAKEIKDELVKKD 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 164 PDKKKTFEKNAQAYLKKLQALDQAYQDGLKDAKQKNFVTQHAAFRYLALDYGLNQVAISGISPDsEPSAARLRELTEYIK 243
Cdd:NF033605  178 PKHKDEYEKNYKKLNKDLKGIDKDMKDITKDKQGNAVFISHESLGYLADRYGFVQKGVQNMNAE-DPSQKELTEIVKEIN 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 244 KNEIKVIYFEENASKSLAKTLSSEAGVELAVLNPLESLTDQEMKDGE-DYVSVMKENLKALEKTTSQAGK--DIQPEHEE 320
Cdd:NF033605  257 DSGAKYILYEDNVSNKVTDTIRKETDAKPLKFYNMESLNKEQQKDKDlTYQSLMKENIKNIDKALNDKIKvkDDKAESKH 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 321 DaKTVQKGYFEDSQVKDRSLANYAGDWKSVYPYLQDGTLDQVFDYKAKLNPTMTAAEYKEYYTKGYQTDIDRIKIDKDSM 400
Cdd:NF033605  337 D-KAISDGYFKDSQVKDRELSDYEGDWQSVYPYLKDGTLDEVMKHKAEDDGDMSAKEYKAYYDKGYKTDISNIKITGDTI 415

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 401 EFYQKGSSKKYTYKYVGKHILTYKKGNRGVRYLFEAKESDAGDF-KYVQFSDHEITPVKAAHFHIFHGGKSQEALyDELE 479
Cdd:NF033605  416 TFTKNGKKVTGKYEYDGKDILKYEKGNRGVRYTFKLVGDANKDLpKYVQFSDHNIAPKKAEHFHIFMGNDKDKVL-KELD 494

                         490       500
                  ....*....|....*....|..
gi 1080617793 480 NWPTYYPSNLSGLEVAQEMLAH 501
Cdd:NF033605  495 NWPTYYPAKLSKDEIKEEMLAH 516
ZinT COG3443
Periplasmic Zn/Cd-binding protein ZinT [Inorganic ion transport and metabolism];
310-501 1.21e-105

Periplasmic Zn/Cd-binding protein ZinT [Inorganic ion transport and metabolism];


Pssm-ID: 442667  Cd Length: 191  Bit Score: 313.00  E-value: 1.21e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 310 AGKDIQPEHEEDAKTVQKGYFEDSQVKDRSLANYAGDWKSVYPYLQDGTLDQVFDYKAKLNPTMTAAEYKEYYTKGYQTD 389
Cdd:COG3443     1 HGHSHGHPHTEAEKKAYEGYFDDKDVKDRSLSDWEGDWQSVYPYLQDGTLDPVFEHKAKKDGDKTAEEYKAYYTKGYATD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 390 IDRIKIDKDSMEFYQKGSSKKYTYKYVGKHILTYKKGNRGVRYLFEAKESDAGDFKYVQFSDHEITPVKAAHFHIFHgGK 469
Cdd:COG3443    81 VDRIVIEGNTVTFHKNGKVKSCEYKYDGYKILTYKSGNRGVRYLFECKDADAGAPKYIQFSDHIIAPEKSAHFHIYW-GN 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1080617793 470 SQEALYDELENWPTYYPSNLSGLEVAQEMLAH 501
Cdd:COG3443   160 DQEALLEEMDNWPTYYPYQLSGDQIVDEMLAH 191
ZnuA COG0803
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ...
 22-299 4.72e-103

ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and metabolism];


Pssm-ID: 440566 [Multi-domain]  Cd Length: 286  Bit Score: 310.25  E-value: 4.72e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793  22 SKSQSQNGKLKVMTTFYPVYDFTKNIVGDEGTVDLLIGAGSEPHEYELSAKGRAMIQDSDVFVYENENMETWVPNLLKSM 101
Cdd:COG0803    21 AAASSAAGKLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTPSDIAKLAKADLVVYNGLGLEGWLDKLLEAA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 102 KDKKTKVIDATKGMVLLPgleeehehEGGEEHHHEYDPHLWLSPHRAMKMVESIRDQLVAAYPDKKKTFEKNAQAYLKKL 181
Cdd:COG0803   101 GNPGVPVVDASEGIDLLE--------LEEGHDHGEPDPHVWLDPKNAKKVAENIADALAELDPANAAYYEANAAAYLAEL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 182 QALDQAYQDGLKDAKQKNFVTQHAAFRYLALDYGLNQVAISGISPDSEPSAARLRELTEYIKKNEIKVIYFEENASKSLA 261
Cdd:COG0803   173 DALDAEIKAKLAAIPGRKLVTSHDAFGYLARAYGLEVVAIQGISPGSEPSPADLAELIDLIKEEGVKAIFVESQVSPKLA 252

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1080617793 262 KTLSSEAGVELAVLNPLESLTDqemkDGEDYVSVMKEN 299
Cdd:COG0803   253 ETLAEETGVKVLYLDSLGGPGG----PGDTYLDMMRHN 286
ZnuA pfam01297
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ...
 33-305 1.15e-98

Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins such as TroA that interacts with an ATP-binding cassette transport system in Treponema pallidum. ZnuA is part of the bacterial zinc-uptake complex ZnuABC, whose components are the following families, ZinT, pfam09223, pfam00950, pfam00005, all of which are regulated by the transcription-regulator family FUR, pfam01475. ZinT acts as a Zn2+-buffering protein that delivers Zn2+ to ZnuA (TroA), a high-affinity zinc-uptake protein. In Gram-negative bacteria the ZnuABC transporter system ensures an adequate import of zinc in Zn2+-poor environments, such as those encountered by pathogens within the infected host.


Pssm-ID: 460151 [Multi-domain]  Cd Length: 269  Bit Score: 298.31  E-value: 1.15e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793  33 VMTTFYPVYDFTKNIVGDEGTVDLLIGAGSEPHEYELSAKGRAMIQDSDVFVYENENMETWVPNLLKSMKDKKtkVIDAT 112
Cdd:pfam01297   1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDKLLEALPNKK--VVDAS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 113 KGMvllPGLEEEHEHEGGEEHHHEYDPHLWLSPHRAMKMVESIRDQLVAAYPDKKKTFEKNAQAYLKKLQALDQAYQDGL 192
Cdd:pfam01297  79 EGV---ELLDEEGEEEDHDGHDHGYDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIKEQL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 193 KDAKQKN--FVTQHAAFRYLALDYGLNQVAISGISPDSEPSAARLRELTEYIKKNEIKVIYFEENASKSLAKTLSSEAGV 270
Cdd:pfam01297 156 ASIPEKTrkLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKETGV 235

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1080617793 271 ElaVLNPLESLTDQEMKDGEDYVSVMKENLKALEK 305
Cdd:pfam01297 236 K--VLGPLYTDSLGEPGGGATYLDLMRHNLDTLAE 268
PRK10306 PRK10306
zinc/cadmium-binding protein; Provisional
 328-501 8.65e-66

zinc/cadmium-binding protein; Provisional


Pssm-ID: 182368 [Multi-domain]  Cd Length: 216  Bit Score: 211.56  E-value: 8.65e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 328 GYFEDSQVKDRSLANYAGDWKSVYPYLQDGTLDQVFDYKAKLNPTMTAAEYKEYYTKGYQTDIDRIKIDKDSMEFYQKGS 407
Cdd:PRK10306   43 GVFDDANVQDRTLSDWDGVWQSVYPYLQSGKLDPVFQKKAKKDKTKTFEEIKAYYRKGYATDVEMIGIENGIVEFHRGNE 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 408 SKKYTYKYVGKHILTYKKGNRGVRYLFEAKESDAGDFKYVQFSDHEITPVKAAHFHIFHGGKSQEALYDELENWPTYYPS 487
Cdd:PRK10306  123 VTSCKYDYDGYKILTYASGKKGVRYLFECKDAESKAPKYVQFSDHIIAPRKSSHFHIFMGNDSQQALLNEMENWPTYYPY 202

                         170
                  ....*....|....
gi 1080617793 488 NLSGLEVAQEMLAH 501
Cdd:PRK10306  203 QLSSEEVVDEMLHH 216
anch_rpt_subst TIGR03772
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ...
 138-305 1.25e-19

anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ABC transporter permease subunits as identified by pfam00950, but additionally contain the Actinobacterial insert domain described by TIGR03769. Some homologs (lacking the insert) have been described as transporters of manganese or of chelated iron. Members of this family typically are found along with an ATP-binding cassette protein, a permease, and an LPXTG-anchored protein with two or three copies of the TIGR03769 insert that occurs just once in this protein family. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 163484 [Multi-domain]  Cd Length: 479  Bit Score: 91.46  E-value: 1.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 138 DPHLWLSPHRAMKMVESIRDQLVAAYPDKKKTFEKNAQAYLKKLQALDQAYQDGLKD--AKQKNFVTQHAAFRYLALDYG 215
Cdd:TIGR03772 310 DPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIATipPSRRHLITTHDAYSYLGQAYG 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 216 LNQVAISGISPDSEPSAARLRELTEYIKKNEIKVIYFEEN---ASKSLAKTlSSEAGVELAVLNPlESLTDqemkDGEDY 292
Cdd:TIGR03772 390 LNIAGFVTPNPAVEPSLADRRRLTRTIENLKVPAVFLEPNlaaRSTTLNEI-ADELGVRVCAIYG-DTFDD----DVTNY 463

                         170
                  ....*....|...
gi 1080617793 293 VSVMKENLKALEK 305
Cdd:TIGR03772 464 VDLMRFNADSLAD 476
znuA PRK09545
zinc ABC transporter substrate-binding protein ZnuA;
54-278 3.43e-15

zinc ABC transporter substrate-binding protein ZnuA;


Pssm-ID: 236558 [Multi-domain]  Cd Length: 311  Bit Score: 76.20  E-value: 3.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793  54 VDLLIGAGSEPHEYELSAKGRAMIQDSDVFVYENENMETWVPNLLKSMKDKKTKVIDATKG--MVLLPGLEEEHEHEGGE 131
Cdd:PRK09545   48 TEVLLPDGASPHDYSLRPSDVKRLQSADLVVWVGPEMEAFLEKPVSKLPENKQVTIAQLPDvkPLLMKGAHDDHHDDDHD 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 132 EHHHE----------YDPHLWLSPHRAMKMVESIRDQLVAAYPDKKKTFEKNAQAYLKKLQALDQAYQDGLKDAKQKNFV 201
Cdd:PRK09545  128 HAGHEksdedhhhgeYNMHIWLSPEIARATAVAIHDKLVELMPQSKAKLDANLKDFEAQLAQTDKQIGNQLAPVKGKGYF 207

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080617793 202 TQHAAFRYLALDYGLNQVAISGISPDSEPSAARLRELTEYIKKNEIKVIYFEENASKSLAKTLSSEAGVELAVLNPL 278
Cdd:PRK09545  208 VFHDAYGYFEKHYGLTPLGHFTVNPEIQPGAQRLHEIRTQLVEQKATCVFAEPQFRPAVIESVAKGTSVRMGTLDPL 284
 
Name Accession Description Interval E-value
AdcA cd01017
Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of ...
 28-308 8.14e-121

Metal binding protein AdcA. These proteins have been shown to function in the ABC uptake of Zn2+ and Mn2+ and in competence for genetic transformation and adhesion. The AdcA proteins belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. They are comprised of two globular subdomains connected by a long alpha helix and they bind their ligand in the cleft between these domains. In addition, many of these proteins have a low complexity region containing metal binding histidine-rich motif (repetitive HDH sequence).


Pssm-ID: 238499 [Multi-domain]  Cd Length: 282  Bit Score: 355.45  E-value: 8.14e-121
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793  28 NGKLKVMTTFYPVYDFTKNIVGDEGTVDLLIGAGSEPHEYELSAKGRAMIQDSDVFVYENENMETWVPNLLKSMKDKKTK 107
Cdd:cd01017     1 SGKLKVVTTFYPLYEFTKAIGGDKADVKLIIPAGTEPHDFEPSPKDIARIADADVFVYNGLGMETWAEKVLKSLQNKKLK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 108 VIDATKGMVLLPGLEEEHEHEGGEEHH-HEYDPHLWLSPHRAMKMVESIRDQLVAAYPDKKKTFEKNAQAYLKKLQALDQ 186
Cdd:cd01017    81 VVEASKGIKLLKAGGAEHDHDHSHSHHhGDYDPHVWLSPVLAIQQVENIKDALIKLDPDNKEYYEKNAAAYAKKLEALDQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 187 AYQDGLKDAKQKNFVTQHAAFRYLALDYGLNQVAISGISPDSEPSAARLRELTEYIKKNEIKVIYFEENASKSLAKTLSS 266
Cdd:cd01017   161 EYRAKLAKAKGKTFVTQHAAFGYLARRYGLKQIAIVGVSPEVEPSPKQLAELVEFVKKSDVKYIFFEENASSKIAETLAK 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1080617793 267 EAGVELAVLNPLESLTDQEMKDGEDYVSVMKENLKALEKTTS 308
Cdd:cd01017   241 ETGAKLLVLNPLETLTKEEIDDGKDYFSLMKENLETLKRALK 282
ZinT pfam09223
ZinT (YodA) periplasmic lipocalin-like zinc-recruitment; ZinT plays a critical role in ...
 321-501 4.20e-114

ZinT (YodA) periplasmic lipocalin-like zinc-recruitment; ZinT plays a critical role in recruiting periplasmic zinc to the bacterial zinc-uptake complex ZnuABC, consisting of families pfam01297,pfam00950, pfam00005, regulated by the transcription-regulator FUR, pfam01475. ZinT acts as a Zn2+-buffering protein that delivers Zn2+ to ZnuA (TroA), pfam01297. Members of this family of prokaryotic domains were first identified as part of the response of bacteria to a challenge with the toxic heavy metal cadmium. They are able to bind to cadmium, and ensure its subsequent elimination.


Pssm-ID: 430470  Cd Length: 181  Bit Score: 334.21  E-value: 4.20e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 321 DAKTVQKGYFEDSQVKDRSLANYAGDWKSVYPYLQDGTLDQVFDYKAKLNPTMTAAEYKEYYTKGYQTDIDRIKIDKDSM 400
Cdd:pfam09223   1 EEKTVYNGYFEDSQVKDRTLSDWAGDWQSVYPYLLDGTLDPVFEHKAKEKGDKTAEEYKAYYTKGYKTDVDRIVIDGDTI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 401 EFYQKGSSKKYTYKYVGKHILTYKKGNRGVRYLFEAKESDAGDFKYVQFSDHEITPVKAAHFHIFHGGKSQEALYDELEN 480
Cdd:pfam09223  81 TFTKNGKKKSGTYKYDGYKILTYEKGNRGVRYLFEAKDKDAGAPKYIQFSDHIIAPTKAEHFHIYWGNDSQEALLEEMDN 160

                         170       180
                  ....*....|....*....|.
gi 1080617793 481 WPTYYPSNLSGLEVAQEMLAH 501
Cdd:pfam09223 161 WPTYYPSSLSGEEIVQEMLAH 181
Zn_bnd_ABC_AdcA NF033605
zinc ABC transporter substrate-binding lipoprotein AdcA;
21-501 2.21e-112

zinc ABC transporter substrate-binding lipoprotein AdcA;


Pssm-ID: 468109 [Multi-domain]  Cd Length: 516  Bit Score: 342.14  E-value: 2.21e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793  21 CSKSQSQNG---KLKVMTTFYPVYDFTKNIVGDEGTVDLLIGAGSEPHEYELSAKGRAMIQDSDVFVYENENMETWVPNL 97
Cdd:NF033605   21 CGKGDSKNKdndKIKINTTVFPLKSFAEQIGGKHVEVESIYPAGTDLHSYEPTQKDILNASKADLFVYTGDDLDPVAKKV 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793  98 LKSMKDKKTKV-----IDATKgmvLLPGLEEEHEHEGGEEHHHE---------YDPHLWLSPHRAMKMVESIRDQLVAAY 163
Cdd:NF033605  101 ASTIKKDDKKLsledkLDKST---LLTDQHEHGEEHEHEEEGHEhehhhhhggYDPHVWLDPKFDQTFAKEIKDELVKKD 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 164 PDKKKTFEKNAQAYLKKLQALDQAYQDGLKDAKQKNFVTQHAAFRYLALDYGLNQVAISGISPDsEPSAARLRELTEYIK 243
Cdd:NF033605  178 PKHKDEYEKNYKKLNKDLKGIDKDMKDITKDKQGNAVFISHESLGYLADRYGFVQKGVQNMNAE-DPSQKELTEIVKEIN 256

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 244 KNEIKVIYFEENASKSLAKTLSSEAGVELAVLNPLESLTDQEMKDGE-DYVSVMKENLKALEKTTSQAGK--DIQPEHEE 320
Cdd:NF033605  257 DSGAKYILYEDNVSNKVTDTIRKETDAKPLKFYNMESLNKEQQKDKDlTYQSLMKENIKNIDKALNDKIKvkDDKAESKH 336

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 321 DaKTVQKGYFEDSQVKDRSLANYAGDWKSVYPYLQDGTLDQVFDYKAKLNPTMTAAEYKEYYTKGYQTDIDRIKIDKDSM 400
Cdd:NF033605  337 D-KAISDGYFKDSQVKDRELSDYEGDWQSVYPYLKDGTLDEVMKHKAEDDGDMSAKEYKAYYDKGYKTDISNIKITGDTI 415

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 401 EFYQKGSSKKYTYKYVGKHILTYKKGNRGVRYLFEAKESDAGDF-KYVQFSDHEITPVKAAHFHIFHGGKSQEALyDELE 479
Cdd:NF033605  416 TFTKNGKKVTGKYEYDGKDILKYEKGNRGVRYTFKLVGDANKDLpKYVQFSDHNIAPKKAEHFHIFMGNDKDKVL-KELD 494

                         490       500
                  ....*....|....*....|..
gi 1080617793 480 NWPTYYPSNLSGLEVAQEMLAH 501
Cdd:NF033605  495 NWPTYYPAKLSKDEIKEEMLAH 516
ZinT COG3443
Periplasmic Zn/Cd-binding protein ZinT [Inorganic ion transport and metabolism];
310-501 1.21e-105

Periplasmic Zn/Cd-binding protein ZinT [Inorganic ion transport and metabolism];


Pssm-ID: 442667  Cd Length: 191  Bit Score: 313.00  E-value: 1.21e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 310 AGKDIQPEHEEDAKTVQKGYFEDSQVKDRSLANYAGDWKSVYPYLQDGTLDQVFDYKAKLNPTMTAAEYKEYYTKGYQTD 389
Cdd:COG3443     1 HGHSHGHPHTEAEKKAYEGYFDDKDVKDRSLSDWEGDWQSVYPYLQDGTLDPVFEHKAKKDGDKTAEEYKAYYTKGYATD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 390 IDRIKIDKDSMEFYQKGSSKKYTYKYVGKHILTYKKGNRGVRYLFEAKESDAGDFKYVQFSDHEITPVKAAHFHIFHgGK 469
Cdd:COG3443    81 VDRIVIEGNTVTFHKNGKVKSCEYKYDGYKILTYKSGNRGVRYLFECKDADAGAPKYIQFSDHIIAPEKSAHFHIYW-GN 159

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1080617793 470 SQEALYDELENWPTYYPSNLSGLEVAQEMLAH 501
Cdd:COG3443   160 DQEALLEEMDNWPTYYPYQLSGDQIVDEMLAH 191
ZnuA COG0803
ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and ...
 22-299 4.72e-103

ABC-type Zn uptake system ZnuABC, Zn-binding component ZnuA [Inorganic ion transport and metabolism];


Pssm-ID: 440566 [Multi-domain]  Cd Length: 286  Bit Score: 310.25  E-value: 4.72e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793  22 SKSQSQNGKLKVMTTFYPVYDFTKNIVGDEGTVDLLIGAGSEPHEYELSAKGRAMIQDSDVFVYENENMETWVPNLLKSM 101
Cdd:COG0803    21 AAASSAAGKLKVVATFSPLADLAKQIGGDKVEVTSLVPPGADPHDYEPTPSDIAKLAKADLVVYNGLGLEGWLDKLLEAA 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 102 KDKKTKVIDATKGMVLLPgleeehehEGGEEHHHEYDPHLWLSPHRAMKMVESIRDQLVAAYPDKKKTFEKNAQAYLKKL 181
Cdd:COG0803   101 GNPGVPVVDASEGIDLLE--------LEEGHDHGEPDPHVWLDPKNAKKVAENIADALAELDPANAAYYEANAAAYLAEL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 182 QALDQAYQDGLKDAKQKNFVTQHAAFRYLALDYGLNQVAISGISPDSEPSAARLRELTEYIKKNEIKVIYFEENASKSLA 261
Cdd:COG0803   173 DALDAEIKAKLAAIPGRKLVTSHDAFGYLARAYGLEVVAIQGISPGSEPSPADLAELIDLIKEEGVKAIFVESQVSPKLA 252

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1080617793 262 KTLSSEAGVELAVLNPLESLTDqemkDGEDYVSVMKEN 299
Cdd:COG0803   253 ETLAEETGVKVLYLDSLGGPGG----PGDTYLDMMRHN 286
ZnuA pfam01297
Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins ...
 33-305 1.15e-98

Zinc-uptake complex component A periplasmic; ZnuA includes periplasmic solute binding proteins such as TroA that interacts with an ATP-binding cassette transport system in Treponema pallidum. ZnuA is part of the bacterial zinc-uptake complex ZnuABC, whose components are the following families, ZinT, pfam09223, pfam00950, pfam00005, all of which are regulated by the transcription-regulator family FUR, pfam01475. ZinT acts as a Zn2+-buffering protein that delivers Zn2+ to ZnuA (TroA), a high-affinity zinc-uptake protein. In Gram-negative bacteria the ZnuABC transporter system ensures an adequate import of zinc in Zn2+-poor environments, such as those encountered by pathogens within the infected host.


Pssm-ID: 460151 [Multi-domain]  Cd Length: 269  Bit Score: 298.31  E-value: 1.15e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793  33 VMTTFYPVYDFTKNIVGDEGTVDLLIGAGSEPHEYELSAKGRAMIQDSDVFVYENENMETWVPNLLKSMKDKKtkVIDAT 112
Cdd:pfam01297   1 VVATTYPLADLAKQIGGDRVEVTSLVPPGADPHDYEPTPSDIAALSDADLVVYNGLGLEPWLDKLLEALPNKK--VVDAS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 113 KGMvllPGLEEEHEHEGGEEHHHEYDPHLWLSPHRAMKMVESIRDQLVAAYPDKKKTFEKNAQAYLKKLQALDQAYQDGL 192
Cdd:pfam01297  79 EGV---ELLDEEGEEEDHDGHDHGYDPHVWLDPKNAKKMAENIADALSELDPANAATYEANAAAYLAELDALDAEIKEQL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 193 KDAKQKN--FVTQHAAFRYLALDYGLNQVAISGISPDSEPSAARLRELTEYIKKNEIKVIYFEENASKSLAKTLSSEAGV 270
Cdd:pfam01297 156 ASIPEKTrkLVTSHDAFGYLARAYGLEQVGIQGVSPESEPSAADLAELIDLIKEKKVKAIFVEPQVSPKLAETVAKETGV 235

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1080617793 271 ElaVLNPLESLTDQEMKDGEDYVSVMKENLKALEK 305
Cdd:pfam01297 236 K--VLGPLYTDSLGEPGGGATYLDLMRHNLDTLAE 268
PRK10306 PRK10306
zinc/cadmium-binding protein; Provisional
 328-501 8.65e-66

zinc/cadmium-binding protein; Provisional


Pssm-ID: 182368 [Multi-domain]  Cd Length: 216  Bit Score: 211.56  E-value: 8.65e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 328 GYFEDSQVKDRSLANYAGDWKSVYPYLQDGTLDQVFDYKAKLNPTMTAAEYKEYYTKGYQTDIDRIKIDKDSMEFYQKGS 407
Cdd:PRK10306   43 GVFDDANVQDRTLSDWDGVWQSVYPYLQSGKLDPVFQKKAKKDKTKTFEEIKAYYRKGYATDVEMIGIENGIVEFHRGNE 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 408 SKKYTYKYVGKHILTYKKGNRGVRYLFEAKESDAGDFKYVQFSDHEITPVKAAHFHIFHGGKSQEALYDELENWPTYYPS 487
Cdd:PRK10306  123 VTSCKYDYDGYKILTYASGKKGVRYLFECKDAESKAPKYVQFSDHIIAPRKSSHFHIFMGNDSQQALLNEMENWPTYYPY 202

                         170
                  ....*....|....
gi 1080617793 488 NLSGLEVAQEMLAH 501
Cdd:PRK10306  203 QLSSEEVVDEMLHH 216
PsaA cd01137
Metal binding protein PsaA. These proteins have been shown to function as initial receptors ...
 21-303 4.60e-62

Metal binding protein PsaA. These proteins have been shown to function as initial receptors in ABC transport of Mn2+ and as surface adhesins in some eubacterial species. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).


Pssm-ID: 238557 [Multi-domain]  Cd Length: 287  Bit Score: 204.43  E-value: 4.60e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793  21 CSKSQSQNGKLKVMTTFYPVYDFTKNIVGDEGTVDLLIGAGSEPHEYELSAKGRAMIQDSDVFVYENENMETWVPNLLKS 100
Cdd:cd01137     8 GSSPATAASKLKVVATFSILADIARNIAGDRVNVTSIVPPGADPHEYEPTPSDIKKLSKADLILYNGLNLEPWLERLVKN 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 101 MKDKKtKVIDATKGMVLLPGleeeheheGGEEHHHEYDPHLWLSPHRAMKMVESIRDQLVAAYPDKKKTFEKNAQAYLKK 180
Cdd:cd01137    88 AGKDV-PVVAVSEGIDPIPL--------EEGHYKGKPDPHAWMSPKNAIIYVKNIAKALSEADPANAETYQKNAAAYKAK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 181 LQALDQAYQDGLKD--AKQKNFVTQHAAFRYLALDYGLNQVAISGISPDSEPSAARLRELTEYIKKNEIKVIYFEENASK 258
Cdd:cd01137   159 LKALDEWAKAKFATipAEKRKLVTSEGAFSYFAKAYGLKEAYLWPINTEEEGTPKQVATLIEQVKKEKVPAVFVESTVND 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1080617793 259 SLAKTLSSEAGVELAvlNPL--ESLTDQEmKDGEDYVSVMKENLKAL 303
Cdd:cd01137   239 RLMKQVAKETGAKIG--GQLytDSLSEKG-GPADTYLDMMEHNLDTI 282
ZnuA cd01019
Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in ...
 32-304 2.17e-59

Zinc binding protein ZnuA. These proteins have been shown to function as initial receptors in the ABC uptake of Zn2+. They belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. They are comprised of two globular subdomains connected by a single helix and bind their specific ligands in the cleft between these domains. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).


Pssm-ID: 238501 [Multi-domain]  Cd Length: 286  Bit Score: 197.21  E-value: 2.17e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793  32 KVMTTFYPVYDFTKNIVGDEGTVDLLIGAGSEPHEYELSAKGRAMIQDSDVFVYENENMETWVPNLLKsmKDKKTKVIDA 111
Cdd:cd01019     5 SVLTSIKPLGFIAAAIMGGVGEVEVLVPPGASPHDYELRPSDARKLQEADLVVWIGPDLEAFLDKVLQ--GRKKGKVLTL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 112 TKGMVLLPGLEEEHEHEGGEEHHHE-----------YDPHLWLSPHRAMKMVESIRDQLVAAYPDKKKTFEKNAQAYLKK 180
Cdd:cd01019    83 AKLIDLKTLEDGASHGDHEHDHEHAhgehdgheeggLDPHLWLSPENAAEVAQAVAEKLSALDPDNAATYAANLEAFNAR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 181 LQALDQAYQDGLKDAKQKNFVTQHAAFRYLALDYGLNQVAISGISPDSEPSAARLRELTEYIKKNEIKVIYFEENASKSL 260
Cdd:cd01019   163 LAELDATIKERLAPVKTKPFFVFHDAYGYFEKRYGLTQAGVFTIDPEIDPGAKRLAKIRKEIKEKGATCVFAEPQFHPKI 242

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1080617793 261 AKTLSSEAGVELAVLNPLESLTDQEmkdGEDYVSVMKENLKALE 304
Cdd:cd01019   243 AETLAEGTGAKVGELDPLGGLIELG---KNSYVNFLRNLADSLA 283
ZntC cd01018
Metal binding protein ZntC. These proteins are predicted to function as initial receptors in ...
 30-287 1.19e-44

Metal binding protein ZntC. These proteins are predicted to function as initial receptors in ABC transport of metal ions. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. They are comprised of two globular subdomains connected by a long alpha helix and bind their specific ligands in the cleft between these domains. In addition, many of these proteins possess a metal-binding histidine-rich motif (repetitive HDH sequence).


Pssm-ID: 238500 [Multi-domain]  Cd Length: 266  Bit Score: 157.91  E-value: 1.19e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793  30 KLKVMTTFYPVYDFTKNIVGDEGTVDLLIGAGSEPHEYELSAKGRAMIQDSDVFVYENENME-TWVPNLLKSmkDKKTKV 108
Cdd:cd01018     2 KPTVAVSIEPQKYFVEKIAGDTVDVVVLVPPGSNPHTYEPKPQQMKKLSEADLYFRIGLGFEeVWLERFRSN--NPKMQV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 109 IDATKGMVLLP--GLEEEHEHEGGEEHHHEYDPHLWLSPHRAMKMVESIRDQLVAAYPDKKKTFEKNAQAYLKKLQALDQ 186
Cdd:cd01018    80 VNMSKGITLIPmaDHHHHHHGEHEHHHHGNYDPHIWLSPANAKIMAENIYEALAELDPQNATYYQANLDALLAELDALDS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 187 AYQDGLKDAKQKNFVTQHAAFRYLALDYGLNQVAISgiSPDSEPSAARLRELTEYIKKNEIKVIYFEENASKSLAKTLSS 266
Cdd:cd01018   160 EIRTILSKLKQRAFMVYHPAWGYFARDYGLTQIPIE--EEGKEPSPADLKRLIDLAKEKGVRVVFVQPQFSTKSAEAIAR 237

                         250       260
                  ....*....|....*....|.
gi 1080617793 267 EAGVELAVLNPLESLTDQEMK 287
Cdd:cd01018   238 EIGAKVVTIDPLAADWEENLL 258
ZnuA COG4531
ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion ...
 32-278 1.18e-43

ABC-type Zn2+ transport system, periplasmic component/surface adhesin ZnuA [Inorganic ion transport and metabolism];


Pssm-ID: 443599 [Multi-domain]  Cd Length: 300  Bit Score: 156.14  E-value: 1.18e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793  32 KVMTTFYPVYDFTKNIVGDEGTVDLLIGAGSEPHEYELSAKGRAMIQDSDVFVYENENMETWVPNLLKSMKDKKTKV-ID 110
Cdd:COG4531    11 RVVTSIKPLHSLVAAVMDGVGEPELLLPPGASPHDYALRPSDARALQDADLVFWVGPDLEPFLEKPLETLAPDAKVVeLL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 111 ATKGMVLLP----GLEEEHEHEGGEEHHHE------------YDPHLWLSPHRAMKMVESIRDQLVAAYPDKKKTFEKNA 174
Cdd:COG4531    91 ELPGLTLLPfregGDFEHHDHHDEHHHHHHhhddhhdhhhggYDPHLWLSPENAKAWAAAIADALSELDPENAATYQANA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 175 QAYLKKLQALDQAYQDGLKDAKQKNFVTQHAAFRYLALDYGLNQV-AISgISPDSEPSAARLRELTEYIKKNEIKVIYFE 253
Cdd:COG4531   171 AAFEARLDALDAEIAAQLAPVKGKPFFVFHDAYQYFEKRFGLNALgAIT-LNPEIQPGAKRLAEIREKLKELGAVCVFAE 249

                         250       260
                  ....*....|....*....|....*
gi 1080617793 254 ENASKSLAKTLSSEAGVELAVLNPL 278
Cdd:COG4531   250 PQFNPALVETVAEGTGVRTGVLDPL 274
TroA cd01016
Metal binding protein TroA. These proteins have been shown to function as initial receptors in ...
 30-299 1.44e-31

Metal binding protein TroA. These proteins have been shown to function as initial receptors in ABC transport of Zn2+ and possibly Fe3+ in many eubacterial species. The TroA proteins belong to the TroA superfamily of periplasmic metal binding proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).


Pssm-ID: 238498 [Multi-domain]  Cd Length: 276  Bit Score: 122.47  E-value: 1.44e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793  30 KLKVMTTFYPVYDFTKNIVGDEGTVDLLIGAGSEPHEYELSAKGRAMIQDSDVFVYENENMETwvpnllkSMKDKKTKVi 109
Cdd:cd01016     1 KPNVVTTTGMIADAVENIGGDHVEVTGLMGPGVDPHLYKATAGDVEKLQNADVVFYNGLHLEG-------KMSDVLSKL- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 110 dATKGMVLLPGLEEEHEHEGGEEHHHEYDPHLWLSPHRAMKMVESIRDQLVAAYPDKKKTFEKNAQAYLKKLQALDQAYQ 189
Cdd:cd01016    73 -GSSKSVIALEDTLDRSQLILDEEEGTYDPHIWFDVKLWKYAVKAVAEVLSEKLPEHKDEFQANSEAYVEELDSLDAYAK 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 190 DGLKD--AKQKNFVTQHAAFRYLALDYGLNQVAISGISPDSEPSAARLRELTEYIKKNEIKVIYFEENAS-KSLAKTLSS 266
Cdd:cd01016   152 KKIAEipEQQRVLVTAHDAFGYFGRAYGFEVKGLQGISTDSEAGLRDINELVDLIVERKIKAIFVESSVNqKSIEALQDA 231

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1080617793 267 --EAGVELAVLNPL--ESLTDQEMKDGeDYVSVMKEN 299
Cdd:cd01016   232 vkARGHDVQIGGELysDAMGEEGTSEG-TYIGMFKHN 267
TroA_b cd01020
Metal binding protein TroA_b. These proteins are predicted to function as initial receptors ...
 29-308 3.29e-24

Metal binding protein TroA_b. These proteins are predicted to function as initial receptors in ABC transport of metal ions. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind the metal ion in the cleft between these domains. In addition, these proteins sometimes have a low complexity region containing a metal-binding histidine-rich motif (repetitive HDH sequence).


Pssm-ID: 238502 [Multi-domain]  Cd Length: 264  Bit Score: 101.75  E-value: 3.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793  29 GKLKVMTT--FYPvyDFTKNIVGDEGTVDLLIGAGS-EPHEYELSAKGRAMIQDSDVFVYENENMETWvpnLLKSMKDKK 105
Cdd:cd01020     1 GKINVVAStnFWG--SVAEAVGGDHVEVTSIITNPDvDPHDFEPTPTDAAKVSTADIVVYNGGGYDPW---MTKLLADTK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 106 TKVIDATKGMVLlpgleeeheheggeEHHHEYDPHLWLSPHRAMKMVESIRDQLVAAYPDKKKTFEKNAQAYLKKLQALD 185
Cdd:cd01020    76 DVIVIAADLDGH--------------DDKEGDNPHLWYDPETMSKVANALADALVKADPDNKKYYQANAKKFVASLKPLA 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 186 QAYQDGLKDAKQKNFVTQHAAFRYLALDYGL---NQVAISGIS-PDSEPSAARLRELTEYIKKNEIKVIYFEENASKSLA 261
Cdd:cd01020   142 AKIAELSAKYKGAPVAATEPVFDYLLDALGMkerTPKGYTATTeSETEPSPADIAAFQNAIKNRQIDALIVNPQQASSAT 221

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1080617793 262 KTLSS---EAGVelavlnPLESLTDQeMKDGEDYVSVMKENLKALEKTTS 308
Cdd:cd01020   222 TNITGlakRSGV------PVVEVTET-MPNGTTYLTWMLKQVDQLEKALQ 264
TroA_c cd01145
Periplasmic binding protein TroA_c. These proteins are predicted to function as initial ...
 30-229 6.07e-24

Periplasmic binding protein TroA_c. These proteins are predicted to function as initial receptors in the ABC metal ion uptake in eubacteria and archaea. They belong to the TroA superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA protein is comprised of two globular subdomains connected by a single helix and can bind their ligands in the cleft between these domains.


Pssm-ID: 238565 [Multi-domain]  Cd Length: 203  Bit Score: 99.11  E-value: 6.07e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793  30 KLKVMTTFYPVYDFTKNIVGDEGTVDLLIGAGSEPHEYELSAKGRAMIQDSDVFVYENENMETWVPNLLksMKDKKTKVI 109
Cdd:cd01145     2 ALNVVVTFPDLKDLVREVAGDAVIVSALTPPGVDPHQYQLKPSDIAKMRKADLVVTSGHELEGFEPKLA--ELSSNSKVQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 110 DATKGMVLLPgLEEEHEHEGGEEHHHEYDPHLWLSPHRAMKMVESIRDQLVAAYPDKKKTFEKNAQAYLKKLQALDQAYQ 189
Cdd:cd01145    80 PGIKILIEDS-DTVGMVDRAMGDYHGKGNPHVWLDPNNAPALAKALADALIELDPSEQEEYKENLRVFLAKLNKLLREWE 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1080617793 190 DGLKDAKQKNFVTQHAAFRYLALDYGLNQVAIsgISPDSE 229
Cdd:cd01145   159 RQFEGLKGIQVVAYHPSYQYLADWLGIEVVAS--LEPLPE 196
anch_rpt_subst TIGR03772
anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ...
 138-305 1.25e-19

anchored repeat ABC transporter, substrate-binding protein; Members of this protein family are ABC transporter permease subunits as identified by pfam00950, but additionally contain the Actinobacterial insert domain described by TIGR03769. Some homologs (lacking the insert) have been described as transporters of manganese or of chelated iron. Members of this family typically are found along with an ATP-binding cassette protein, a permease, and an LPXTG-anchored protein with two or three copies of the TIGR03769 insert that occurs just once in this protein family. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 163484 [Multi-domain]  Cd Length: 479  Bit Score: 91.46  E-value: 1.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 138 DPHLWLSPHRAMKMVESIRDQLVAAYPDKKKTFEKNAQAYLKKLQALDQAYQDGLKD--AKQKNFVTQHAAFRYLALDYG 215
Cdd:TIGR03772 310 DPHLWHNVKNAIAYVEVIRDKLIEVDPRGAQAYRSNASAYIHRLERLDTYVRRTIATipPSRRHLITTHDAYSYLGQAYG 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 216 LNQVAISGISPDSEPSAARLRELTEYIKKNEIKVIYFEEN---ASKSLAKTlSSEAGVELAVLNPlESLTDqemkDGEDY 292
Cdd:TIGR03772 390 LNIAGFVTPNPAVEPSLADRRRLTRTIENLKVPAVFLEPNlaaRSTTLNEI-ADELGVRVCAIYG-DTFDD----DVTNY 463

                         170
                  ....*....|...
gi 1080617793 293 VSVMKENLKALEK 305
Cdd:TIGR03772 464 VDLMRFNADSLAD 476
znuA PRK09545
zinc ABC transporter substrate-binding protein ZnuA;
54-278 3.43e-15

zinc ABC transporter substrate-binding protein ZnuA;


Pssm-ID: 236558 [Multi-domain]  Cd Length: 311  Bit Score: 76.20  E-value: 3.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793  54 VDLLIGAGSEPHEYELSAKGRAMIQDSDVFVYENENMETWVPNLLKSMKDKKTKVIDATKG--MVLLPGLEEEHEHEGGE 131
Cdd:PRK09545   48 TEVLLPDGASPHDYSLRPSDVKRLQSADLVVWVGPEMEAFLEKPVSKLPENKQVTIAQLPDvkPLLMKGAHDDHHDDDHD 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1080617793 132 EHHHE----------YDPHLWLSPHRAMKMVESIRDQLVAAYPDKKKTFEKNAQAYLKKLQALDQAYQDGLKDAKQKNFV 201
Cdd:PRK09545  128 HAGHEksdedhhhgeYNMHIWLSPEIARATAVAIHDKLVELMPQSKAKLDANLKDFEAQLAQTDKQIGNQLAPVKGKGYF 207

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1080617793 202 TQHAAFRYLALDYGLNQVAISGISPDSEPSAARLRELTEYIKKNEIKVIYFEENASKSLAKTLSSEAGVELAVLNPL 278
Cdd:PRK09545  208 VFHDAYGYFEKHYGLTPLGHFTVNPEIQPGAQRLHEIRTQLVEQKATCVFAEPQFRPAVIESVAKGTSVRMGTLDPL 284
 
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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