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Conserved domains on  [gi|56693221|ref|NP_001008575|]
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proton-coupled zinc antiporter SLC30A9, mitochondrial [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FieF COG0053
Divalent metal cation (Fe/Co/Zn/Cd) efflux pump [Inorganic ion transport and metabolism];
243-568 1.88e-57

Divalent metal cation (Fe/Co/Zn/Cd) efflux pump [Inorganic ion transport and metabolism];


:

Pssm-ID: 439823 [Multi-domain]  Cd Length: 284  Bit Score: 193.78  E-value: 1.88e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221 243 KVVMVAICINGLNFFFKLLAWVYTGSASMFSEAIHSLADTCNQALLALGISQSVRNPDAIHPYGFSNMRYIASLISGVgI 322
Cdd:COG0053   3 RAALASLAANLLLAVLKLVAGLLTGSVALLADALHSLSDLVASLLVLLGLRLAAKPADEEHPYGHGKAEYLASLIVAV-L 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221 323 FMMGAGLSWYHGIMGLLHPQPIESLLWAYCILAGSLVSEGATLLVAINEIKKsartqglsfyeyvmqSRDPSTNVVLLED 402
Cdd:COG0053  82 ILLAGLFILYEAIERLLHPEPVEPSGLGLAVLLISIVVNEALARYLRRVGKK---------------TGSPALKADALHD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221 403 AAAVLGVVLAAGCMGLTSLTGNPYYDSLGSLGVGTLLGTVSAFLIYTNTEALLGRSIQAEHMQKLTEFLENDPAVRAIHD 482
Cdd:COG0053 147 RSDALTSLGVLIGLLLALLTGWPWLDPIAAILIGLLILKVAYKLARESLSLLMDEALDEELVERIRAIILSVPGVIGVHD 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221 483 VKATDMGlSKVRFKAEVDFDGrvvtrsylekqdieqilneiqqvktpeeleNFMLKHGENIIdtlgaevDRLEKELKQRN 562
Cdd:COG0053 227 LRTRKSG-PRIFVDLHIEVDP------------------------------DLTVEEAHDIA-------DRIEAALREEF 268

                ....*.
gi 56693221 563 PEVRHV 568
Cdd:COG0053 269 PGVADV 274
NTD_ZNT9 cd21078
N-terminal domain found in zinc transporter 9 (ZNT9) and similar proteins; ZNT9, also known as ...
132-220 1.02e-47

N-terminal domain found in zinc transporter 9 (ZNT9) and similar proteins; ZNT9, also known as solute carrier family 30 member 9 (SLC30A9), may act as a zinc transporter involved in intracellular zinc homeostasis and may also play a role as nuclear receptor coactivator.


:

Pssm-ID: 410964  Cd Length: 89  Bit Score: 161.21  E-value: 1.02e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221 132 QNNFITAVRAMNEFCLKPSDLEHLRKIRRRSPHDDTEAFTVFLRSDVEAKALEVWGSQEALARERDQRKEVEREYQENIF 211
Cdd:cd21078   1 ENNYITAVRAMNEYLLKPSDLEGLRKIKRRSPYDDEPPITVYLRSDVEAKAIEKWGSLEALEKERKKRKEIEEAYREYLF 80

                ....*....
gi 56693221 212 RNQKLLKEY 220
Cdd:cd21078  81 LLKKLLREY 89
 
Name Accession Description Interval E-value
FieF COG0053
Divalent metal cation (Fe/Co/Zn/Cd) efflux pump [Inorganic ion transport and metabolism];
243-568 1.88e-57

Divalent metal cation (Fe/Co/Zn/Cd) efflux pump [Inorganic ion transport and metabolism];


Pssm-ID: 439823 [Multi-domain]  Cd Length: 284  Bit Score: 193.78  E-value: 1.88e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221 243 KVVMVAICINGLNFFFKLLAWVYTGSASMFSEAIHSLADTCNQALLALGISQSVRNPDAIHPYGFSNMRYIASLISGVgI 322
Cdd:COG0053   3 RAALASLAANLLLAVLKLVAGLLTGSVALLADALHSLSDLVASLLVLLGLRLAAKPADEEHPYGHGKAEYLASLIVAV-L 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221 323 FMMGAGLSWYHGIMGLLHPQPIESLLWAYCILAGSLVSEGATLLVAINEIKKsartqglsfyeyvmqSRDPSTNVVLLED 402
Cdd:COG0053  82 ILLAGLFILYEAIERLLHPEPVEPSGLGLAVLLISIVVNEALARYLRRVGKK---------------TGSPALKADALHD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221 403 AAAVLGVVLAAGCMGLTSLTGNPYYDSLGSLGVGTLLGTVSAFLIYTNTEALLGRSIQAEHMQKLTEFLENDPAVRAIHD 482
Cdd:COG0053 147 RSDALTSLGVLIGLLLALLTGWPWLDPIAAILIGLLILKVAYKLARESLSLLMDEALDEELVERIRAIILSVPGVIGVHD 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221 483 VKATDMGlSKVRFKAEVDFDGrvvtrsylekqdieqilneiqqvktpeeleNFMLKHGENIIdtlgaevDRLEKELKQRN 562
Cdd:COG0053 227 LRTRKSG-PRIFVDLHIEVDP------------------------------DLTVEEAHDIA-------DRIEAALREEF 268

                ....*.
gi 56693221 563 PEVRHV 568
Cdd:COG0053 269 PGVADV 274
NTD_ZNT9 cd21078
N-terminal domain found in zinc transporter 9 (ZNT9) and similar proteins; ZNT9, also known as ...
132-220 1.02e-47

N-terminal domain found in zinc transporter 9 (ZNT9) and similar proteins; ZNT9, also known as solute carrier family 30 member 9 (SLC30A9), may act as a zinc transporter involved in intracellular zinc homeostasis and may also play a role as nuclear receptor coactivator.


Pssm-ID: 410964  Cd Length: 89  Bit Score: 161.21  E-value: 1.02e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221 132 QNNFITAVRAMNEFCLKPSDLEHLRKIRRRSPHDDTEAFTVFLRSDVEAKALEVWGSQEALARERDQRKEVEREYQENIF 211
Cdd:cd21078   1 ENNYITAVRAMNEYLLKPSDLEGLRKIKRRSPYDDEPPITVYLRSDVEAKAIEKWGSLEALEKERKKRKEIEEAYREYLF 80

                ....*....
gi 56693221 212 RNQKLLKEY 220
Cdd:cd21078  81 LLKKLLREY 89
Cation_efflux pfam01545
Cation efflux family; Members of this family are integral membrane proteins, that are found to ...
254-455 5.17e-39

Cation efflux family; Members of this family are integral membrane proteins, that are found to increase tolerance to divalent metal ions such as cadmium, zinc, and cobalt. These proteins are thought to be efflux pumps that remove these ions from cells.


Pssm-ID: 426316 [Multi-domain]  Cd Length: 189  Bit Score: 141.25  E-value: 5.17e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221   254 LNFFFKLLAWVYTGSASMFSEAIHSLADTCNQALLALGISQSVRNPDAIHPYGFSNMRYIASLISGVgIFMMGAGLSWYH 333
Cdd:pfam01545   1 LLALVKLAAGLLTGSLALLADAVHSLIDLISSLLALLALRLSRKPPDERFPFGHGRLEPLAALVVGI-LLLGGGVFLLYE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221   334 GIMGLLHPQPIESLLWAYCILAGSLVSEGATLLVAINEIKKsartqglsfyeyvmqSRDPSTNVVLLE---DAAAVLGVV 410
Cdd:pfam01545  80 SIQRLLSPGEEIDPGLALILALVSLLVNLFLLLYLRRAARR---------------IRSPALKADALHalsDVLASLGVL 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 56693221   411 LAAGCMGLTSLTGNPYYDSLGSLGVGTLLGTVSAFLIYTNTEALL 455
Cdd:pfam01545 145 ISALLIYLGPITGGLLADPLASLLIGLLILYTALRLLKESLSILL 189
CDF TIGR01297
cation diffusion facilitator family transporter; This model describes a broadly distributed ...
259-525 1.40e-26

cation diffusion facilitator family transporter; This model describes a broadly distributed family of transporters, a number of which have been shown to transport divalent cations of cobalt, cadmium and/or zinc. The family has six predicted transmembrane domains. Members of the family are variable in length because of variably sized inserts, often containing low-complexity sequence. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273544 [Multi-domain]  Cd Length: 268  Bit Score: 109.23  E-value: 1.40e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221   259 KLLAWVYTGSASMFSEAIHSLADTCNQALLALGISQSVRNPDAIHPYGFSNMRYIASLISGVGIFMMGAGLSWyHGIMGL 338
Cdd:TIGR01297   6 KIVGGLLSGSLALLADAIHSLSDVAASAIALLALRISRRPADERHPFGHGRAEILAALLNGLFLVVVALFILY-EAIERL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221   339 LHPQPIESLLWAYCILAGSLVsegATLLVAINEIKKSARTQglsfyeyvmqsrdpSTNV--VLLEDAAAVLGVVLAAGCM 416
Cdd:TIGR01297  85 INPEPEIDGGTMLIVAIVGLI---VNLILALYLHRVGHRLG--------------SLALraAALHVLSDALSSVGVLIGA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221   417 GLtSLTGNPYYDSLGSLGVGTLLGTVSAFLIYTNTEALLGRSIQAEHMQKLTEFLENDPAVRAIHDVKATDMGLSKVRFK 496
Cdd:TIGR01297 148 LL-IYFGWHWADPIAALLISLLILYTAFRLLKESINVLLDAAPDEEDLEEIKKAILSIPGVKGVHDLHIWRIGPGKLFLD 226
                         250       260
                  ....*....|....*....|....*....
gi 56693221   497 AEVDFDGRvvtrsyLEKQDIEQILNEIQQ 525
Cdd:TIGR01297 227 VHVVVDPD------LDLKQAHDIALEIER 249
rad14 TIGR00598
DNA repair protein; All proteins in this family for which functions are known are used for the ...
129-219 3.80e-10

DNA repair protein; All proteins in this family for which functions are known are used for the recognition of DNA damage as part of nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273164  Cd Length: 172  Bit Score: 59.04  E-value: 3.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221   129 KYTQNNFITAVRAMNEFCLKPSDLEH----LRKIRRRSPHDDTEA-FTVFLRSDVEAKALEVWGSQEALARERDQRKEVE 203
Cdd:TIGR00598  28 KDDKYKLLTKTEAKEEYLLKDCDLDKreplLRRIVKKNPHNPRWGdMKLYLKLQVEKRALEVWGSEEALDEEKERREESK 107
                          90
                  ....*....|....*.
gi 56693221   204 REYQENIFrnQKLLKE 219
Cdd:TIGR00598 108 EEMKEKKF--EKKLKE 121
RAD14 COG5145
DNA excision repair protein [DNA replication, recombination, and repair];
123-254 9.72e-07

DNA excision repair protein [DNA replication, recombination, and repair];


Pssm-ID: 227474  Cd Length: 292  Bit Score: 50.77  E-value: 9.72e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221 123 KREYGLKYTqnnFITAVRAMNEFCLKPSDL---EHLRKIRRRSPHDDTEA-FTVFLRSDVEAKALEVWGSQEALARERDQ 198
Cdd:COG5145 144 RHSMPDKYK---LLTKTECKSDYLLTDPELkdqELFRRLQKPNPHKGTWSkMHLYLREEVEQFAIKKWGSLEELDREKQR 220
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56693221 199 RKEVEREYQENIFRNQKL---LKEYKDFWGNTKPRSRKR-----ATFLQGP-GKVVMVAICINGL 254
Cdd:COG5145 221 REKMKDDRKEKKLEKKIKelrRKTRTSNYSRMDVREKEKhvhvfDEFVDGPnEPGVIIQRCSCGL 285
fieF PRK09509
CDF family cation-efflux pump FieF;
256-484 1.09e-05

CDF family cation-efflux pump FieF;


Pssm-ID: 181919 [Multi-domain]  Cd Length: 299  Bit Score: 47.36  E-value: 1.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221  256 FFFKLLAWVYTGSASMFSEAIHSLADTCNQALLALGISQSVRNPDAIHPYGFSNMRYIASL-----ISGVGIFMMgagls 330
Cdd:PRK09509  24 LLIKIFAWWYTGSVSLLAALVDSLVDIAASLTNLLVVRYSLQPADDEHTFGHGKAESLAALaqsmfISGSALFLF----- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221  331 wYHGIMGLLHPQPIESLLWAYCILAGSLVSEGATLLVAINEIKKSaRTQGLSFYEYVMQSRdpstnvvLLEDAAAVLGVV 410
Cdd:PRK09509  99 -LTGIQHLISPTPMNDPGVGIIVTLVALICTLILVTFQRWVVRKT-QSQAVRADMLHYQSD-------VMMNGAILLALG 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56693221  411 LaagcmgltSLTGNPYYDSLGSLGVGTLLgTVSAF-LIYTNTEALLGRSIQAEHMQKLTEFLENDPAVRAIHDVK 484
Cdd:PRK09509 170 L--------SWYGWHRADALFALGIGIYI-LYSALrMGYEAVQSLLDRALPDEERQEIIDIVTSWPGVSGAHDLR 235
 
Name Accession Description Interval E-value
FieF COG0053
Divalent metal cation (Fe/Co/Zn/Cd) efflux pump [Inorganic ion transport and metabolism];
243-568 1.88e-57

Divalent metal cation (Fe/Co/Zn/Cd) efflux pump [Inorganic ion transport and metabolism];


Pssm-ID: 439823 [Multi-domain]  Cd Length: 284  Bit Score: 193.78  E-value: 1.88e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221 243 KVVMVAICINGLNFFFKLLAWVYTGSASMFSEAIHSLADTCNQALLALGISQSVRNPDAIHPYGFSNMRYIASLISGVgI 322
Cdd:COG0053   3 RAALASLAANLLLAVLKLVAGLLTGSVALLADALHSLSDLVASLLVLLGLRLAAKPADEEHPYGHGKAEYLASLIVAV-L 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221 323 FMMGAGLSWYHGIMGLLHPQPIESLLWAYCILAGSLVSEGATLLVAINEIKKsartqglsfyeyvmqSRDPSTNVVLLED 402
Cdd:COG0053  82 ILLAGLFILYEAIERLLHPEPVEPSGLGLAVLLISIVVNEALARYLRRVGKK---------------TGSPALKADALHD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221 403 AAAVLGVVLAAGCMGLTSLTGNPYYDSLGSLGVGTLLGTVSAFLIYTNTEALLGRSIQAEHMQKLTEFLENDPAVRAIHD 482
Cdd:COG0053 147 RSDALTSLGVLIGLLLALLTGWPWLDPIAAILIGLLILKVAYKLARESLSLLMDEALDEELVERIRAIILSVPGVIGVHD 226
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221 483 VKATDMGlSKVRFKAEVDFDGrvvtrsylekqdieqilneiqqvktpeeleNFMLKHGENIIdtlgaevDRLEKELKQRN 562
Cdd:COG0053 227 LRTRKSG-PRIFVDLHIEVDP------------------------------DLTVEEAHDIA-------DRIEAALREEF 268

                ....*.
gi 56693221 563 PEVRHV 568
Cdd:COG0053 269 PGVADV 274
NTD_ZNT9 cd21078
N-terminal domain found in zinc transporter 9 (ZNT9) and similar proteins; ZNT9, also known as ...
132-220 1.02e-47

N-terminal domain found in zinc transporter 9 (ZNT9) and similar proteins; ZNT9, also known as solute carrier family 30 member 9 (SLC30A9), may act as a zinc transporter involved in intracellular zinc homeostasis and may also play a role as nuclear receptor coactivator.


Pssm-ID: 410964  Cd Length: 89  Bit Score: 161.21  E-value: 1.02e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221 132 QNNFITAVRAMNEFCLKPSDLEHLRKIRRRSPHDDTEAFTVFLRSDVEAKALEVWGSQEALARERDQRKEVEREYQENIF 211
Cdd:cd21078   1 ENNYITAVRAMNEYLLKPSDLEGLRKIKRRSPYDDEPPITVYLRSDVEAKAIEKWGSLEALEKERKKRKEIEEAYREYLF 80

                ....*....
gi 56693221 212 RNQKLLKEY 220
Cdd:cd21078  81 LLKKLLREY 89
Cation_efflux pfam01545
Cation efflux family; Members of this family are integral membrane proteins, that are found to ...
254-455 5.17e-39

Cation efflux family; Members of this family are integral membrane proteins, that are found to increase tolerance to divalent metal ions such as cadmium, zinc, and cobalt. These proteins are thought to be efflux pumps that remove these ions from cells.


Pssm-ID: 426316 [Multi-domain]  Cd Length: 189  Bit Score: 141.25  E-value: 5.17e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221   254 LNFFFKLLAWVYTGSASMFSEAIHSLADTCNQALLALGISQSVRNPDAIHPYGFSNMRYIASLISGVgIFMMGAGLSWYH 333
Cdd:pfam01545   1 LLALVKLAAGLLTGSLALLADAVHSLIDLISSLLALLALRLSRKPPDERFPFGHGRLEPLAALVVGI-LLLGGGVFLLYE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221   334 GIMGLLHPQPIESLLWAYCILAGSLVSEGATLLVAINEIKKsartqglsfyeyvmqSRDPSTNVVLLE---DAAAVLGVV 410
Cdd:pfam01545  80 SIQRLLSPGEEIDPGLALILALVSLLVNLFLLLYLRRAARR---------------IRSPALKADALHalsDVLASLGVL 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 56693221   411 LAAGCMGLTSLTGNPYYDSLGSLGVGTLLGTVSAFLIYTNTEALL 455
Cdd:pfam01545 145 ISALLIYLGPITGGLLADPLASLLIGLLILYTALRLLKESLSILL 189
CDF TIGR01297
cation diffusion facilitator family transporter; This model describes a broadly distributed ...
259-525 1.40e-26

cation diffusion facilitator family transporter; This model describes a broadly distributed family of transporters, a number of which have been shown to transport divalent cations of cobalt, cadmium and/or zinc. The family has six predicted transmembrane domains. Members of the family are variable in length because of variably sized inserts, often containing low-complexity sequence. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273544 [Multi-domain]  Cd Length: 268  Bit Score: 109.23  E-value: 1.40e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221   259 KLLAWVYTGSASMFSEAIHSLADTCNQALLALGISQSVRNPDAIHPYGFSNMRYIASLISGVGIFMMGAGLSWyHGIMGL 338
Cdd:TIGR01297   6 KIVGGLLSGSLALLADAIHSLSDVAASAIALLALRISRRPADERHPFGHGRAEILAALLNGLFLVVVALFILY-EAIERL 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221   339 LHPQPIESLLWAYCILAGSLVsegATLLVAINEIKKSARTQglsfyeyvmqsrdpSTNV--VLLEDAAAVLGVVLAAGCM 416
Cdd:TIGR01297  85 INPEPEIDGGTMLIVAIVGLI---VNLILALYLHRVGHRLG--------------SLALraAALHVLSDALSSVGVLIGA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221   417 GLtSLTGNPYYDSLGSLGVGTLLGTVSAFLIYTNTEALLGRSIQAEHMQKLTEFLENDPAVRAIHDVKATDMGLSKVRFK 496
Cdd:TIGR01297 148 LL-IYFGWHWADPIAALLISLLILYTAFRLLKESINVLLDAAPDEEDLEEIKKAILSIPGVKGVHDLHIWRIGPGKLFLD 226
                         250       260
                  ....*....|....*....|....*....
gi 56693221   497 AEVDFDGRvvtrsyLEKQDIEQILNEIQQ 525
Cdd:TIGR01297 227 VHVVVDPD------LDLKQAHDIALEIER 249
CzcD COG1230
Co/Zn/Cd efflux system component [Inorganic ion transport and metabolism];
242-543 2.32e-16

Co/Zn/Cd efflux system component [Inorganic ion transport and metabolism];


Pssm-ID: 440843 [Multi-domain]  Cd Length: 294  Bit Score: 79.78  E-value: 2.32e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221 242 GKVVMVAICINGLNFFFKLLAWVYTGSASMFSEAIHSLADTcnqalLALGIS-----QSVRNPDAIHPYGFSNMRYIASL 316
Cdd:COG1230  17 ERRLLIALALTLGFMVVEIVGGLLSGSLALLADAGHMLSDA-----LALGLAlfayrLARRPADARFTFGYKRAEILAAL 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221 317 ISGVGIFMMGAGLSWyHGIMGLLHPQPIES--LLWAycilagslvsegATLLVAINeikksartqGLSFYeYVMQSRDPS 394
Cdd:COG1230  92 ANALLLLVVAGYILY-EAIQRLFNPPPVAGggMLVV------------AVIGLVVN---------LVSAW-LLHRGSKHD 148
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221 395 TNVV-----LLEDAAAVLGVVLAAgcmGLTSLTGNPYYDSLGSLGVGTLLGtVSAF-LIYTNTEALLGRSIQAEHMQKLT 468
Cdd:COG1230 149 LNLRgaylhVLADALGSVAVIVAA---LVILFTGWTWLDPLLSLLIALLIL-RSAWgLLRESLRILLEGVPDGIDLEEVR 224
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56693221 469 EFLENDPAVRAIHDVKATDMGLSKVRFKAEVDFDgrvvtrsylEKQDIEQILNEIQQvktpeelenfMLKHGENI 543
Cdd:COG1230 225 AALEALPGVADVHDLHVWSLSSGENALTAHVVVD---------DGADADAILDEIRE----------LLAERFGI 280
DBD_XPA-like cd21075
DNA-binding domain found in DNA repair protein complementing XP-A cells (XPA), yeast DNA ...
136-199 6.38e-15

DNA-binding domain found in DNA repair protein complementing XP-A cells (XPA), yeast DNA repair protein RAD14 and similar proteins; The family includes DNA repair protein complementing XP-A cells (XPA), yeast DNA repair protein RAD14, zinc transporter 9 (ZNT9) and similar proteins. XPA, also known as xeroderma pigmentosum group A-complementing protein (XPAC), is involved in DNA excision repair. It initiates repair by binding to damaged sites with various affinities, depending on the photoproduct and the transcriptional state of the region. Rad14 is involved in nucleotide excision repair. It binds specifically to damaged DNA and is required for the incision step. Rad14 is a component of the nucleotide excision repair factor 1 (NEF1) complex consisting of Rad1, Rad10 and Rad14. ZNT9, also known as solute carrier family 30 member 9 (SLC30A9), may act as a zinc transporter involved in intracellular zinc homeostasis and may also play a role as nuclear receptor coactivator. The model corresponds to the DNA-binding domain found in XPA and Rad14. It consists of a conserved N-terminal zinc-binding subdomain and a C-terminal alpha/beta fold subdomain. ZNT9 contains only C-terminal alpha/beta fold subdomain but lacks of N-terminal zinc-binding subdomain.


Pssm-ID: 410961  Cd Length: 67  Bit Score: 69.54  E-value: 6.38e-15
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56693221 136 ITAVRAMNEFCLKPSDLEHLRKIRRRSPHDDTEAFT-VFLRSDVEAKALEVWGSQEALARERDQR 199
Cdd:cd21075   3 ITKTDAKKEYRLTDKDLAGLPYEEKPNPHGPSAAPMkLYLEREVERLAWRKHGGPEGLEAALEKR 67
DBD_XPA cd21076
DNA-binding domain found in DNA repair protein complementing XP-A cells (XPA) and similar ...
135-199 1.09e-12

DNA-binding domain found in DNA repair protein complementing XP-A cells (XPA) and similar proteins; XPA, also known as xeroderma pigmentosum group A-complementing protein (XPAC), is involved in DNA excision repair. It initiates repair by binding to damaged sites with various affinities, depending on the photoproduct and the transcriptional state of the region.


Pssm-ID: 410962 [Multi-domain]  Cd Length: 107  Bit Score: 64.58  E-value: 1.09e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221 135 FITAVRAMNEFCLKPSDLEH----LRKIRRRSPHDDTEA-FTVFLRSDVEAKALEVWGSQEALARERDQR 199
Cdd:cd21076  38 LITKTEAKQEYLLKDCDLDKreppLKFILKKNPHNSRWGdMKLYLKLQVEKRALEVWGSEEALEEEKEKR 107
rad14 TIGR00598
DNA repair protein; All proteins in this family for which functions are known are used for the ...
129-219 3.80e-10

DNA repair protein; All proteins in this family for which functions are known are used for the recognition of DNA damage as part of nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273164  Cd Length: 172  Bit Score: 59.04  E-value: 3.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221   129 KYTQNNFITAVRAMNEFCLKPSDLEH----LRKIRRRSPHDDTEA-FTVFLRSDVEAKALEVWGSQEALARERDQRKEVE 203
Cdd:TIGR00598  28 KDDKYKLLTKTEAKEEYLLKDCDLDKreplLRRIVKKNPHNPRWGdMKLYLKLQVEKRALEVWGSEEALDEEKERREESK 107
                          90
                  ....*....|....*.
gi 56693221   204 REYQENIFrnQKLLKE 219
Cdd:TIGR00598 108 EEMKEKKF--EKKLKE 121
RAD14 COG5145
DNA excision repair protein [DNA replication, recombination, and repair];
123-254 9.72e-07

DNA excision repair protein [DNA replication, recombination, and repair];


Pssm-ID: 227474  Cd Length: 292  Bit Score: 50.77  E-value: 9.72e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221 123 KREYGLKYTqnnFITAVRAMNEFCLKPSDL---EHLRKIRRRSPHDDTEA-FTVFLRSDVEAKALEVWGSQEALARERDQ 198
Cdd:COG5145 144 RHSMPDKYK---LLTKTECKSDYLLTDPELkdqELFRRLQKPNPHKGTWSkMHLYLREEVEQFAIKKWGSLEELDREKQR 220
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56693221 199 RKEVEREYQENIFRNQKL---LKEYKDFWGNTKPRSRKR-----ATFLQGP-GKVVMVAICINGL 254
Cdd:COG5145 221 REKMKDDRKEKKLEKKIKelrRKTRTSNYSRMDVREKEKhvhvfDEFVDGPnEPGVIIQRCSCGL 285
fieF PRK09509
CDF family cation-efflux pump FieF;
256-484 1.09e-05

CDF family cation-efflux pump FieF;


Pssm-ID: 181919 [Multi-domain]  Cd Length: 299  Bit Score: 47.36  E-value: 1.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221  256 FFFKLLAWVYTGSASMFSEAIHSLADTCNQALLALGISQSVRNPDAIHPYGFSNMRYIASL-----ISGVGIFMMgagls 330
Cdd:PRK09509  24 LLIKIFAWWYTGSVSLLAALVDSLVDIAASLTNLLVVRYSLQPADDEHTFGHGKAESLAALaqsmfISGSALFLF----- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221  331 wYHGIMGLLHPQPIESLLWAYCILAGSLVSEGATLLVAINEIKKSaRTQGLSFYEYVMQSRdpstnvvLLEDAAAVLGVV 410
Cdd:PRK09509  99 -LTGIQHLISPTPMNDPGVGIIVTLVALICTLILVTFQRWVVRKT-QSQAVRADMLHYQSD-------VMMNGAILLALG 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 56693221  411 LaagcmgltSLTGNPYYDSLGSLGVGTLLgTVSAF-LIYTNTEALLGRSIQAEHMQKLTEFLENDPAVRAIHDVK 484
Cdd:PRK09509 170 L--------SWYGWHRADALFALGIGIYI-LYSALrMGYEAVQSLLDRALPDEERQEIIDIVTSWPGVSGAHDLR 235
DBD_Rad14 cd21077
DNA-binding domain found in yeast DNA repair protein Rad14 and similar proteins; Rad14 is ...
123-199 1.32e-04

DNA-binding domain found in yeast DNA repair protein Rad14 and similar proteins; Rad14 is involved in nucleotide excision repair. It binds specifically to damaged DNA and is required for the incision step. Rad14 is a component of the nucleotide excision repair factor 1 (NEF1) complex consisting of Rad1, Rad10 and Rad14.


Pssm-ID: 410963 [Multi-domain]  Cd Length: 105  Bit Score: 41.23  E-value: 1.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221 123 KREYGLKYTqnnFITAVRAMNEFCLKPSDL---EHLRKIRRRSPHDDT-EAFTVFLRSDVEAKALEVWGSQEALARERDQ 198
Cdd:cd21077  28 KEKHPEKYS---LLTKTECKEDYLLTDPELndeELLPHLEKPNPHKSTwSDMQLFLRCQVEAFALKKWGSPEALDEEFER 104

                .
gi 56693221 199 R 199
Cdd:cd21077 105 R 105
RapA_C pfam12137
RNA polymerase recycling family C-terminal; This domain is found in bacteria. This domain is ...
428-573 1.80e-04

RNA polymerase recycling family C-terminal; This domain is found in bacteria. This domain is about 360 amino acids in length. This domain is found associated with pfam00271, pfam00176. The function of this domain is not known, but structurally it forms an alpha-beta fold in nature with a central beta-sheet flanked by helices and loops, the beta-sheet being mainly antiparallel and flanked by four alpha helices, among which the two longer helices exhibit a coiled-coil arrangement.


Pssm-ID: 432354  Cd Length: 359  Bit Score: 44.07  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221   428 DSLGSLGVGTLL------GTVSAFLIYTnTEAllgrsiQAEHMQKLTEFLENDPaVRAIHDVKATDMGlskvrfkAEVDF 501
Cdd:pfam12137 189 SDTGNAAVALLKnkalpaGTLLLELIFV-VEC------VAPKALQLDRFLPPTP-IRLLLDKKGNDLS-------AKVPF 253
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 56693221   502 DGrvvTRSYLEKQDIEQILNEIQQVKtpEELENfMLKHGENII----------------DTLGAEVDRLEkELKQRNPEV 565
Cdd:pfam12137 254 ES---LNRQLSPVNRHTARKLVKAQR--DLIEK-LLAKAEQLAeeqaealieqakarmdQTLSAELERLE-ALQAVNPNI 326

                  ....*...
gi 56693221   566 RHVDLEIL 573
Cdd:pfam12137 327 RDDEIEAL 334
 
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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