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Conserved domains on  [gi|2581072013|ref|WP_311045446|]
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ABC transporter substrate-binding protein, partial [Staphylococcus hominis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CeuA super family cl30255
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ...
 1-143 2.51e-56

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


The actual alignment was detected with superfamily member COG4607:

Pssm-ID: 443657 [Multi-domain]  Cd Length: 310  Bit Score: 178.07  E-value: 2.51e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2581072013   1 TKLDQKISDMKKQTKDlDKSVMYLLVNEGELSTFGPGGRFGdLVFNTLGFKPADKHVKISPHGQNINNEYISNHNPDIIL 80
Cdd:COG4607   169 ADLDAKIAALKAAAAG-KGTALIVLTNGGKISAYGPGSRFG-PIHDVLGFKPADEDIEASTHGQAISFEFIAEANPDWLF 246

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2581072013  81 AMDRGSVVGGK-STAKQVLKNDVIKDVTAVKNNNVYELDPKLWYFASGSTTTTVKQIDELEKVI 143
Cdd:COG4607   247 VIDRDAAIGGEgPAAKQVLDNELVKQTTAWKNGQIVYLDPDAWYLAGGGIQSLTEMLDEVADAL 310
 
Name Accession Description Interval E-value
CeuA COG4607
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ...
 1-143 2.51e-56

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


Pssm-ID: 443657 [Multi-domain]  Cd Length: 310  Bit Score: 178.07  E-value: 2.51e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2581072013   1 TKLDQKISDMKKQTKDlDKSVMYLLVNEGELSTFGPGGRFGdLVFNTLGFKPADKHVKISPHGQNINNEYISNHNPDIIL 80
Cdd:COG4607   169 ADLDAKIAALKAAAAG-KGTALIVLTNGGKISAYGPGSRFG-PIHDVLGFKPADEDIEASTHGQAISFEFIAEANPDWLF 246

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2581072013  81 AMDRGSVVGGK-STAKQVLKNDVIKDVTAVKNNNVYELDPKLWYFASGSTTTTVKQIDELEKVI 143
Cdd:COG4607   247 VIDRDAAIGGEgPAAKQVLDNELVKQTTAWKNGQIVYLDPDAWYLAGGGIQSLTEMLDEVADAL 310
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 1-141 7.67e-47

Siderophore binding protein FatB. These proteins have been shown to function as ABC-type initial receptors in the siderophore-mediated iron uptake 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 their ligands in the cleft between these domains.


Pssm-ID: 238560 [Multi-domain]  Cd Length: 270  Bit Score: 152.80  E-value: 7.67e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2581072013   1 TKLDQKISDMKKQTKDlDKSVMYLLVNEGELSTFGPGGRFGDLvFNTLGFKPADKHVKISPHGQNINNEYISNHNPDIIL 80
Cdd:cd01140   131 AEIDASIAEAKSAAKG-KKKALVVLVNGGKLSAFGPGSRFGWL-HDLLGFEPADENIKASSHGQPVSFEYILEANPDWLF 208

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2581072013  81 AMDRGSVVG-GKSTAKQVLKNDVIKDVTAVKNNNVYELDPKLWYFASGSTTTTVKQIDELEK 141
Cdd:cd01140   209 VIDRGAAIGaEGSSAKEVLDNDLVKNTTAWKNGKVIYLDPDLWYLSGGGLESLKQMIDDLKK 270
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 1-119 7.86e-16

Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding proteins, several of which are involved in iron and cobalamin transport. Among its ligands are siderophores bacillibactin, enterobactin and iron(III)-hydroxamates (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 426291 [Multi-domain]  Cd Length: 233  Bit Score: 71.25  E-value: 7.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2581072013   1 TKLDQKISDMKK--QTKDLDKSVMYLLVNEGELSTFGPGGRFGDLvFNTLGFKPADK-HVKISphGQNINNEYISNHNPD 77
Cdd:pfam01497 116 AEIDSALAAAKKavPSLTRKPVLVFGGADGGGYVVAGSNTYIGDL-LRILGIENIAAeLSGSE--YAPISFEAILSSNPD 192

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2581072013  78 IILAMDRGSVVggKSTAKQVLKNDVIKDVTAVKNNNVYELDP 119
Cdd:pfam01497 193 VIIVSGRDSFT--KTGPEFVAANPLWAGLPAVKNGRVYTLPS 232
 
Name Accession Description Interval E-value
CeuA COG4607
ABC-type enterochelin transport system, periplasmic component [Inorganic ion transport and ...
 1-143 2.51e-56

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


Pssm-ID: 443657 [Multi-domain]  Cd Length: 310  Bit Score: 178.07  E-value: 2.51e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2581072013   1 TKLDQKISDMKKQTKDlDKSVMYLLVNEGELSTFGPGGRFGdLVFNTLGFKPADKHVKISPHGQNINNEYISNHNPDIIL 80
Cdd:COG4607   169 ADLDAKIAALKAAAAG-KGTALIVLTNGGKISAYGPGSRFG-PIHDVLGFKPADEDIEASTHGQAISFEFIAEANPDWLF 246

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2581072013  81 AMDRGSVVGGK-STAKQVLKNDVIKDVTAVKNNNVYELDPKLWYFASGSTTTTVKQIDELEKVI 143
Cdd:COG4607   247 VIDRDAAIGGEgPAAKQVLDNELVKQTTAWKNGQIVYLDPDAWYLAGGGIQSLTEMLDEVADAL 310
FatB cd01140
Siderophore binding protein FatB. These proteins have been shown to function as ABC-type ...
 1-141 7.67e-47

Siderophore binding protein FatB. These proteins have been shown to function as ABC-type initial receptors in the siderophore-mediated iron uptake 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 their ligands in the cleft between these domains.


Pssm-ID: 238560 [Multi-domain]  Cd Length: 270  Bit Score: 152.80  E-value: 7.67e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2581072013   1 TKLDQKISDMKKQTKDlDKSVMYLLVNEGELSTFGPGGRFGDLvFNTLGFKPADKHVKISPHGQNINNEYISNHNPDIIL 80
Cdd:cd01140   131 AEIDASIAEAKSAAKG-KKKALVVLVNGGKLSAFGPGSRFGWL-HDLLGFEPADENIKASSHGQPVSFEYILEANPDWLF 208

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2581072013  81 AMDRGSVVG-GKSTAKQVLKNDVIKDVTAVKNNNVYELDPKLWYFASGSTTTTVKQIDELEK 141
Cdd:cd01140   209 VIDRGAAIGaEGSSAKEVLDNDLVKNTTAWKNGKVIYLDPDLWYLSGGGLESLKQMIDDLKK 270
FepB COG0614
ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and ...
 3-143 7.70e-17

ABC-type Fe3+-hydroxamate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 440379 [Multi-domain]  Cd Length: 264  Bit Score: 74.65  E-value: 7.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2581072013   3 LDQKISDMKKQTKDLDK--SVMYLLVNEGELSTFGPGGrFGDLVFNTLGFKPADKHVKisPHGQNINNEYISNHNPDIIL 80
Cdd:COG0614   121 YEARLAAVRARLAGAEErpTVLYEIWSGDPLYTAGGGS-FIGELLELAGGRNVAADLG--GGYPEVSLEQVLALDPDVII 197

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2581072013  81 AMDRGSVVGG-KSTAKQVLKNDVIKDVTAVKNNNVYELDPKLWYFASgstTTTVKQIDELEKVI 143
Cdd:COG0614   198 LSGGGYDAETaEEALEALLADPGWQSLPAVKNGRVYVVPGDLLSRPG---PRLLLALEDLAKAL 258
Peripla_BP_2 pfam01497
Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding ...
 1-119 7.86e-16

Periplasmic binding protein; This is sensor domain found in bacterial periplasmic binding proteins, several of which are involved in iron and cobalamin transport. Among its ligands are siderophores bacillibactin, enterobactin and iron(III)-hydroxamates (Matilla et. al., FEMS Microbiology Reviews, fuab043, 45, 2021, 1 https://doi.org/10.1093/femsre/fuab043).


Pssm-ID: 426291 [Multi-domain]  Cd Length: 233  Bit Score: 71.25  E-value: 7.86e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2581072013   1 TKLDQKISDMKK--QTKDLDKSVMYLLVNEGELSTFGPGGRFGDLvFNTLGFKPADK-HVKISphGQNINNEYISNHNPD 77
Cdd:pfam01497 116 AEIDSALAAAKKavPSLTRKPVLVFGGADGGGYVVAGSNTYIGDL-LRILGIENIAAeLSGSE--YAPISFEAILSSNPD 192

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2581072013  78 IILAMDRGSVVggKSTAKQVLKNDVIKDVTAVKNNNVYELDP 119
Cdd:pfam01497 193 VIIVSGRDSFT--KTGPEFVAANPLWAGLPAVKNGRVYTLPS 232
FecB COG4594
ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and ...
 2-139 4.79e-14

ABC-type Fe3+-citrate transport system, periplasmic component [Inorganic ion transport and metabolism];


Pssm-ID: 443650 [Multi-domain]  Cd Length: 316  Bit Score: 67.25  E-value: 4.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2581072013   2 KLDQKISDMKKQ--TKDLDKSVMYLLVNEGELSTFGPGGRFGDlVFNTLGFKPADKHVKISPHGQN-INNEYISNHNPDI 78
Cdd:COG4594   174 DHDQRIAEAKAKlaAADKGKKVAVGQFRADGLRLYTPNSFAGS-VLAALGFENPPKQSKDNGYGYSeVSLEQLPALDPDV 252

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2581072013  79 ILAMdrgsVVGGKSTAKQVLKNDVIKDVTAVKNNNVYELDPKLWYFASG--STTTTVKQIDEL 139
Cdd:COG4594   253 LFIA----TYDDPSILKEWKNNPLWKNLKAVKNGRVYEVDGDLWTRGRGplAAELMADDLVEI 311
FhuD cd01146
Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial ...
 1-127 1.03e-09

Fe3+-siderophore binding domain FhuD. These proteins have been shown to function as initial receptors in ABC transport of Fe3+-siderophores in many eubacterial species. They belong to the TroA-like superfamily of helical backbone metal receptor proteins that share a distinct fold and ligand binding mechanism. A typical TroA-like protein is comprised of two globular subdomains connected by a long alpha helix and binds its specific ligands in the cleft between these domains.


Pssm-ID: 238566 [Multi-domain]  Cd Length: 256  Bit Score: 54.98  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2581072013   1 TKLDQKISDMKKQTKDLDKSVMYLLV--NEGELSTFGPGGRFGDLVfNTLGFKPADKHVKISPHG-QNINNEYISNHNPD 77
Cdd:cd01146   123 AEYDQRLAELRQKLPDKGPKPVSVVRfsDAGSIRLYGPNSFAGSVL-EDLGLQNPWAQETTNDSGfATISLERLAKADAD 201

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2581072013  78 IILAMdrgsVVGGKSTAKQVLKNDVIKDVTAVKNNNVYELDPKLWYFASG 127
Cdd:cd01146   202 VLFVF----TYEDEELAQALQANPLWQNLPAVKNGRVYVVDDVWWFFGGG 247
FeuA cd01138
Periplasmic binding protein FeuA. These proteins have predicted to function as initial ...
 4-127 1.19e-09

Periplasmic binding protein FeuA. These proteins have predicted to function as initial receptors in ABC transport of metal ions 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 their ligands in the cleft between these domains.


Pssm-ID: 238558 [Multi-domain]  Cd Length: 248  Bit Score: 54.65  E-value: 1.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2581072013   4 DQKISDMKKQTKDLDKSVMYLLVNE--GELSTFGPGGRFGDLVFN-TLGFKPADKHVKIS--PHGQNINNEYISNHNPD- 77
Cdd:cd01138   124 KQKAKEAKEKIKKKLGNDKSVAVLRgrKQIYVFGEDGRGGGPILYaDLGLKAPEKVKEIEdkPGYAAISLEVLPEFDADy 203

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2581072013  78 IILAMDRGSvvggkSTAKQVLKNDVIKDVTAVKNNNVYELDPKLWYFASG 127
Cdd:cd01138   204 IFLLFFTGP-----EAKADFESLPIWKNLPAVKNNHVYIVDAWVFYFADG 248
TroA_a cd01148
Metal binding protein TroA_a. These proteins are predicted to function as initial receptors ...
 1-136 4.44e-07

Metal binding protein TroA_a. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria. 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.


Pssm-ID: 238568 [Multi-domain]  Cd Length: 284  Bit Score: 47.72  E-value: 4.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2581072013   1 TKLDQKISDMKKQTKDLDKSVMYLLVNEGELS--TFGPGGRFGDLVfNTLGFKPADKHVKISphGQNINNEYISNHNPDI 78
Cdd:cd01148   150 ADLKARLAEISAKVKGDGKKVAVFVYDSGEDKpfTSGRGGIPNAII-TAAGGRNVFADVDES--WTTVSWETVIARNPDV 226

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2581072013  79 ILAMDRGSVVGGKSTAKQVLKNDVIKDVTAVKNNNVYELDPKLWYfASGSTTTTVKQI 136
Cdd:cd01148   227 IVIIDYGDQNAAEQKIKFLKENPALKNVPAVKNNRFIVLPLAEAT-PGIRNVDAIEKL 283
TroA_e cd01142
Periplasmic binding protein TroA_e. These proteins are predicted to function as initial ...
 1-123 1.81e-06

Periplasmic binding protein TroA_e. 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: 238562 [Multi-domain]  Cd Length: 289  Bit Score: 45.81  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2581072013   1 TKLDQKISDMKKQTKDLD----KSVMYllVNEGELSTFGPGgRFGDLVFNTLGFKPADKHVKISPHGQnINNEYISNHNP 76
Cdd:cd01142   145 AYFDDNLAYVAARTKKLPdserPRVYY--AGPDPLTTDGTG-SITNSWIDLAGGINVASEATKKGSGE-VSLEQLLKWNP 220

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2581072013  77 DIILAMDRGsvvggksTAKQVLKNDVIKDVTAVKNNNVYeLDPKLWY 123
Cdd:cd01142   221 DVIIVGNAD-------TKAAILADPRWQNLRAVKNGRVY-VNPEGAF 259
HemV-2 cd01147
Metal binding protein HemV-2. These proteins are predicted to function as initial receptors ...
 3-124 1.30e-04

Metal binding protein HemV-2. 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: 238567 [Multi-domain]  Cd Length: 262  Bit Score: 40.40  E-value: 1.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2581072013   3 LDQKISDMKKQTKDL---DKSVMYLlvneGELSTFGPGGRFGDL--------------VFNTLGfkpADKHVKISPhgqn 65
Cdd:cd01147   137 IESILADVEERTKDIpdeEKPTVYF----GRIGTKGAAGLESGLagsievfelagginVADGLG---GGGLKEVSP---- 205

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2581072013  66 innEYISNHNPDIILAMDRGsvvGGKSTAKQVLKNDVIKDVTAVKNNNVYEL--DPKLWYF 124
Cdd:cd01147   206 ---EQILLWNPDVIFLDTGS---FYLSLEGYAKNRPFWQSLKAVKNGRVYLLpaLPFNWYD 260
TroA_f cd01139
Periplasmic binding protein TroA_f. These proteins are predicted to function as initial ...
 32-117 2.53e-04

Periplasmic binding protein TroA_f. 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: 238559 [Multi-domain]  Cd Length: 342  Bit Score: 39.60  E-value: 2.53e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2581072013  32 STFGPGGrFGDLVFNTLGFKPADKHVKISPhgQNINNEYISNHNPDIILA--MDRGSVVGG-------------KSTAKQ 96
Cdd:cd01139   193 STYGNGN-WGELVDAAGGDNIADGLIPGTS--GELNAEYVIAANPEIIIAtgGNWAKDPSGvslgpdgttadakESLLRA 269

                          90       100
                  ....*....|....*....|.
gi 2581072013  97 VLKNDVIKDVTAVKNNNVYEL 117
Cdd:cd01139   270 LLKRPGWSSLQAVKNGRVYAL 290
YvrC cd01143
Periplasmic binding protein YvrC. These proteins are predicted to function as initial ...
 1-80 7.90e-04

Periplasmic binding protein YvrC. These proteins are predicted to function as initial receptors in ABC transport of metal ions in eubacteria and archaea. 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.


Pssm-ID: 238563 [Multi-domain]  Cd Length: 195  Bit Score: 38.03  E-value: 7.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2581072013   1 TKLDQKISDMKKQTKDLDKSVMYLLVNEGELSTFGPGGRFGDLvFNTLGFKpadkhvKISPHGQN---INNEYISNHNPD 77
Cdd:cd01143   119 KEMKQKIDKVKDKGKTIKKSKVYIEVSLGGPYTAGKNTFINEL-IRLAGAK------NIAADSGGwpqVSPEEILKANPD 191


                  ...
gi 2581072013  78 IIL 80
Cdd:cd01143   192 VII 194
BtuF cd01144
Cobalamin binding protein BtuF. These proteins have been shown to function as initial ...
 69-127 3.85e-03

Cobalamin binding protein BtuF. These proteins have been shown to function as initial receptors in ABC transport of vitamin B12 (cobalamin) in eubacterial and some archaeal species. 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: 238564 [Multi-domain]  Cd Length: 245  Bit Score: 36.12  E-value: 3.85e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2581072013  69 EYISNHNPDIILAMDrgsvvGGKSTAKQVLKNDVIKD-VTAVKNNNVYELDPKlWYFASG 127
Cdd:cd01144   180 EDVLAANPDVIVLSP-----CGFGFTPAILRKEPAWQaLPAVRNGRVYAVDGN-WYFRPS 233
 
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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