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Conserved domains on  [gi|1017232786|gb|KZE97997|]
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Spore coat protein I [Geobacillus stearothermophilus]

Protein Classification

CotS family spore coat protein( domain architecture ID 10021577)

CotS family spore coat protein similar to Bacillus subtilis spore coat protein S (CotS) that may be required for the assembly of the CotSA protein in spores

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
42-356 3.23e-125

spore coat protein, CotS family; Members of this family include the spore coat proteins CotS and YtaA from Bacillus subtilis and, from other endospore-forming bacteria, homologs that are more closely related to these two than to the spore coat proteins YutH and YsxE. The CotS family is more broadly distributed than YutH or YsxE, but still is not universal among spore-formers. [Cellular processes, Sporulation and germination]


:

Pssm-ID: 131952 [Multi-domain]  Cd Length: 313  Bit Score: 362.75  E-value: 3.23e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786  42 MQIVTTKPDKGgaIWKLETKSGPKSLKLLHRRPTRSLFSLGAQEYLAEVRKaRVPPIVKTKSGNNYVEAGGKLWFVAEWI 121
Cdd:TIGR02906   1 IDVKSIKPLRN--VYKVETDSGNKCLKKINYPPERLLFILGAQEHLRKNGF-NIPKILKTKDGELYVKYNGDLYVLTEWI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786 122 EPLTPVTKDLEGAKQLCYALGEFHHLSKGYIPPQKAEMASRLHKWPKNYEKMITKMSWFRNIAHCYR-EMPASSPLLEVI 200
Cdd:TIGR02906  78 EGRECDFNNPIDLKKAAKGLALFHHASKGYVPPDGSKIRSKLGKWPKQFEKRLKELERFKKIALEKKyKDEFDKLYLKEV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786 201 DQFEEQARKGMERFRQSKYWELVGQGTTGWGLAHQDYGWSNGQTGADGMWIIDLDGVAFDLPIRDLRKLISGTMADLYRW 280
Cdd:TIGR02906 158 DYFLERGKKALELLNKSKYYDLCKEAKKIRGFCHQDYAYHNILLKDNEVYVIDFDYCTIDLPVRDLRKLIIKLMKKNGVW 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1017232786 281 DAKWVREMILAYHEANPITPELYEILMIDLAMPNEFYKNIKEMVYEPEIFLNEQTAQLVRTIVETDQSKWPVLAEI 356
Cdd:TIGR02906 238 DLEKAKEIIEAYSSINPLSKEEKEVLYIDLAFPHKFWKIGKQYYYKRKIWSEEKFLKKLEKIIEEEESKQEFLKEF 313
 
Name Accession Description Interval E-value
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
42-356 3.23e-125

spore coat protein, CotS family; Members of this family include the spore coat proteins CotS and YtaA from Bacillus subtilis and, from other endospore-forming bacteria, homologs that are more closely related to these two than to the spore coat proteins YutH and YsxE. The CotS family is more broadly distributed than YutH or YsxE, but still is not universal among spore-formers. [Cellular processes, Sporulation and germination]


Pssm-ID: 131952 [Multi-domain]  Cd Length: 313  Bit Score: 362.75  E-value: 3.23e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786  42 MQIVTTKPDKGgaIWKLETKSGPKSLKLLHRRPTRSLFSLGAQEYLAEVRKaRVPPIVKTKSGNNYVEAGGKLWFVAEWI 121
Cdd:TIGR02906   1 IDVKSIKPLRN--VYKVETDSGNKCLKKINYPPERLLFILGAQEHLRKNGF-NIPKILKTKDGELYVKYNGDLYVLTEWI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786 122 EPLTPVTKDLEGAKQLCYALGEFHHLSKGYIPPQKAEMASRLHKWPKNYEKMITKMSWFRNIAHCYR-EMPASSPLLEVI 200
Cdd:TIGR02906  78 EGRECDFNNPIDLKKAAKGLALFHHASKGYVPPDGSKIRSKLGKWPKQFEKRLKELERFKKIALEKKyKDEFDKLYLKEV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786 201 DQFEEQARKGMERFRQSKYWELVGQGTTGWGLAHQDYGWSNGQTGADGMWIIDLDGVAFDLPIRDLRKLISGTMADLYRW 280
Cdd:TIGR02906 158 DYFLERGKKALELLNKSKYYDLCKEAKKIRGFCHQDYAYHNILLKDNEVYVIDFDYCTIDLPVRDLRKLIIKLMKKNGVW 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1017232786 281 DAKWVREMILAYHEANPITPELYEILMIDLAMPNEFYKNIKEMVYEPEIFLNEQTAQLVRTIVETDQSKWPVLAEI 356
Cdd:TIGR02906 238 DLEKAKEIIEAYSSINPLSKEEKEVLYIDLAFPHKFWKIGKQYYYKRKIWSEEKFLKKLEKIIEEEESKQEFLKEF 313
CotI COG5881
Spore coat protein CotI/CotS, protein kinase superfamily [Cell cycle control, cell division, ...
24-360 1.18e-115

Spore coat protein CotI/CotS, protein kinase superfamily [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444583 [Multi-domain]  Cd Length: 331  Bit Score: 338.79  E-value: 1.18e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786  24 IIQLAEEVLKHYDLSVQNMqivttKPDKGgaIWKLETKSGPKSLKLLHRRPTRSLFSLGAQEYLAEVRKARVPPIVKTKS 103
Cdd:COG5881     1 MEELIEEILENYDLKIESI-----KPVRG--VYKIETDQGPKCLKKIKYSPERLLFIYEAQEHLKKNGFNNIPRIVPTKD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786 104 GNNYVEAGGKLWFVAEWIEPLTPVTKDLEGAKQLCYALGEFHHLSKGYIPPQKAEMASRLHKWPKNYEKMITKMSWFRNI 183
Cdd:COG5881    74 GKPYVKYGGKLYYLTEWIEGRECDYKNPEDLKKAAETLAEFHKASKGFEPPPGSKGRSHLGKWPERFEKRLEELEKFKKI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786 184 AHCYR-EMPASSPLLEVIDQFEEQARKGMERFRQSKYWELVGQGTTGWGLAHQDYGWSNGQ-TGADGMWIIDLDGVAFDL 261
Cdd:COG5881   154 AEKKKnKNEFDRLFLKNIDYFLEQAEKALELLEKSAYYKLVKEAKKEGGFCHHDYAYHNILiDEDGKIYIIDFDYCIYDL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786 262 PIRDLRKLISGTMaDLYRWDAKWVREMILAYHEANPITPELYEILMIDLAMPNEFYKNIKEMVYEPEIFLNEQTAQLVRT 341
Cdd:COG5881   234 PVHDLAKLLRRVM-KRGNWDIEKAKEILEAYNKINPLSKEEIEVLLAFLLFPQKFWRLVNKYYYEKKNWSEEKFIKKLQK 312
                         330
                  ....*....|....*....
gi 1017232786 342 IVETDQSKWPVLAEIEKDW 360
Cdd:COG5881   313 LIEEEEEKEEFLEEFEKIL 331
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
29-312 1.25e-09

Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270702 [Multi-domain]  Cd Length: 300  Bit Score: 58.81  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786  29 EEVLKHYDLSvqnmQIVTTKPDKGGAI---WKLETKSGPKSLKLLHRRPTR-SL-FSLGAQEYLAEVRKArVPPIVKTKS 103
Cdd:cd05153     5 AEFLAHYDLG----ELLSFEGIAAGIEntnYFVTTTDGRYVLTLFEKRRSAaELpFELELLDHLAQAGLP-VPRPLADKD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786 104 GNNYVEAGGKLWFVAEWI--EPLTPVTkdLEGAKQLCYALGEFHHLSKGYIPPQKAEMAsrLHKWPKNYEKMITKMswfR 181
Cdd:cd05153    80 GELLGELNGKPAALFPFLpgESLTTPT--PEQCRAIGAALARLHLALAGFPPPRPNPRG--LAWWKPLAERLKARL---D 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786 182 NIAHCYREMpasspLLEVIDQFEEQARKGMerfrqskywelvgqgttGWGLAHQDYG-----WSNGQTGAdgmwIIDLDG 256
Cdd:cd05153   153 LLAADDRAL-----LEDELARLQALAPSDL-----------------PRGVIHADLFrdnvlFDGDRLSG----IIDFYD 206
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1017232786 257 VAFDLPIRDLRKLISG-TMADLYRWDAKWVREMILAYHEANPITPElyEILMIDLAM 312
Cdd:cd05153   207 ACYDPLLYDLAIALNDwCFDDDGKLDPERAKALLAGYQSVRPLTEE--EKAALPLLL 261
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
46-297 1.51e-03

Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.


Pssm-ID: 426359 [Multi-domain]  Cd Length: 239  Bit Score: 39.79  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786  46 TTKPDKGGAI---WKLETKSGPKSLKLlHRRPTRSLFSLGAQEYLAEVRKARVPPIVKTKSGNNYVEAGGKLWFVAEWIE 122
Cdd:pfam01636   1 TLRPISSGASnrtYLVTTGDGRYVLRL-PPPGRAAEELRRELALLRHLAAAGVPPVPRVLAGCTDAELLGLPFLLMEYLP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786 123 PLTPVTKDL-EGAKQLCYALGEFH---HLskgyIPPQKAEMASRLHKWPKNYEkmitkmsWFRNIAHCYREmpasSPLLE 198
Cdd:pfam01636  80 GEVLARPLLpEERGALLEALGRALarlHA----VDPAALPLAGRLARLLELLR-------QLEAALARLLA----AELLD 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786 199 VIDQFEEQArkgMERFRQSKYWELVgqgttgWGLAHQDYGWSN----GQTGADGmwIIDLDGVAFDLPIRDLRKLISGTM 274
Cdd:pfam01636 145 RLEELEERL---LAALLALLPAELP------PVLVHGDLHPGNllvdPGGRVSG--VIDFEDAGLGDPAYDLAILLNSWG 213
                         250       260
                  ....*....|....*....|...
gi 1017232786 275 ADlyrWDAKWVREMILAYHEANP 297
Cdd:pfam01636 214 RE---LGAELLAAYLAAYGAFGY 233
 
Name Accession Description Interval E-value
spore_CotS TIGR02906
spore coat protein, CotS family; Members of this family include the spore coat proteins CotS ...
42-356 3.23e-125

spore coat protein, CotS family; Members of this family include the spore coat proteins CotS and YtaA from Bacillus subtilis and, from other endospore-forming bacteria, homologs that are more closely related to these two than to the spore coat proteins YutH and YsxE. The CotS family is more broadly distributed than YutH or YsxE, but still is not universal among spore-formers. [Cellular processes, Sporulation and germination]


Pssm-ID: 131952 [Multi-domain]  Cd Length: 313  Bit Score: 362.75  E-value: 3.23e-125
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786  42 MQIVTTKPDKGgaIWKLETKSGPKSLKLLHRRPTRSLFSLGAQEYLAEVRKaRVPPIVKTKSGNNYVEAGGKLWFVAEWI 121
Cdd:TIGR02906   1 IDVKSIKPLRN--VYKVETDSGNKCLKKINYPPERLLFILGAQEHLRKNGF-NIPKILKTKDGELYVKYNGDLYVLTEWI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786 122 EPLTPVTKDLEGAKQLCYALGEFHHLSKGYIPPQKAEMASRLHKWPKNYEKMITKMSWFRNIAHCYR-EMPASSPLLEVI 200
Cdd:TIGR02906  78 EGRECDFNNPIDLKKAAKGLALFHHASKGYVPPDGSKIRSKLGKWPKQFEKRLKELERFKKIALEKKyKDEFDKLYLKEV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786 201 DQFEEQARKGMERFRQSKYWELVGQGTTGWGLAHQDYGWSNGQTGADGMWIIDLDGVAFDLPIRDLRKLISGTMADLYRW 280
Cdd:TIGR02906 158 DYFLERGKKALELLNKSKYYDLCKEAKKIRGFCHQDYAYHNILLKDNEVYVIDFDYCTIDLPVRDLRKLIIKLMKKNGVW 237
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1017232786 281 DAKWVREMILAYHEANPITPELYEILMIDLAMPNEFYKNIKEMVYEPEIFLNEQTAQLVRTIVETDQSKWPVLAEI 356
Cdd:TIGR02906 238 DLEKAKEIIEAYSSINPLSKEEKEVLYIDLAFPHKFWKIGKQYYYKRKIWSEEKFLKKLEKIIEEEESKQEFLKEF 313
CotI COG5881
Spore coat protein CotI/CotS, protein kinase superfamily [Cell cycle control, cell division, ...
24-360 1.18e-115

Spore coat protein CotI/CotS, protein kinase superfamily [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444583 [Multi-domain]  Cd Length: 331  Bit Score: 338.79  E-value: 1.18e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786  24 IIQLAEEVLKHYDLSVQNMqivttKPDKGgaIWKLETKSGPKSLKLLHRRPTRSLFSLGAQEYLAEVRKARVPPIVKTKS 103
Cdd:COG5881     1 MEELIEEILENYDLKIESI-----KPVRG--VYKIETDQGPKCLKKIKYSPERLLFIYEAQEHLKKNGFNNIPRIVPTKD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786 104 GNNYVEAGGKLWFVAEWIEPLTPVTKDLEGAKQLCYALGEFHHLSKGYIPPQKAEMASRLHKWPKNYEKMITKMSWFRNI 183
Cdd:COG5881    74 GKPYVKYGGKLYYLTEWIEGRECDYKNPEDLKKAAETLAEFHKASKGFEPPPGSKGRSHLGKWPERFEKRLEELEKFKKI 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786 184 AHCYR-EMPASSPLLEVIDQFEEQARKGMERFRQSKYWELVGQGTTGWGLAHQDYGWSNGQ-TGADGMWIIDLDGVAFDL 261
Cdd:COG5881   154 AEKKKnKNEFDRLFLKNIDYFLEQAEKALELLEKSAYYKLVKEAKKEGGFCHHDYAYHNILiDEDGKIYIIDFDYCIYDL 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786 262 PIRDLRKLISGTMaDLYRWDAKWVREMILAYHEANPITPELYEILMIDLAMPNEFYKNIKEMVYEPEIFLNEQTAQLVRT 341
Cdd:COG5881   234 PVHDLAKLLRRVM-KRGNWDIEKAKEILEAYNKINPLSKEEIEVLLAFLLFPQKFWRLVNKYYYEKKNWSEEKFIKKLQK 312
                         330
                  ....*....|....*....
gi 1017232786 342 IVETDQSKWPVLAEIEKDW 360
Cdd:COG5881   313 LIEEEEEKEEFLEEFEKIL 331
SrkA COG2334
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ...
26-312 6.82e-12

Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal transduction mechanisms]; Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist is part of the Pathway/BioSystem: Threonine biosynthesis


Pssm-ID: 441905 [Multi-domain]  Cd Length: 297  Bit Score: 65.33  E-value: 6.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786  26 QLAEEVLKHYDLSVqnmqIVTTKPDKGG--AIWKLETKSGPKS-LKLlHRRPTRS----LFSLGAQEYLAEvRKARVPPI 98
Cdd:COG2334     1 DELAAALERYGLGP----LSSLKPLNSGenRNYRVETEDGRRYvLKL-YRPGRWSpeeiPFELALLAHLAA-AGLPVPAP 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786  99 VKTKSGNNYVEAGGKLWFVAEWIEPLTPVTKDLEGAKQLCYALGEFHHLSKGYIPPqkaemASRLHKWpknyekmitkms 178
Cdd:COG2334    75 VPTRDGETLLELEGRPAALFPFLPGRSPEEPSPEQLEELGRLLARLHRALADFPRP-----NARDLAW------------ 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786 179 WFRNIAHCYREMPASSPLLEVIDQFEEQArkgmERFRQSKYWELVgqgttgWGLAHQDY--G---WSNGQTGAdgmwIID 253
Cdd:COG2334   138 WDELLERLLGPLLPDPEDRALLEELLDRL----EARLAPLLGALP------RGVIHGDLhpDnvlFDGDGVSG----LID 203
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1017232786 254 LDGVAFDLPIRDLRKLISGTMADlyRWDAKWVREMILAYHEANPITPElyEILMIDLAM 312
Cdd:COG2334   204 FDDAGYGPRLYDLAIALNGWADG--PLDPARLAALLEGYRAVRPLTEA--ELAALPPLL 258
HomoserineK_II cd05153
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ...
29-312 1.25e-09

Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270702 [Multi-domain]  Cd Length: 300  Bit Score: 58.81  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786  29 EEVLKHYDLSvqnmQIVTTKPDKGGAI---WKLETKSGPKSLKLLHRRPTR-SL-FSLGAQEYLAEVRKArVPPIVKTKS 103
Cdd:cd05153     5 AEFLAHYDLG----ELLSFEGIAAGIEntnYFVTTTDGRYVLTLFEKRRSAaELpFELELLDHLAQAGLP-VPRPLADKD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786 104 GNNYVEAGGKLWFVAEWI--EPLTPVTkdLEGAKQLCYALGEFHHLSKGYIPPQKAEMAsrLHKWPKNYEKMITKMswfR 181
Cdd:cd05153    80 GELLGELNGKPAALFPFLpgESLTTPT--PEQCRAIGAALARLHLALAGFPPPRPNPRG--LAWWKPLAERLKARL---D 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786 182 NIAHCYREMpasspLLEVIDQFEEQARKGMerfrqskywelvgqgttGWGLAHQDYG-----WSNGQTGAdgmwIIDLDG 256
Cdd:cd05153   153 LLAADDRAL-----LEDELARLQALAPSDL-----------------PRGVIHADLFrdnvlFDGDRLSG----IIDFYD 206
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1017232786 257 VAFDLPIRDLRKLISG-TMADLYRWDAKWVREMILAYHEANPITPElyEILMIDLAM 312
Cdd:cd05153   207 ACYDPLLYDLAIALNDwCFDDDGKLDPERAKALLAGYQSVRPLTEE--EKAALPLLL 261
APH pfam01636
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ...
46-297 1.51e-03

Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.


Pssm-ID: 426359 [Multi-domain]  Cd Length: 239  Bit Score: 39.79  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786  46 TTKPDKGGAI---WKLETKSGPKSLKLlHRRPTRSLFSLGAQEYLAEVRKARVPPIVKTKSGNNYVEAGGKLWFVAEWIE 122
Cdd:pfam01636   1 TLRPISSGASnrtYLVTTGDGRYVLRL-PPPGRAAEELRRELALLRHLAAAGVPPVPRVLAGCTDAELLGLPFLLMEYLP 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786 123 PLTPVTKDL-EGAKQLCYALGEFH---HLskgyIPPQKAEMASRLHKWPKNYEkmitkmsWFRNIAHCYREmpasSPLLE 198
Cdd:pfam01636  80 GEVLARPLLpEERGALLEALGRALarlHA----VDPAALPLAGRLARLLELLR-------QLEAALARLLA----AELLD 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1017232786 199 VIDQFEEQArkgMERFRQSKYWELVgqgttgWGLAHQDYGWSN----GQTGADGmwIIDLDGVAFDLPIRDLRKLISGTM 274
Cdd:pfam01636 145 RLEELEERL---LAALLALLPAELP------PVLVHGDLHPGNllvdPGGRVSG--VIDFEDAGLGDPAYDLAILLNSWG 213
                         250       260
                  ....*....|....*....|...
gi 1017232786 275 ADlyrWDAKWVREMILAYHEANP 297
Cdd:pfam01636 214 RE---LGAELLAAYLAAYGAFGY 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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