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Conserved domains on  [gi|568947626|ref|XP_006540832|]
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outer dynein arm-docking complex subunit 1 isoform X3 [Mus musculus]

Protein Classification

coiled-coil domain-containing protein( domain architecture ID 1000095)

coiled-coil domain-containing protein contains a region with alpha-helical coiled-coil sequence signatures that is being annotated by a variety of protein family models, not necessarily indicating family membership

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
30-317 2.51e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.84  E-value: 2.51e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626    30 ELSRLQRQCKMMELERRAYSKEVhQRLRKQVEEIRQ-LEMLRAKLQ---TQINVAQSQVKRLGdkkhlAEMECLLKSRAQ 105
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKAL-AELRKELEELEEeLEQLRKELEelsRQISALRKDLARLE-----AEVEQLEERIAQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626   106 VQVEIEALQEQNRALDKQIQDWETHVLTQSKEasapdlimyqKMKIQRRIRILEDQLDRVTCHFDihlvrnaALREELEL 185
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAE----------IEELEAQIEQLKEELKALREALD-------ELRAELTL 814
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626   186 LRIERGRYLNMDRKLKKEIHLLREMVGALstsstsaytarEEAKTKMGMLQERAEKELAQSDTEAQILLRQISHL----E 261
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDL-----------EEQIEELSEDIESLAAEIEELEELIEELESELEALlnerA 883
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568947626   262 QLHRFLKLKNDERQPDPRVVQKAEQRDWEVSEGLR--KTSQEKLVLRYEDTLGKLAQL 317
Cdd:TIGR02168  884 SLEEALALLRSELEELSEELRELESKRSELRRELEelREKLAQLELRLEGLEVRIDNL 941
CCDC158 super family cl37899
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
472-564 9.64e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


The actual alignment was detected with superfamily member pfam15921:

Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.80  E-value: 9.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626   472 INEQNSEIHHLQEEIKEMQEALVSehASQDKQRMQQEQQckMLQQDVDKMCSESEQLEGRFQVLRGQLEKIK---TDIQV 548
Cdd:pfam15921  736 ITAKRGQIDALQSKIQFLEEAMTN--ANKEKHFLKEEKN--KLSQELSTVATEKNKMAGELEVLRSQERRLKekvANMEV 811
                           90
                   ....*....|....*.
gi 568947626   549 LFDKAKCDSSVIKDLL 564
Cdd:pfam15921  812 ALDKASLQFAECQDII 827
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
30-317 2.51e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.84  E-value: 2.51e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626    30 ELSRLQRQCKMMELERRAYSKEVhQRLRKQVEEIRQ-LEMLRAKLQ---TQINVAQSQVKRLGdkkhlAEMECLLKSRAQ 105
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKAL-AELRKELEELEEeLEQLRKELEelsRQISALRKDLARLE-----AEVEQLEERIAQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626   106 VQVEIEALQEQNRALDKQIQDWETHVLTQSKEasapdlimyqKMKIQRRIRILEDQLDRVTCHFDihlvrnaALREELEL 185
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAE----------IEELEAQIEQLKEELKALREALD-------ELRAELTL 814
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626   186 LRIERGRYLNMDRKLKKEIHLLREMVGALstsstsaytarEEAKTKMGMLQERAEKELAQSDTEAQILLRQISHL----E 261
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDL-----------EEQIEELSEDIESLAAEIEELEELIEELESELEALlnerA 883
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568947626   262 QLHRFLKLKNDERQPDPRVVQKAEQRDWEVSEGLR--KTSQEKLVLRYEDTLGKLAQL 317
Cdd:TIGR02168  884 SLEEALALLRSELEELSEELRELESKRSELRRELEelREKLAQLELRLEGLEVRIDNL 941
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
50-262 1.68e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.92  E-value: 1.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626  50 KEVHQRLRKQVEEIRQLEMLRAKLQTQINVAQSQVKRLGDKkhLAEMECLLKsraQVQVEIEALQEQNRALDKQIQDWET 129
Cdd:COG4942   23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR--IAALARRIR---ALEQELAALEAELAELEKEIAELRA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626 130 HvLTQSKEASAPDLIMYQKMKIQRRIRIL---EDQLDrvtchfdihLVRNAALREELELLRIERGRYLnmdRKLKKEIHL 206
Cdd:COG4942   98 E-LEAQKEELAELLRALYRLGRQPPLALLlspEDFLD---------AVRRLQYLKYLAPARREQAEEL---RADLAELAA 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568947626 207 LREMVGALSTSSTSAYTAREEAKTKMGMLQERAEKELAQSDTEAQILLRQISHLEQ 262
Cdd:COG4942  165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
472-564 9.64e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.80  E-value: 9.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626   472 INEQNSEIHHLQEEIKEMQEALVSehASQDKQRMQQEQQckMLQQDVDKMCSESEQLEGRFQVLRGQLEKIK---TDIQV 548
Cdd:pfam15921  736 ITAKRGQIDALQSKIQFLEEAMTN--ANKEKHFLKEEKN--KLSQELSTVATEKNKMAGELEVLRSQERRLKekvANMEV 811
                           90
                   ....*....|....*.
gi 568947626   549 LFDKAKCDSSVIKDLL 564
Cdd:pfam15921  812 ALDKASLQFAECQDII 827
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
23-320 7.96e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 7.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626  23 LEGSVDGELSRLQR----QCKMMELERRAYSKEvhQRLRKQVEEIRQLEMLRAKLQTQINVAQSQVKRLGDKKHLAE--- 95
Cdd:PRK03918 219 LREELEKLEKEVKEleelKEEIEELEKELESLE--GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEeyi 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626  96 -----MECLLKSRAQVQVEIEALQEQNRALDKQIQDWEthvltqSKEASAPDLiMYQKMKIQRRIRILEDQLDRvtchfd 170
Cdd:PRK03918 297 klsefYEEYLDELREIEKRLSRLEEEINGIEERIKELE------EKEERLEEL-KKKLKELEKRLEELEERHEL------ 363
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626 171 ihLVRNAALREELELLRIERGRY--------LNMDRKLKKEIHL----LREMVGALSTSSTSAYTAREEAKTKMGM---- 234
Cdd:PRK03918 364 --YEEAKAKKEELERLKKRLTGLtpeklekeLEELEKAKEEIEEeiskITARIGELKKEIKELKKAIEELKKAKGKcpvc 441
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626 235 ---LQERAEKELAQSDTE-----AQILLRQISHLEQLHRFLKLKNDERQPDPRVV---QKAEQRDwEVSEGLRKTSQEKL 303
Cdd:PRK03918 442 greLTEEHRKELLEEYTAelkriEKELKEIEEKERKLRKELRELEKVLKKESELIklkELAEQLK-ELEEKLKKYNLEEL 520
                        330       340
                 ....*....|....*....|
gi 568947626 304 ---VLRYEDTLGKLAQLTGE 320
Cdd:PRK03918 521 ekkAEEYEKLKEKLIKLKGE 540
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
30-317 2.51e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.84  E-value: 2.51e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626    30 ELSRLQRQCKMMELERRAYSKEVhQRLRKQVEEIRQ-LEMLRAKLQ---TQINVAQSQVKRLGdkkhlAEMECLLKSRAQ 105
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKAL-AELRKELEELEEeLEQLRKELEelsRQISALRKDLARLE-----AEVEQLEERIAQ 751
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626   106 VQVEIEALQEQNRALDKQIQDWETHVLTQSKEasapdlimyqKMKIQRRIRILEDQLDRVTCHFDihlvrnaALREELEL 185
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAEEELAEAEAE----------IEELEAQIEQLKEELKALREALD-------ELRAELTL 814
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626   186 LRIERGRYLNMDRKLKKEIHLLREMVGALstsstsaytarEEAKTKMGMLQERAEKELAQSDTEAQILLRQISHL----E 261
Cdd:TIGR02168  815 LNEEAANLRERLESLERRIAATERRLEDL-----------EEQIEELSEDIESLAAEIEELEELIEELESELEALlnerA 883
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 568947626   262 QLHRFLKLKNDERQPDPRVVQKAEQRDWEVSEGLR--KTSQEKLVLRYEDTLGKLAQL 317
Cdd:TIGR02168  884 SLEEALALLRSELEELSEELRELESKRSELRRELEelREKLAQLELRLEGLEVRIDNL 941
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
27-317 2.04e-08

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 57.77  E-value: 2.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626    27 VDGELSRLQRQCKMMELERRAYSKEVHQRLR------KQVEEIRQLEMLRakLQTQINVAQSQVKRLGDKKHLA--EMEC 98
Cdd:TIGR02169  242 IERQLASLEEELEKLTEEISELEKRLEEIEQlleelnKKIKDLGEEEQLR--VKEKIGELEAEIASLERSIAEKerELED 319
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626    99 LLKSRAQVQVEIEALQEQNRALDKQIQDWETHVltqskeasapDLIMYQKMKIQRRIRILEDQLDRVTCHFDIHLVRNAA 178
Cdd:TIGR02169  320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRR----------DKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626   179 LREELELLRIERGRYLNMDRKLKKEIHLLREMVGALSTSSTSAytarEEAKTKMGMLQERAEKELAQSDTEAQILLRQIS 258
Cdd:TIGR02169  390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGI----EAKINELEEEKEDKALEIKKQEWKLEQLAADLS 465
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568947626   259 HLEQLHRFLKLKNDERQPDPRVVQK------AEQRDWEVSEGLRKTSQEKLVLRYEDTLGKLAQL 317
Cdd:TIGR02169  466 KYEQELYDLKEEYDRVEKELSKLQRelaeaeAQARASEERVRGGRAVEEVLKASIQGVHGTVAQL 530
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
50-262 1.68e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.92  E-value: 1.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626  50 KEVHQRLRKQVEEIRQLEMLRAKLQTQINVAQSQVKRLGDKkhLAEMECLLKsraQVQVEIEALQEQNRALDKQIQDWET 129
Cdd:COG4942   23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERR--IAALARRIR---ALEQELAALEAELAELEKEIAELRA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626 130 HvLTQSKEASAPDLIMYQKMKIQRRIRIL---EDQLDrvtchfdihLVRNAALREELELLRIERGRYLnmdRKLKKEIHL 206
Cdd:COG4942   98 E-LEAQKEELAELLRALYRLGRQPPLALLlspEDFLD---------AVRRLQYLKYLAPARREQAEEL---RADLAELAA 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568947626 207 LREMVGALSTSSTSAYTAREEAKTKMGMLQERAEKELAQSDTEAQILLRQISHLEQ 262
Cdd:COG4942  165 LRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
43-316 3.57e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 50.45  E-value: 3.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626    43 LERRAYSKEVHQRLRKQVEEIRQLEMLRAK--LQTQINVAQSQVKRLgdKKHLAEMECLLKSRAQVQVEIEA-LQEQNRA 119
Cdd:TIGR02169  203 LRREREKAERYQALLKEKREYEGYELLKEKeaLERQKEAIERQLASL--EEELEKLTEEISELEKRLEEIEQlLEELNKK 280
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626   120 LDK-----QIQDWETHVLTQSKEASAPDLIMYQKM---KIQRRIRILEDQLDRVtchfdihLVRNAALREELELLRIERG 191
Cdd:TIGR02169  281 IKDlgeeeQLRVKEKIGELEAEIASLERSIAEKEReleDAEERLAKLEAEIDKL-------LAEIEELEREIEEERKRRD 353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626   192 RYLNMDRKLKKEIHLLREMVGALSTSSTSAYTAREEAKTKMGMLQERAEKELAQSDTEAQILLRQISHLEQLHRFLK--- 268
Cdd:TIGR02169  354 KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAgie 433
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 568947626   269 ---LKNDERQPDPRV-VQKAEQRDWEVSEGLRKTSQEKLVLR-----YEDTLGKLAQ 316
Cdd:TIGR02169  434 akiNELEEEKEDKALeIKKQEWKLEQLAADLSKYEQELYDLKeeydrVEKELSKLQR 490
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
28-309 7.57e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.67  E-value: 7.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626    28 DGELSRLQRQCKMMELERRAYSKEVHQRLrkqvEEIRQLEMLRAKLQTQINVAQSQVKRLGDKKHLAEMEcllksRAQVQ 107
Cdd:TIGR02168  238 REELEELQEELKEAEEELEELTAELQELE----EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQ-----KQILR 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626   108 VEIEALQEQNRALDKQIQDWETHVLTQSKEASApdlIMYQKMKIQRRIRILEDQLDRVTCHFDIHLVRNAALREELELLR 187
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAE---LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLR 385
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626   188 IERGRYLNMDRKLKKEIHLLREMVGALSTSSTSAYTAREEAKTKmgmLQERAEKEL-AQSDTEAQILLRQISHLEQLHRF 266
Cdd:TIGR02168  386 SKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKK---LEEAELKELqAELEELEEELEELQEELERLEEA 462
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 568947626   267 LKLKNDERQPDPRVVQKAEQRDWEVSEglRKTSQEKLVLRYED 309
Cdd:TIGR02168  463 LEELREELEEAEQALDAAERELAQLQA--RLDSLERLQENLEG 503
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
30-289 1.15e-05

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626  30 ELSRLQRQCKMMELERRAYSkevhQRLRKQVEEIRQLEMLRAKLQTQINVAQSQVKRLgdkkhLAEMECLLKSRAQVQve 109
Cdd:COG1196  296 ELARLEQDIARLEERRRELE----ERLEELEEELAELEEELEELEEELEELEEELEEA-----EEELEEAEAELAEAE-- 364
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626 110 iEALQEQNRALDKQIQDWETHVLTQSKEASapdlimyQKMKIQRRIRILEDQLdrvtchfdihlvrnAALREELELLRIE 189
Cdd:COG1196  365 -EALLEAEAELAEAEEELEELAEELLEALR-------AAAELAAQLEELEEAE--------------EALLERLERLEEE 422
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626 190 RGRYLNMDRKLKKEIHLLREMVGALSTSSTSAYTAREEAKTKmgmlQERAEKELAQSDTEAQILLRQISHLEQLHRFLKL 269
Cdd:COG1196  423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL----LAELLEEAALLEAALAELLEELAEAAARLLLLLE 498
                        250       260
                 ....*....|....*....|
gi 568947626 270 KNDERQPDPRVVQKAEQRDW 289
Cdd:COG1196  499 AEADYEGFLEGVKAALLLAG 518
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
42-288 3.52e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 3.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626  42 ELERRAyskevhQRLRKQVEeirqlemlRAK----LQTQINVAQSQVKRLGDKKHLAEMECLLKSRAQVQVEIEALQEQN 117
Cdd:COG1196  197 ELERQL------EPLERQAE--------KAEryreLKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAEL 262
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626 118 RALDKQIQDWETHVLTQSKEASApdlimyqkmkIQRRIRILEDQLDRVTCHFDIHLVRNAALREELELLRIERGRYLNMD 197
Cdd:COG1196  263 AELEAELEELRLELEELELELEE----------AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL 332
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626 198 RKLKKEIHLLREMVGALSTSSTSAYTAREEAKtkmgmlQERAEKELAQSDTEAQILLRQISHLEQLHRFLKLKNDERQPD 277
Cdd:COG1196  333 EELEEELEELEEELEEAEEELEEAEAELAEAE------EALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
                        250
                 ....*....|.
gi 568947626 278 PRVVQKAEQRD 288
Cdd:COG1196  407 EAEEALLERLE 417
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
44-322 3.96e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 3.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626    44 ERRaysKEVHQRLRKQVEEIRQLEMLRAKLQTQINVAQSQVKR----------LGDKKH---LAEMECLLKSRAQVQVEI 110
Cdd:TIGR02168  172 ERR---KETERKLERTRENLDRLEDILNELERQLKSLERQAEKaerykelkaeLRELELallVLRLEELREELEELQEEL 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626   111 EALQEQNRALDKQIQ----DWETHVL-TQSKEASAPDL-------------IMYQKMKIQRRIRILEDQLDRVTCHFDIH 172
Cdd:TIGR02168  249 KEAEEELEELTAELQeleeKLEELRLeVSELEEEIEELqkelyalaneisrLEQQKQILRERLANLERQLEELEAQLEEL 328
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626   173 LVRNAALREELELLRIERGRylnmdrkLKKEIHLLREMVGALSTSSTSAYTAREEAKTKMGMLQ-ERAEKELAQSDTEAQ 251
Cdd:TIGR02168  329 ESKLDELAEELAELEEKLEE-------LKEELESLEAELEELEAELEELESRLEELEEQLETLRsKVAQLELQIASLNNE 401
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 568947626   252 IlLRQISHLEQLHRFLKLKNDERQPDPRVVQKAEQRDWEVSEGLRKTSQEKLVLRYEDTLGKLAQLTGESD 322
Cdd:TIGR02168  402 I-ERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
51-600 4.50e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 4.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626    51 EVHQRLRKQVEEIRQLEMLRAKLQTQInvAQSQVKRLGDKKHLAEMECLLksrAQVQVEIEALQEQNRALDKQIQDWETH 130
Cdd:TIGR02168  299 RLEQQKQILRERLANLERQLEELEAQL--EELESKLDELAEELAELEEKL---EELKEELESLEAELEELEAELEELESR 373
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626   131 VLTQSKE----ASAPDLIMYQKMKIQRRIRILEDQLDRVTCHFDIHLVRNAALREELELLRIERgrylnMDRKLKKEIHL 206
Cdd:TIGR02168  374 LEELEEQletlRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE-----LQAELEELEEE 448
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626   207 LREMVGALSTSSTSAYTAREEAKTKMGMLQErAEKELAQSDTEAQILLRQISHLEQLHRFLK--LKNDERQPDPRVVqka 284
Cdd:TIGR02168  449 LEELQEELERLEEALEELREELEEAEQALDA-AERELAQLQARLDSLERLQENLEGFSEGVKalLKNQSGLSGILGV--- 524
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626   285 eqrdweVSEGLRktSQEKLVLRYEDTLGKLAQltgesdpDLLVEK---YLEC-EWAEWTRGGGAT---------QHHPKH 351
Cdd:TIGR02168  525 ------LSELIS--VDEGYEAAIEAALGGRLQ-------AVVVENlnaAKKAiAFLKQNELGRVTflpldsikgTEIQGN 589
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626   352 GTLALPWGSCLVSSFHSVAWCASLASASVSFHMSQ-------TSSLHICPLtlsvcfLGPSQifyqpclsrcvgallwlf 424
Cdd:TIGR02168  590 DREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGvlvvddlDNALELAKK------LRPGY------------------ 645
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626   425 lfhlslffclcfcRLATLSDPSVSnsipldpPC---TPPVEERNfaefNFINEQNSEIHHLQEEIKEMQEALVSEHASQD 501
Cdd:TIGR02168  646 -------------RIVTLDGDLVR-------PGgviTGGSAKTN----SSILERRREIEELEEKIEELEEKIAELEKALA 701
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626   502 KQRMQQEQqckmLQQDVDKMCSESEQLEGRFQVLRGQLEKIKTDIQVLFDKAKCDSSVIKDLLGVKTYMRDRDIGLFlST 581
Cdd:TIGR02168  702 ELRKELEE----LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE-EE 776
                          570
                   ....*....|....*....
gi 568947626   582 IERRLVQLLTVQAFLQVQN 600
Cdd:TIGR02168  777 LAEAEAEIEELEAQIEQLK 795
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
27-265 8.81e-04

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 8.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626    27 VDGELSRLQRQCKMMELERRA-YSKEVHQRLRKQVEEIRQLEMLRAKLQTQINVAQSQVKRLGDKKHLAE---------M 96
Cdd:TIGR02169  763 LEARIEELEEDLHKLEEALNDlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEkeiqelqeqR 842
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626    97 ECLLKSRAQVQVEIEALQEQNRALDKQIQDWETHVLTQSKE----ASAPDLIMYQKMKIQRRIRILEDQLDRVTCHFDIH 172
Cdd:TIGR02169  843 IDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRlgdlKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626   173 LVRNAALREEL-----ELLRIERGRYLNMD-RKLKKEIHLLREMVGALSTSSTSAYTAREEAKTKMGMLQERAEKELAQS 246
Cdd:TIGR02169  923 KAKLEALEEELseiedPKGEDEEIPEEELSlEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEER 1002
                          250
                   ....*....|....*....
gi 568947626   247 DteaQILLRqISHLEQLHR 265
Cdd:TIGR02169 1003 K---AILER-IEEYEKKKR 1017
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
472-564 9.64e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.80  E-value: 9.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626   472 INEQNSEIHHLQEEIKEMQEALVSehASQDKQRMQQEQQckMLQQDVDKMCSESEQLEGRFQVLRGQLEKIK---TDIQV 548
Cdd:pfam15921  736 ITAKRGQIDALQSKIQFLEEAMTN--ANKEKHFLKEEKN--KLSQELSTVATEKNKMAGELEVLRSQERRLKekvANMEV 811
                           90
                   ....*....|....*.
gi 568947626   549 LFDKAKCDSSVIKDLL 564
Cdd:pfam15921  812 ALDKASLQFAECQDII 827
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
24-322 1.06e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.36  E-value: 1.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626    24 EGSVDGELSRLQRqckmmelERRAYSKEVHQ------RLRKQVEEI-RQLEMLRAKLQT--------QINVAQSQVKRLG 88
Cdd:TIGR02169  683 LEGLKRELSSLQS-------ELRRIENRLDElsqelsDASRKIGEIeKEIEQLEQEEEKlkerleelEEDLSSLEQEIEN 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626    89 DKKHLAEMECLLKSR----AQVQVEIEAL------------QEQNRALDKQIQDWETHV--LTQSKEASAPDLIMYQKMK 150
Cdd:TIGR02169  756 VKSELKELEARIEELeedlHKLEEALNDLearlshsripeiQAELSKLEEEVSRIEARLreIEQKLNRLTLEKEYLEKEI 835
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626   151 --IQRRIRILEDQLdrvtchfdihlvrnAALREELELLRIERGRYLNMDRKLKKEIHLLREMVGALSTSstsaytaREEA 228
Cdd:TIGR02169  836 qeLQEQRIDLKEQI--------------KSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKE-------RDEL 894
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626   229 KTKMGMLQ----------ERAEKELAQSDTEAQILLRQISHLEQLHRFLKlKNDERQPDPRVVQKAEQRdweVSEGLRKT 298
Cdd:TIGR02169  895 EAQLRELErkieeleaqiEKKRKRLSELKAKLEALEEELSEIEDPKGEDE-EIPEEELSLEDVQAELQR---VEEEIRAL 970
                          330       340       350
                   ....*....|....*....|....*....|...
gi 568947626   299 SQ---------EKLVLRYEDTLGKLAQLTGESD 322
Cdd:TIGR02169  971 EPvnmlaiqeyEEVLKRLDELKEKRAKLEEERK 1003
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
49-273 5.21e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 5.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626   49 SKEVHQRLRKQVEEIRQLEMLRAKLQTQINVAQSQVKRLGDKKHLAEMECLLKSR--AQVQVEIEALQEQNRA------- 119
Cdd:TIGR04523 309 NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRelEEKQNEIEKLKKENQSykqeikn 388
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626  120 LDKQIQDWETHVLTQSKEASapdlimyqkmKIQRRIRILEDQLDRvtchfdihlvrnaaLREELELLRIERgrylnmdRK 199
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQ----------QKDEQIKKLQQEKEL--------------LEKEIERLKETI-------IK 437
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626  200 LKKEIHLLREMVGALSTSSTSAYTAREEAKTKMGML----------QERAEKELAQSDTEAQILLRQISHLEQLHRFLKL 269
Cdd:TIGR04523 438 NNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLsrsinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTK 517

                  ....
gi 568947626  270 KNDE 273
Cdd:TIGR04523 518 KISS 521
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
23-320 7.96e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 7.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626  23 LEGSVDGELSRLQR----QCKMMELERRAYSKEvhQRLRKQVEEIRQLEMLRAKLQTQINVAQSQVKRLGDKKHLAE--- 95
Cdd:PRK03918 219 LREELEKLEKEVKEleelKEEIEELEKELESLE--GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEeyi 296
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626  96 -----MECLLKSRAQVQVEIEALQEQNRALDKQIQDWEthvltqSKEASAPDLiMYQKMKIQRRIRILEDQLDRvtchfd 170
Cdd:PRK03918 297 klsefYEEYLDELREIEKRLSRLEEEINGIEERIKELE------EKEERLEEL-KKKLKELEKRLEELEERHEL------ 363
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626 171 ihLVRNAALREELELLRIERGRY--------LNMDRKLKKEIHL----LREMVGALSTSSTSAYTAREEAKTKMGM---- 234
Cdd:PRK03918 364 --YEEAKAKKEELERLKKRLTGLtpeklekeLEELEKAKEEIEEeiskITARIGELKKEIKELKKAIEELKKAKGKcpvc 441
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568947626 235 ---LQERAEKELAQSDTE-----AQILLRQISHLEQLHRFLKLKNDERQPDPRVV---QKAEQRDwEVSEGLRKTSQEKL 303
Cdd:PRK03918 442 greLTEEHRKELLEEYTAelkriEKELKEIEEKERKLRKELRELEKVLKKESELIklkELAEQLK-ELEEKLKKYNLEEL 520
                        330       340
                 ....*....|....*....|
gi 568947626 304 ---VLRYEDTLGKLAQLTGE 320
Cdd:PRK03918 521 ekkAEEYEKLKEKLIKLKGE 540
 
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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