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Conserved domains on  [gi|2056392190|ref|NP_001382255|]
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myomegalin isoform 45 [Homo sapiens]

Protein Classification

Cnn_1N and PRK12704 domain-containing protein( domain architecture ID 10546816)

Cnn_1N and PRK12704 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Cnn_1N pfam07989
Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated ...
 72-139 7.90e-18

Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated proteins in Schizosaccharomyces pombe, Mto1 and Pcp1. Mto1 has been identified in association with spindle pole body and non-spindle pole body microtubules. The pericentrin homolog Pcp1 is also associated with the fungal centrosome or spindle pole body (SPB). Members of this family have been named centrosomins, and are an essential mitotic centrosome component required for assembly of all other known pericentriolar matrix proteins in order to achieve microtubule-organizing activity in fission yeast. Cnn_1N is a short conserved motif towards the N-terminus. Motif 1 is found to be necessary for proper recruitment of gamma-tubulin, D-TACC (the homolog of vertebrate transforming acidic coiled-coil proteins [TACC]), and Minispindles (Msps) to embryonic centrosomes but is not required for assembly of other centrosome components including Aurora A kinase and CP60 in Drosophila.


:

Pssm-ID: 462333 [Multi-domain]  Cd Length: 69  Bit Score: 75.64  E-value: 7.90e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392190  72 RDFEKHLNDLKKENFSLKLRIYFLEERMQQKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTW 139
Cdd:pfam07989   1 REQEKQIDKLKKENFNLKLKIHFLEERLEKLAPEQIEEALKENIELKVELETLQRELKKLKKLLREAE 68
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 69-278 4.29e-05

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: 44.66  E-value: 4.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392190   69 QALRDFEKHLNDLKKENFSLKLRIYFLE-ERMQQKYEASREDIYKRNIELkVEVESLKRELQDKKQHLDKTWADVENLNS 147
Cdd:TIGR02168  220 AELRELELALLVLRLEELREELEELQEElKEAEEELEELTAELQELEEKL-EELRLEVSELEEEIEELQKELYALANEIS 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392190  148 QNEAELRRQFEERQQ------ETEHVYELLENKIQLLQEESRL-------AKNEAARMAALVEAEKECNLELSEKLKGVT 214
Cdd:TIGR02168  299 RLEQQKQILRERLANlerqleELEAQLEELESKLDELAEELAEleekleeLKEELESLEAELEELEAELEELESRLEELE 378

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2056392190  215 KNWEDVPGDQvkpDQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEPTSMEVQ 278
Cdd:TIGR02168  379 EQLETLRSKV---AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
 
Name Accession Description Interval E-value
Cnn_1N pfam07989
Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated ...
 72-139 7.90e-18

Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated proteins in Schizosaccharomyces pombe, Mto1 and Pcp1. Mto1 has been identified in association with spindle pole body and non-spindle pole body microtubules. The pericentrin homolog Pcp1 is also associated with the fungal centrosome or spindle pole body (SPB). Members of this family have been named centrosomins, and are an essential mitotic centrosome component required for assembly of all other known pericentriolar matrix proteins in order to achieve microtubule-organizing activity in fission yeast. Cnn_1N is a short conserved motif towards the N-terminus. Motif 1 is found to be necessary for proper recruitment of gamma-tubulin, D-TACC (the homolog of vertebrate transforming acidic coiled-coil proteins [TACC]), and Minispindles (Msps) to embryonic centrosomes but is not required for assembly of other centrosome components including Aurora A kinase and CP60 in Drosophila.


Pssm-ID: 462333 [Multi-domain]  Cd Length: 69  Bit Score: 75.64  E-value: 7.90e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392190  72 RDFEKHLNDLKKENFSLKLRIYFLEERMQQKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTW 139
Cdd:pfam07989   1 REQEKQIDKLKKENFNLKLKIHFLEERLEKLAPEQIEEALKENIELKVELETLQRELKKLKKLLREAE 68
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 69-278 4.29e-05

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: 44.66  E-value: 4.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392190   69 QALRDFEKHLNDLKKENFSLKLRIYFLE-ERMQQKYEASREDIYKRNIELkVEVESLKRELQDKKQHLDKTWADVENLNS 147
Cdd:TIGR02168  220 AELRELELALLVLRLEELREELEELQEElKEAEEELEELTAELQELEEKL-EELRLEVSELEEEIEELQKELYALANEIS 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392190  148 QNEAELRRQFEERQQ------ETEHVYELLENKIQLLQEESRL-------AKNEAARMAALVEAEKECNLELSEKLKGVT 214
Cdd:TIGR02168  299 RLEQQKQILRERLANlerqleELEAQLEELESKLDELAEELAEleekleeLKEELESLEAELEELEAELEELESRLEELE 378

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2056392190  215 KNWEDVPGDQvkpDQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEPTSMEVQ 278
Cdd:TIGR02168  379 EQLETLRSKV---AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 116-271 3.64e-04

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: 41.29  E-value: 3.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392190 116 ELKVEVESLKRELQDKKQHLDKTWADVENLNSQneaelRRQFEERQQETEHVYELLENKIQLLQEESRLAKNEAARMAAL 195
Cdd:COG4942    24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQ-----LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392190 196 VEAEKEcnlELSEKLKGVTKNWE----------DVPGDQVKPDQYTEALAQ-RDKRIEELNQSLAAQERLVEQLSREKQQ 264
Cdd:COG4942    99 LEAQKE---ELAELLRALYRLGRqpplalllspEDFLDAVRRLQYLKYLAPaRREQAEELRADLAELAALRAELEAERAE 175


                  ....*..
gi 2056392190 265 LLHLLEE 271
Cdd:COG4942   176 LEALLAE 182
PRK12704 PRK12704
phosphodiesterase; Provisional
 100-211 5.92e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 37.84  E-value: 5.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392190 100 QQKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTWADVENLNSQNEAE------LRRQFEERQQETEhvyELLEN 173
Cdd:PRK12704   63 KEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKekeleqKQQELEKKEEELE---ELIEE 139

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2056392190 174 KIQLLQEESRLAKNEAARMaALVEAEKECNLELSEKLK 211
Cdd:PRK12704  140 QLQELERISGLTAEEAKEI-LLEKVEEEARHEAAVLIK 176
 
Name Accession Description Interval E-value
Cnn_1N pfam07989
Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated ...
 72-139 7.90e-18

Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated proteins in Schizosaccharomyces pombe, Mto1 and Pcp1. Mto1 has been identified in association with spindle pole body and non-spindle pole body microtubules. The pericentrin homolog Pcp1 is also associated with the fungal centrosome or spindle pole body (SPB). Members of this family have been named centrosomins, and are an essential mitotic centrosome component required for assembly of all other known pericentriolar matrix proteins in order to achieve microtubule-organizing activity in fission yeast. Cnn_1N is a short conserved motif towards the N-terminus. Motif 1 is found to be necessary for proper recruitment of gamma-tubulin, D-TACC (the homolog of vertebrate transforming acidic coiled-coil proteins [TACC]), and Minispindles (Msps) to embryonic centrosomes but is not required for assembly of other centrosome components including Aurora A kinase and CP60 in Drosophila.


Pssm-ID: 462333 [Multi-domain]  Cd Length: 69  Bit Score: 75.64  E-value: 7.90e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392190  72 RDFEKHLNDLKKENFSLKLRIYFLEERMQQKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTW 139
Cdd:pfam07989   1 REQEKQIDKLKKENFNLKLKIHFLEERLEKLAPEQIEEALKENIELKVELETLQRELKKLKKLLREAE 68
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 69-278 4.29e-05

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: 44.66  E-value: 4.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392190   69 QALRDFEKHLNDLKKENFSLKLRIYFLE-ERMQQKYEASREDIYKRNIELkVEVESLKRELQDKKQHLDKTWADVENLNS 147
Cdd:TIGR02168  220 AELRELELALLVLRLEELREELEELQEElKEAEEELEELTAELQELEEKL-EELRLEVSELEEEIEELQKELYALANEIS 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392190  148 QNEAELRRQFEERQQ------ETEHVYELLENKIQLLQEESRL-------AKNEAARMAALVEAEKECNLELSEKLKGVT 214
Cdd:TIGR02168  299 RLEQQKQILRERLANlerqleELEAQLEELESKLDELAEELAEleekleeLKEELESLEAELEELEAELEELESRLEELE 378

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2056392190  215 KNWEDVPGDQvkpDQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEPTSMEVQ 278
Cdd:TIGR02168  379 EQLETLRSKV---AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 69-279 6.76e-05

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: 44.28  E-value: 6.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392190   69 QALRDFEKHLNDLKKENFSLKLRIYFLEERMQQ------KYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTWADV 142
Cdd:TIGR02168  281 EEIEELQKELYALANEISRLEQQKQILRERLANlerqleELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392190  143 ENLNsqneaELRRQFEERQQETEHVYELLENKIQLLQEESRLAKNEAARMAALVEAEKECNLELSEKLKGVTKNWEDVpg 222
Cdd:TIGR02168  361 EELE-----AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA-- 433

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392190  223 dqvkpdQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEPTSMEVQL 279
Cdd:TIGR02168  434 ------ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 116-271 3.64e-04

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: 41.29  E-value: 3.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392190 116 ELKVEVESLKRELQDKKQHLDKTWADVENLNSQneaelRRQFEERQQETEHVYELLENKIQLLQEESRLAKNEAARMAAL 195
Cdd:COG4942    24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQ-----LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392190 196 VEAEKEcnlELSEKLKGVTKNWE----------DVPGDQVKPDQYTEALAQ-RDKRIEELNQSLAAQERLVEQLSREKQQ 264
Cdd:COG4942    99 LEAQKE---ELAELLRALYRLGRqpplalllspEDFLDAVRRLQYLKYLAPaRREQAEELRADLAELAALRAELEAERAE 175


                  ....*..
gi 2056392190 265 LLHLLEE 271
Cdd:COG4942   176 LEALLAE 182
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 63-279 1.17e-03

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: 39.75  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392190  63 PPQVQTQALRDFEKHLNDLKKENFSLKLRIyfleermqQKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTWADV 142
Cdd:COG4942    14 AAAAQADAAAEAEAELEQLQQEIAELEKEL--------AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392190 143 ENLNSQnEAELRRQFEERQQEtehvYELLENKIQLLQEESRLA-------KNEAARMAALVEAEKECNLELSEKLKGVTK 215
Cdd:COG4942    86 AELEKE-IAELRAELEAQKEE----LAELLRALYRLGRQPPLAlllspedFLDAVRRLQYLKYLAPARREQAEELRADLA 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2056392190 216 NWEDVPGD-QVKPDQYTEALAQRDKRIEELNQSLAAQERLVEQLSREK----QQLLHLLEEPTSMEVQL 279
Cdd:COG4942   161 ELAALRAElEAERAELEALLAELEEERAALEALKAERQKLLARLEKELaelaAELAELQQEAEELEALI 229
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 67-271 1.94e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 1.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392190  67 QTQALRDFEKHLNDLKKENFSLKLRIyfleERMQQKYEASREDIYKRNIELkveveslkRELQDKKQHLDKTWADVENLN 146
Cdd:COG1196   251 LEAELEELEAELAELEAELEELRLEL----EELELELEEAQAEEYELLAEL--------ARLEQDIARLEERRRELEERL 318

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392190 147 SQNEAELRRQFEERQQETEHVYELLENKIQLLQEESRLAKNEAARMAALVEAEKECNLELSEKLKGVTKNWEDVPGDQVK 226
Cdd:COG1196   319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2056392190 227 PDQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEE 271
Cdd:COG1196   399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 116-271 3.21e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 3.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392190 116 ELKVEVESLK-RELQDKKQHLDKTWADVENLNSQNEAELrRQFEERQQETEHVYELLENKIQLLQEESRLAKNEAARMAA 194
Cdd:COG1196   224 ELEAELLLLKlRELEAELEELEAELEELEAELEELEAEL-AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392190 195 LVEAEKECNLELSEKLKGVTKNWEDVPGDQVK-PDQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEE 271
Cdd:COG1196   303 DIARLEERRRELEERLEELEEELAELEEELEElEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
PRK12704 PRK12704
phosphodiesterase; Provisional
 100-211 5.92e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 37.84  E-value: 5.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392190 100 QQKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTWADVENLNSQNEAE------LRRQFEERQQETEhvyELLEN 173
Cdd:PRK12704   63 KEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKekeleqKQQELEKKEEELE---ELIEE 139

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2056392190 174 KIQLLQEESRLAKNEAARMaALVEAEKECNLELSEKLK 211
Cdd:PRK12704  140 QLQELERISGLTAEEAKEI-LLEKVEEEARHEAAVLIK 176
 
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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