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Conserved domains on  [gi|2056392219|ref|NP_001382254|]
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myomegalin isoform 44 [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 ...
143-210 1.17e-20

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: 84.49  E-value: 1.17e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392219 143 RDFEKHLNDLKKENFSLKLRIYFLEERMQQKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTW 210
Cdd:pfam07989   1 REQEKQIDKLKKENFNLKLKIHFLEERLEKLAPEQIEEALKENIELKVELETLQRELKKLKKLLREAE 68
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
140-349 8.50e-07

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: 50.83  E-value: 8.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219  140 QALRDFEKHLNDLKKENFSLKLRIYFLE-ERMQQKYEASREDIYKRNIELkVEVESLKRELQDKKQHLDKTW----ADVE 214
Cdd:TIGR02168  220 AELRELELALLVLRLEELREELEELQEElKEAEEELEELTAELQELEEKL-EELRLEVSELEEEIEELQKELyalaNEIS 298
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219  215 NLNSQ------NEAELRRQFEERQQETEHVY---ELLENKIQLLQEESRLAKNEAARMAALVEAEKECNLELSEKLKGVT 285
Cdd:TIGR02168  299 RLEQQkqilreRLANLERQLEELEAQLEELEsklDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2056392219  286 KNWEDVPGDQvkpDQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEPTSMEVQ 349
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 ...
143-210 1.17e-20

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: 84.49  E-value: 1.17e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392219 143 RDFEKHLNDLKKENFSLKLRIYFLEERMQQKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTW 210
Cdd:pfam07989   1 REQEKQIDKLKKENFNLKLKIHFLEERLEKLAPEQIEEALKENIELKVELETLQRELKKLKKLLREAE 68
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
140-349 8.50e-07

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: 50.83  E-value: 8.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219  140 QALRDFEKHLNDLKKENFSLKLRIYFLE-ERMQQKYEASREDIYKRNIELkVEVESLKRELQDKKQHLDKTW----ADVE 214
Cdd:TIGR02168  220 AELRELELALLVLRLEELREELEELQEElKEAEEELEELTAELQELEEKL-EELRLEVSELEEEIEELQKELyalaNEIS 298
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219  215 NLNSQ------NEAELRRQFEERQQETEHVY---ELLENKIQLLQEESRLAKNEAARMAALVEAEKECNLELSEKLKGVT 285
Cdd:TIGR02168  299 RLEQQkqilreRLANLERQLEELEAQLEELEsklDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2056392219  286 KNWEDVPGDQvkpDQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEPTSMEVQ 349
Cdd:TIGR02168  379 EQLETLRSKV---AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
187-342 1.81e-05

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: 46.30  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 187 ELKVEVESLKRELQDKKQHLDKTWADVENLNSQneaelRRQFEERQQETEHVYELLENKIQLLQEESRLAKNEAARMAAL 266
Cdd:COG4942    24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQ-----LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 267 VEAEKEcnlELSEKLKGVTKNWE----------DVPGDQVKPDQYTEALAQ-RDKRIEELNQSLAAQERLVEQLSREKQQ 335
Cdd:COG4942    99 LEAQKE---ELAELLRALYRLGRqpplalllspEDFLDAVRRLQYLKYLAPaRREQAEELRADLAELAALRAELEAERAE 175

                  ....*..
gi 2056392219 336 LLHLLEE 342
Cdd:COG4942   176 LEALLAE 182
PRK01156 PRK01156
chromosome segregation protein; Provisional
127-331 1.16e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.04  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 127 SLRAFEKPPQVQTQALRDFEKHLNDLKKENFSLKLriyfleERMQQKYE------ASREDIykrNIE-LKVEVESLKREL 199
Cdd:PRK01156  526 SARADLEDIKIKINELKDKHDKYEEIKNRYKSLKL------EDLDSKRTswlnalAVISLI---DIEtNRSRSNEIKKQL 596
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 200 QDKKQHLDKTWADVENLNSQNEAELRRQFEERQQETEHVYELLENKIQL--LQEESRLAKNEAARMAALVEAEKECNLEL 277
Cdd:PRK01156  597 NDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIekLRGKIDNYKKQIAEIDSIIPDLKEITSRI 676
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392219 278 SE---KLKGVTKNWEDVPGDQVKPDQYTEALAQrdkRIEELNQSLAAQERLVEQLSR 331
Cdd:PRK01156  677 NDiedNLKKSRKALDDAKANRARLESTIEILRT---RINELSDRINDINETLESMKK 730
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
142-348 5.70e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 38.25  E-value: 5.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 142 LRDFEKHLNDLKKENFSLKLRIYFLEERMQqKYEASREDIYKRNIELKVEVESLKRELQDKKQHLD----KTWADVENLN 217
Cdd:pfam15905  75 QKELEKEIRALVQERGEQDKRLQALEEELE-KVEAKLNAAVREKTSLSASVASLEKQLLELTRVNEllkaKFSEDGTQKK 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 218 SQNEA----ELRRQFEERQQETEHVYELLENKIQLLQEESRLAKNEAARMAA-LVEAEKECNLELSEKLKGVTKNWE--- 289
Cdd:pfam15905 154 MSSLSmelmKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEkLVSTEKEKIEEKSETEKLLEYITElsc 233
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2056392219 290 ---DVPGDQVKPDQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEPTSMEV 348
Cdd:pfam15905 234 vseQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELL 295
 
Name Accession Description Interval E-value
Cnn_1N pfam07989
Centrosomin N-terminal motif 1; This domain has been identified in two microtubule associated ...
143-210 1.17e-20

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: 84.49  E-value: 1.17e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392219 143 RDFEKHLNDLKKENFSLKLRIYFLEERMQQKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTW 210
Cdd:pfam07989   1 REQEKQIDKLKKENFNLKLKIHFLEERLEKLAPEQIEEALKENIELKVELETLQRELKKLKKLLREAE 68
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
140-349 8.50e-07

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: 50.83  E-value: 8.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219  140 QALRDFEKHLNDLKKENFSLKLRIYFLE-ERMQQKYEASREDIYKRNIELkVEVESLKRELQDKKQHLDKTW----ADVE 214
Cdd:TIGR02168  220 AELRELELALLVLRLEELREELEELQEElKEAEEELEELTAELQELEEKL-EELRLEVSELEEEIEELQKELyalaNEIS 298
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219  215 NLNSQ------NEAELRRQFEERQQETEHVY---ELLENKIQLLQEESRLAKNEAARMAALVEAEKECNLELSEKLKGVT 285
Cdd:TIGR02168  299 RLEQQkqilreRLANLERQLEELEAQLEELEsklDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2056392219  286 KNWEDVPGDQvkpDQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEPTSMEVQ 349
Cdd:TIGR02168  379 EQLETLRSKV---AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ 439
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
140-350 2.37e-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: 49.28  E-value: 2.37e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219  140 QALRDFEKHLNDLKKENFSLKLRIYFLEERMQQ------KYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTWADV 213
Cdd:TIGR02168  281 EEIEELQKELYALANEISRLEQQKQILRERLANlerqleELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219  214 ENLNsqneaELRRQFEERQQETEHVYELLENKIQLLQEESRLAKNEAARMAALVEAEKECNLELSEKLKGVTKNWEDVpg 293
Cdd:TIGR02168  361 EELE-----AELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA-- 433
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392219  294 dqvkpdQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEPTSMEVQL 350
Cdd:TIGR02168  434 ------ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREL 484
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
146-345 9.04e-06

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: 47.32  E-value: 9.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 146 EKHLNDLKKENFSLKLRIYFLEERMQQ--KYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTWADVENLNSQNEaE 223
Cdd:TIGR04523 186 QKNIDKIKNKLLKLELLLSNLKKKIQKnkSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQN-K 264
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 224 LRRQFEERQQETEHVYELLENKIQLLQEesrlAKNEaarmaaLVEAEKECNLELSEKLKGVTKNWEDvpgdqvKPDQYTE 303
Cdd:TIGR04523 265 IKKQLSEKQKELEQNNKKIKELEKQLNQ----LKSE------ISDLNNQKEQDWNKELKSELKNQEK------KLEEIQN 328
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2056392219 304 ALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEPTS 345
Cdd:TIGR04523 329 QISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQN 370
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
187-342 1.81e-05

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: 46.30  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 187 ELKVEVESLKRELQDKKQHLDKTWADVENLNSQneaelRRQFEERQQETEHVYELLENKIQLLQEESRLAKNEAARMAAL 266
Cdd:COG4942    24 EAEAELEQLQQEIAELEKELAALKKEEKALLKQ-----LAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 267 VEAEKEcnlELSEKLKGVTKNWE----------DVPGDQVKPDQYTEALAQ-RDKRIEELNQSLAAQERLVEQLSREKQQ 335
Cdd:COG4942    99 LEAQKE---ELAELLRALYRLGRqpplalllspEDFLDAVRRLQYLKYLAPaRREQAEELRADLAELAALRAELEAERAE 175

                  ....*..
gi 2056392219 336 LLHLLEE 342
Cdd:COG4942   176 LEALLAE 182
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
134-350 3.19e-05

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: 45.53  E-value: 3.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 134 PPQVQTQALRDFEKHLNDLKKENFSLKLRIyfleermqQKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTWADV 213
Cdd:COG4942    14 AAAAQADAAAEAEAELEQLQQEIAELEKEL--------AALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 214 ENLNSQnEAELRRQFEERQQEtehvYELLENKIQLLQEESRLA-------KNEAARMAALVEAEKECNLELSEKLKGVTK 286
Cdd:COG4942    86 AELEKE-IAELRAELEAQKEE----LAELLRALYRLGRQPPLAlllspedFLDAVRRLQYLKYLAPARREQAEELRADLA 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2056392219 287 NWEDVPGD-QVKPDQYTEALAQRDKRIEELNQSLAAQERLVEQLSREK----QQLLHLLEEPTSMEVQL 350
Cdd:COG4942   161 ELAALRAElEAERAELEALLAELEEERAALEALKAERQKLLARLEKELaelaAELAELQQEAEELEALI 229
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
151-342 1.89e-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: 43.51  E-value: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219  151 DLKKENFSLKLRIYFLE-ERMQQKYEASREDIykrnIELKVEVESLKRELQdkkqhldKTWADVENLNSQNeAELRRQFE 229
Cdd:TIGR02168  217 ELKAELRELELALLVLRlEELREELEELQEEL----KEAEEELEELTAELQ-------ELEEKLEELRLEV-SELEEEIE 284
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219  230 ERQQEtehvYELLENKIQLLQEESRLAKneaARMAALVEAEKECNLELSEKLKgvtknwedvpgdqvKPDQYTEALAQRD 309
Cdd:TIGR02168  285 ELQKE----LYALANEISRLEQQKQILR---ERLANLERQLEELEAQLEELES--------------KLDELAEELAELE 343
                          170       180       190
                   ....*....|....*....|....*....|...
gi 2056392219  310 KRIEELNQSLAAQERLVEQLSREKQQLLHLLEE 342
Cdd:TIGR02168  344 EKLEELKEELESLEAELEELEAELEELESRLEE 376
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
138-342 2.02e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 138 QTQALRDFEKHLNDLKKENFSLKLRIyfleERMQQKYEASREDIYKRNIELkveveslkRELQDKKQHLDKTWADVENLN 217
Cdd:COG1196   251 LEAELEELEAELAELEAELEELRLEL----EELELELEEAQAEEYELLAEL--------ARLEQDIARLEERRRELEERL 318
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 218 SQNEAELRRQFEERQQETEHVYELLENKIQLLQEESRLAKNEAARMAALVEAEKECNLELSEKLKGVTKNWEDVPGDQVK 297
Cdd:COG1196   319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2056392219 298 PDQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEE 342
Cdd:COG1196   399 AAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
187-342 3.49e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 3.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 187 ELKVEVESLK-RELQDKKQHLDKTWADVENLNSQNEAELrRQFEERQQETEHVYELLENKIQLLQEESRLAKNEAARMAA 265
Cdd:COG1196   224 ELEAELLLLKlRELEAELEELEAELEELEAELEELEAEL-AELEAELEELRLELEELELELEEAQAEEYELLAELARLEQ 302
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2056392219 266 LVEAEKECNLELSEKLKGVTKNWEDVPGDQVK-PDQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEE 342
Cdd:COG1196   303 DIARLEERRRELEERLEELEEELAELEEELEElEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
136-332 4.46e-04

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: 42.31  E-value: 4.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 136 QVQTQALRDFEKHLNDLKKENFSLKLRIYFLEERMQQK------YEASREDIYKRNIELKVEVESLKRELQDKKQHLDKT 209
Cdd:TIGR04523 415 KKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKeliiknLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSK 494
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 210 WADVENLNSQNeaelrRQFEERQQETEHVYELLENKIQLL------------QEESRLAKNEAARMAALVEAEKECNLEL 277
Cdd:TIGR04523 495 EKELKKLNEEK-----KELEEKVKDLTKKISSLKEKIEKLesekkekeskisDLEDELNKDDFELKKENLEKEIDEKNKE 569
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2056392219 278 SEKLKGVTKNWEDvpgdqvKPDQYTEALAQRDKRIEELNQSLAAQERLVEQLSRE 332
Cdd:TIGR04523 570 IEELKQTQKSLKK------KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKE 618
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
136-343 1.07e-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: 41.21  E-value: 1.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219  136 QVQTQALRDFEKHLNDLKKENFSLKLRIYFLEERMQQK------YEASREDIYKRNIELKVEVESLKRELQDKKQHLDKT 209
Cdd:TIGR02169  712 SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLeqeienVKSELKELEARIEELEEDLHKLEEALNDLEARLSHS 791
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219  210 -WADVENLNSQNEAELRRQfEERQQETE-------HVYELLENKIQLLQEESRLAKNEAARMAALVE------------- 268
Cdd:TIGR02169  792 rIPEIQAELSKLEEEVSRI-EARLREIEqklnrltLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEnlngkkeeleeel 870
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392219  269 AEKECNL-ELSEKLKGVTKNWEDVPGD-QVKPDQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEP 343
Cdd:TIGR02169  871 EELEAALrDLESRLGDLKKERDELEAQlRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIP 947
PRK01156 PRK01156
chromosome segregation protein; Provisional
127-331 1.16e-03

chromosome segregation protein; Provisional


Pssm-ID: 100796 [Multi-domain]  Cd Length: 895  Bit Score: 41.04  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 127 SLRAFEKPPQVQTQALRDFEKHLNDLKKENFSLKLriyfleERMQQKYE------ASREDIykrNIE-LKVEVESLKREL 199
Cdd:PRK01156  526 SARADLEDIKIKINELKDKHDKYEEIKNRYKSLKL------EDLDSKRTswlnalAVISLI---DIEtNRSRSNEIKKQL 596
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 200 QDKKQHLDKTWADVENLNSQNEAELRRQFEERQQETEHVYELLENKIQL--LQEESRLAKNEAARMAALVEAEKECNLEL 277
Cdd:PRK01156  597 NDLESRLQEIEIGFPDDKSYIDKSIREIENEANNLNNKYNEIQENKILIekLRGKIDNYKKQIAEIDSIIPDLKEITSRI 676
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392219 278 SE---KLKGVTKNWEDVPGDQVKPDQYTEALAQrdkRIEELNQSLAAQERLVEQLSR 331
Cdd:PRK01156  677 NDiedNLKKSRKALDDAKANRARLESTIEILRT---RINELSDRINDINETLESMKK 730
PRK12704 PRK12704
phosphodiesterase; Provisional
140-282 1.24e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 140 QALRDFEKHLNDLKKENFSLKLriyflEERMQQKYEAS--REDIYKRNIELKVEVESLKRELQDKKQHLDKTWADVENLN 217
Cdd:PRK12704   35 EAEEEAKRILEEAKKEAEAIKK-----EALLEAKEEIHklRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2056392219 218 SQNEAE------LRRQFEERQQETEhvyELLENKIQLLQEESRLAKNEAARMaALVEAEKECNLELSEKLK 282
Cdd:PRK12704  110 EELEKKekeleqKQQELEKKEEELE---ELIEEQLQELERISGLTAEEAKEI-LLEKVEEEARHEAAVLIK 176
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
127-336 2.67e-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: 39.67  E-value: 2.67e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219  127 SLRAFEKPPQVQTQA--LRDFEKHLNDLKKENFSLKLRIYFLEERMQQKyEASREDIYKRNIELKVEVESLKRELQDKKQ 204
Cdd:TIGR02169  666 ILFSRSEPAELQRLRerLEGLKRELSSLQSELRRIENRLDELSQELSDA-SRKIGEIEKEIEQLEQEEEKLKERLEELEE 744
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219  205 HLDKTWADVENLNSQNE------AELRRQFEERQQETEHVY-ELLENKIQLLQEESRLAKNEAARM-AALVEAEKECNLE 276
Cdd:TIGR02169  745 DLSSLEQEIENVKSELKeleariEELEEDLHKLEEALNDLEaRLSHSRIPEIQAELSKLEEEVSRIeARLREIEQKLNRL 824
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219  277 LSEKlkgvTKNWEDVPGDQVKPDQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQL 336
Cdd:TIGR02169  825 TLEK----EYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDL 880
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
195-349 3.27e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 3.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 195 LKRELQDKKQHLDKTWADVENLNSQNEAELRRQFEERQQETEHVYELLENKIQLLQEESRLAKNEAARMAALVEAEKECN 274
Cdd:COG4717    47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2056392219 275 L-ELSEKLKGVTKNWEDVpgdqvkPDQYtEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEPTSMEVQ 349
Cdd:COG4717   127 LlPLYQELEALEAELAEL------PERL-EELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQ 195
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
187-336 4.42e-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: 38.85  E-value: 4.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 187 ELKVEVESLKRELQDKKQHLDKTWADVENLNS--QNEAELRRQFEERQQETEHVYELLENKIQLLQEESRLAKNEAARMa 264
Cdd:TIGR04523 367 EKQNEIEKLKKENQSYKQEIKNLESQINDLESkiQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDL- 445
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2056392219 265 alveAEKECNLELS-EKLKGVTKNWEDvpgdqvKPDQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQL 336
Cdd:TIGR04523 446 ----TNQDSVKELIiKNLDNTRESLET------QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEL 508
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
179-329 4.82e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 4.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219  179 EDIYKRNIELKVEVESLkRELQDKKQHLDKTWADvenLNSQNEAELRRQFEERQQEtehvYELLENKIQLLQEEsrLAKN 258
Cdd:COG4913    238 ERAHEALEDAREQIELL-EPIRELAERYAAARER---LAELEYLRAALRLWFAQRR----LELLEAELEELRAE--LARL 307
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2056392219  259 EAARmaALVEAEKEcnlELSEKLKGVTKNWEDVPGDQVkpDQYTEALAQRDKRIEELNQSLAAQERLVEQL 329
Cdd:COG4913    308 EAEL--ERLEARLD---ALREELDELEAQIRGNGGDRL--EQLEREIERLERELEERERRRARLEALLAAL 371
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
142-348 5.70e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 38.25  E-value: 5.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 142 LRDFEKHLNDLKKENFSLKLRIYFLEERMQqKYEASREDIYKRNIELKVEVESLKRELQDKKQHLD----KTWADVENLN 217
Cdd:pfam15905  75 QKELEKEIRALVQERGEQDKRLQALEEELE-KVEAKLNAAVREKTSLSASVASLEKQLLELTRVNEllkaKFSEDGTQKK 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 218 SQNEA----ELRRQFEERQQETEHVYELLENKIQLLQEESRLAKNEAARMAA-LVEAEKECNLELSEKLKGVTKNWE--- 289
Cdd:pfam15905 154 MSSLSmelmKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEkLVSTEKEKIEEKSETEKLLEYITElsc 233
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2056392219 290 ---DVPGDQVKPDQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEEPTSMEV 348
Cdd:pfam15905 234 vseQVEKYKLDIAQLEELLKEKNDEIESLKQSLEEKEQELSKQIKDLNEKCKLLESEKEELL 295
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
187-342 6.08e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.27  E-value: 6.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 187 ELKVEVESLKRELQDKKQHLDKTWADVENLNSQnEAELRRQFEERQQETEHVYELLENKIQLLQEESRLAK--------- 257
Cdd:COG3883    34 AAQAELDALQAELEELNEEYNELQAELEALQAE-IDKLQAEIAEAEAEIEERREELGERARALYRSGGSVSyldvllgse 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 258 ------NEAARMAALVEAEKECNLELSEKLKGVTKNWEDVpgdQVKPDQYTEALAQRDKRIEELNQSLAAQERLVEQLSR 331
Cdd:COG3883   113 sfsdflDRLSALSKIADADADLLEELKADKAELEAKKAEL---EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189
                         170
                  ....*....|.
gi 2056392219 332 EKQQLLHLLEE 342
Cdd:COG3883   190 EEAAAEAQLAE 200
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
145-332 6.30e-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: 38.51  E-value: 6.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219  145 FEKHLNDLKKENFSLKLRIYFLEERMQQ-------------KYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTWA 211
Cdd:TIGR02169  292 VKEKIGELEAEIASLERSIAEKERELEDaeerlakleaeidKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRA 371
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219  212 DVENLnsqnEAELRRQFEERQQETEHVYEL------LENKIQLLQEESRLAKNEAARMAALVEAEKECNLELSEKLKGVT 285
Cdd:TIGR02169  372 ELEEV----DKEFAETRDELKDYREKLEKLkreineLKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2056392219  286 knwEDVPGDQVKPDQYTEALAQRDKRIEELNQSLAAQERLVEQLSRE 332
Cdd:TIGR02169  448 ---LEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE 491
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
142-342 6.91e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.51  E-value: 6.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 142 LRDFEKHLNDLKKENFSLKLRIYFLEermqqKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDKTWADVENLNSQNE 221
Cdd:PRK03918  157 LDDYENAYKNLGEVIKEIKRRIERLE-----KFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 222 A--ELRRQFEERQQETEHV---YELLENKIQllQEESRLAKNEaARMAALVEAEKEcnlelSEKLKGVTKNWEDVPGDQv 296
Cdd:PRK03918  232 EleELKEEIEELEKELESLegsKRKLEEKIR--ELEERIEELK-KEIEELEEKVKE-----LKELKEKAEEYIKLSEFY- 302
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2056392219 297 kpDQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEE 342
Cdd:PRK03918  303 --EEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKK 346
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
141-342 8.96e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.12  E-value: 8.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 141 ALRDFEKHLNDLK-----KENFSLKLRIYFLE--ERMQQKYEASREDIYKRNIELKVEVESLKRELQDKKQHLDK----- 208
Cdd:PRK03918  356 ELEERHELYEEAKakkeeLERLKKRLTGLTPEklEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEElkkak 435
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2056392219 209 ----------TWADVENLNSQNEAELRRQFEERQQETEHVYELLENKIQL---LQEESRLAKNEAArMAALVEAEKECNL 275
Cdd:PRK03918  436 gkcpvcgrelTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELekvLKKESELIKLKEL-AEQLKELEEKLKK 514
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2056392219 276 ELSEKLKGVTKNWEDVPGDQVKPDQYTEALAQRDKRIEELNQSLAAQERLVEQLSREKQQLLHLLEE 342
Cdd:PRK03918  515 YNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEE 581
 
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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