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Conserved domains on  [gi|113677306|ref|NP_001038475|]
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uncharacterized protein LOC563117 [Danio rerio]

Protein Classification

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 ...
 2-154 1.91e-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: 47.74  E-value: 1.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306     2 QTISSLQEQKEDLRKRLSYTTHKLELLEREFDSTrqylETELRRAQEELDKFTDKLRRIQSSYSALQrinqDLEDKIHRN 81
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERRIAAT----ERRLEDLEEQIEELSEDIESLAAEIEELE----ELIEELESE 874

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113677306    82 SQHHDDEKRALSREIIVLNNHLMEAKMTIEKLREDNDLYRKDCNLAAQLLqcnkSHYRAQLSELP---AEFQERVS 154
Cdd:TIGR02168  875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL----AQLELRLEGLEvriDNLQERLS 946
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-154 1.91e-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: 47.74  E-value: 1.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306     2 QTISSLQEQKEDLRKRLSYTTHKLELLEREFDSTrqylETELRRAQEELDKFTDKLRRIQSSYSALQrinqDLEDKIHRN 81
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERRIAAT----ERRLEDLEEQIEELSEDIESLAAEIEELE----ELIEELESE 874

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113677306    82 SQHHDDEKRALSREIIVLNNHLMEAKMTIEKLREDNDLYRKDCNLAAQLLqcnkSHYRAQLSELP---AEFQERVS 154
Cdd:TIGR02168  875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL----AQLELRLEGLEvriDNLQERLS 946
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2-148 2.33e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306   2 QTISSLQEQKEDLRKRLSYTTHKLELLEREFDSTRQYLetELRRAQEELDKFTDKLRRIQS---SYSALQRINQDLEDKI 78
Cdd:COG4717   95 EELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ--ELEALEAELAELPERLEELEErleELRELEEELEELEAEL 172

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306  79 HRNSQHHDDEKRALSREIIvlnNHLMEAKMTIEKLREDNDLYRKdcnlAAQLLQCNKSHYRAQLSELPAE 148
Cdd:COG4717  173 AELQEELEELLEQLSLATE---EELQDLAEELEELQQRLAELEE----ELEEAQEELEELEEELEQLENE 235
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 1-115 3.70e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 43.08  E-value: 3.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306     1 MQTISSLqeqKEDLRKRLSYTTHKLELLEREFDSTRQYLETELRRAQEELDKFTDKLRRIQSSYSALQRINQDLEDKIHR 80
Cdd:smart00787 167 LELLNSI---KPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIED 243

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 113677306    81 -NSQHHDDEKRALSREIIVLNNHLMEAKmTIEKLRE 115
Cdd:smart00787 244 lTNKKSELNTEIAEAEKKLEQCRGFTFK-EIEKLKE 278
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
4-148 1.62e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306   4 ISSLQEQKEDLRKRLSytthKLELLEREFDSTRQYlETELRRAQEELDKFTDKLRRIQSSYSALQRINQDLEDKIhrnsq 83
Cdd:PRK03918 261 IRELEERIEELKKEIE----ELEEKVKELKELKEK-AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI----- 330

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113677306  84 hhdDEKRALSREIIVLNNHLMEAKMTIEKLREDNDLYRKdcnlaAQLLQCNKSHYRAQLSELPAE 148
Cdd:PRK03918 331 ---KELEEKEERLEELKKKLKELEKRLEELEERHELYEE-----AKAKKEELERLKKRLTGLTPE 387
 
Name Accession Description Interval E-value
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-154 1.91e-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: 47.74  E-value: 1.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306     2 QTISSLQEQKEDLRKRLSYTTHKLELLEREFDSTrqylETELRRAQEELDKFTDKLRRIQSSYSALQrinqDLEDKIHRN 81
Cdd:TIGR02168  803 EALDELRAELTLLNEEAANLRERLESLERRIAAT----ERRLEDLEEQIEELSEDIESLAAEIEELE----ELIEELESE 874

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113677306    82 SQHHDDEKRALSREIIVLNNHLMEAKMTIEKLREDNDLYRKDCNLAAQLLqcnkSHYRAQLSELP---AEFQERVS 154
Cdd:TIGR02168  875 LEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKL----AQLELRLEGLEvriDNLQERLS 946
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
2-148 2.33e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.45  E-value: 2.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306   2 QTISSLQEQKEDLRKRLSYTTHKLELLEREFDSTRQYLetELRRAQEELDKFTDKLRRIQS---SYSALQRINQDLEDKI 78
Cdd:COG4717   95 EELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ--ELEALEAELAELPERLEELEErleELRELEEELEELEAEL 172

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306  79 HRNSQHHDDEKRALSREIIvlnNHLMEAKMTIEKLREDNDLYRKdcnlAAQLLQCNKSHYRAQLSELPAE 148
Cdd:COG4717  173 AELQEELEELLEQLSLATE---EELQDLAEELEELQQRLAELEE----ELEEAQEELEELEEELEQLENE 235
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1-153 3.03e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.43  E-value: 3.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306   1 MQTISSLQEQKEDLRKRLSYTTHKLELLEREFDSTR---QYLETELRRAQEELDKFTDKLRRIQSSYSALQRINQDLEDK 77
Cdd:COG4372   37 LFELDKLQEELEQLREELEQAREELEQLEEELEQARselEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEE 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306  78 IHR-NSQHHD--DEKRALSREIIVLNNHLMEAKMTIEKLRED-NDLYRKDCNLAAQLLQCNKSHYRAQLSELPAEFQERV 153
Cdd:COG4372  117 LEElQKERQDleQQRKQLEAQIAELQSEIAEREEELKELEEQlESLQEELAALEQELQALSEAEAEQALDELLKEANRNA 196
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 4-151 4.69e-05

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 45.30  E-value: 4.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306   4 ISSLQEQKEDLRKRLSYTTHKLELLEREfdstRQYLETELRRAQEELDKFTDKLRRIQSS--YSALQRinqdledkihrn 81
Cdd:COG1579   33 LAELEDELAALEARLEAAKTELEDLEKE----IKRLELEIEEVEARIKKYEEQLGNVRNNkeYEALQK------------ 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306  82 sqhhddEKRALSREIIVLNNHLMEAKMTIEKLREDNDLYRKDCNLAAQLLQCNKSHYRAQLSELPAEFQE 151
Cdd:COG1579   97 ------EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEE 160
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 10-154 5.60e-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: 46.20  E-value: 5.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306    10 QKEDLRKRLSYTTHKLELLEREFDStrqyLETELRRAQEELDKFTDKLRRIQSSYSALQRINQDLEDKIHR---NSQHHD 86
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEE----LTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRleqQKQILR 308

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306    87 DEKRALSREIIVLNNHLMEAKMTIEKLREDNDLyrkdcnLAAQLLQCNKSH--YRAQLSELPAEFQERVS 154
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEELAE------LEEKLEELKEELesLEAELEELEAELEELES 372
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 2-99 9.41e-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: 45.14  E-value: 9.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306   2 QTISSLQEQKEDLRKRLSYTTHKLELLEREfdstRQYLETELRRAQEELDKFTDKLRRIQSSYSALQRINQDLEDKIHRN 81
Cdd:COG4942   20 DAAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95

                         90
                 ....*....|....*...
gi 113677306  82 SQHHDDEKRALSREIIVL 99
Cdd:COG4942   96 RAELEAQKEELAELLRAL 113
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 1-115 3.70e-04

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 43.08  E-value: 3.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306     1 MQTISSLqeqKEDLRKRLSYTTHKLELLEREFDSTRQYLETELRRAQEELDKFTDKLRRIQSSYSALQRINQDLEDKIHR 80
Cdd:smart00787 167 LELLNSI---KPKLRDRKDALEEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEIMIKVKKLEELEEELQELESKIED 243

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 113677306    81 -NSQHHDDEKRALSREIIVLNNHLMEAKmTIEKLRE 115
Cdd:smart00787 244 lTNKKSELNTEIAEAEKKLEQCRGFTFK-EIEKLKE 278
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 4-151 4.42e-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: 43.52  E-value: 4.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306     4 ISSLQEQKEDLRKRLSYTTHKLELLEREFDSTRQYLETELRRAQEElDKFTDKLRRIQSSY-SALQRINQDLEDkIHRNS 82
Cdd:TIGR02169  331 IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEV-DKEFAETRDELKDYrEKLEKLKREINE-LKREL 408

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 113677306    83 QHHDDEKRALSREIIVLNNHLMEAKMTIEKLREDNDLYRKDCNLAAQLLQCNK---SHYRAQLSELPAEFQE 151
Cdd:TIGR02169  409 DRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAadlSKYEQELYDLKEEYDR 480
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 2-117 6.71e-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: 42.70  E-value: 6.71e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306    2 QTISSLQEQKEDLRKRLSYTTHKLELLEREFDSTRQYLETELRRAQEELDKFTDKLRRIQSSYSALQRI---NQDLEDKI 78
Cdd:TIGR04523 335 KIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQeklNQQKDEQI 414

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 113677306   79 HRNSQhhddEKRALSREIIVLNNHLMEAKMTIEKLREDN 117
Cdd:TIGR04523 415 KKLQQ----EKELLEKEIERLKETIIKNNSEIKDLTNQD 449
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
4-148 1.62e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306   4 ISSLQEQKEDLRKRLSytthKLELLEREFDSTRQYlETELRRAQEELDKFTDKLRRIQSSYSALQRINQDLEDKIhrnsq 83
Cdd:PRK03918 261 IRELEERIEELKKEIE----ELEEKVKELKELKEK-AEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERI----- 330

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113677306  84 hhdDEKRALSREIIVLNNHLMEAKMTIEKLREDNDLYRKdcnlaAQLLQCNKSHYRAQLSELPAE 148
Cdd:PRK03918 331 ---KELEEKEERLEELKKKLKELEKRLEELEERHELYEE-----AKAKKEELERLKKRLTGLTPE 387
46 PHA02562
endonuclease subunit; Provisional
 1-132 1.74e-03

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.15  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306   1 MQTISSLQEQKEDLRKRLSYTTHKLELLEREFDSTRQyLETELRRAQEELDKFTDKLRRIQSSYSALQRINQDLEDKIHR 80
Cdd:PHA02562 291 TQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEE-IMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEE 369

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 113677306  81 NSQHHDDEKralsREIIVLNNHLMEAKMTIEKLREDNDLYrkdcNLAAQLLQ 132
Cdd:PHA02562 370 LQAEFVDNA----EELAKLQDELDKIVKTKSELVKEKYHR----GIVTDLLK 413
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1-99 2.18e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 2.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306   1 MQTISSLQEQKEDLRKRLsytTHKLELLEREFDSTRQYLETELRRAQEELDKFTDKLRRIQSSYSALQRINQDLEDKIHR 80
Cdd:COG4717  155 LEELRELEEELEELEAEL---AELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQ 231

                         90       100
                 ....*....|....*....|.
gi 113677306  81 --NSQHHDDEKRALSREIIVL 99
Cdd:COG4717  232 leNELEAAALEERLKEARLLL 252
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
5-116 3.53e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 3.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306   5 SSLQEQKEDLRK--RLSYTTHKLELLEREFDStrqyLETELRRAQEELDKFTDKLRRIQSSYSALQRINQDLEdkiHRNS 82
Cdd:PRK03918 592 ERLKELEPFYNEylELKDAEKELEREEKELKK----LEEELDKAFEELAETEKRLEELRKELEELEKKYSEEE---YEEL 664

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 113677306  83 QhhdDEKRALSREII-------VLNNHLMEAKMTIEKLRED 116
Cdd:PRK03918 665 R---EEYLELSRELAglraeleELEKRREEIKKTLEKLKEE 702
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 2-151 3.93e-03

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: 40.43  E-value: 3.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306     2 QTISSLQEQK---EDLRKrlsytthKLELLEREFDSTRQYLEtELRRAQEELDKFTDKLRRI-----------QSSYSAL 67
Cdd:TIGR02168  667 KTNSSILERRreiEELEE-------KIEELEEKIAELEKALA-ELRKELEELEEELEQLRKEleelsrqisalRKDLARL 738

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306    68 QRINQDLEDKIHRNS---QHHDDEKRALSREIIVLNNHLMEAKMTIEKLREDndlyrkdcnLAAQLLQCNKShyRAQLSE 144
Cdd:TIGR02168  739 EAEVEQLEERIAQLSkelTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ---------IEQLKEELKAL--REALDE 807


                   ....*..
gi 113677306   145 LPAEFQE 151
Cdd:TIGR02168  808 LRAELTL 814
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 2-145 4.17e-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: 4.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306    2 QTISSLQEQKEDLRKrlsyTTHKLELLEREFDSTRQYLETelrraqeELDKFTDKLRRIQSSysaLQRINQDLEDKihrN 81
Cdd:TIGR04523 433 ETIIKNNSEIKDLTN----QDSVKELIIKNLDNTRESLET-------QLKVLSRSINKIKQN---LEQKQKELKSK---E 495

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 113677306   82 SQHH--DDEKRALSREIIVLNNHLMEAKMTIEKLRE------------DNDLYRKDCNLAAQLLQCNKSHYRAQLSEL 145
Cdd:TIGR04523 496 KELKklNEEKKELEEKVKDLTKKISSLKEKIEKLESekkekeskisdlEDELNKDDFELKKENLEKEIDEKNKEIEEL 573
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
24-116 4.17e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 4.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306   24 KLELLEREfdstRQYLETELRRAQEELDKFTDKLRRIQSSYSALQRINQDLEDKI-----HRNSQHHDDEKRALSREiiv 98
Cdd:COG4913   611 KLAALEAE----LAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvasaEREIAELEAELERLDAS--- 683

                          90
                  ....*....|....*...
gi 113677306   99 lNNHLMEAKMTIEKLRED 116
Cdd:COG4913   684 -SDDLAALEEQLEELEAE 700
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 2-151 4.30e-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: 4.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306   2 QTISSLQEQKEDLRKRLSYTTHKLELLEREFDSTRQYLETELRRAQ-----EEL------DKFTDKLRRIQsSYSALQRI 70
Cdd:COG4942   69 RRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYrlgrqPPLalllspEDFLDAVRRLQ-YLKYLAPA 147

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306  71 NQDLEDKIHRNSQHHDDEKRALSREIIVLNNHLMEAKMTIEKLREDndlyRKDCNLAAQLLQCNKSHYRAQLSELPAEFQ 150
Cdd:COG4942  148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEAL----KAERQKLLARLEKELAELAAELAELQQEAE 223


                 .
gi 113677306 151 E 151
Cdd:COG4942  224 E 224
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 10-152 4.67e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 4.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306  10 QKEDLRKRLSYTTHKLELLEREFDStrqyLETELRRAQEELDKFTDKLRRIQSSYSALQRINQDLEDKIHRNSQ---HHD 86
Cdd:COG1196  233 KLRELEAELEELEAELEELEAELEE----LEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQdiaRLE 308

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 113677306  87 DEKRALSREIIVLNNHLMEAKMTIEKLREDNDLYRKDCNLAAQLLQCNKSHYRAQLSELPAEFQER 152
Cdd:COG1196  309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
2-152 5.77e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 5.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306    2 QTISSLQEQKEDLRKRLSYTTHKLELLER--EFDSTR---QYLETELRRAQ---EELDKFTDKLRRIQSSYSALQRINQD 73
Cdd:COG4913   624 EELAEAEERLEALEAELDALQERREALQRlaEYSWDEidvASAEREIAELEaelERLDASSDDLAALEEQLEELEAELEE 703

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 113677306   74 LEdkihrnsqhhdDEKRALSREIIVLNNHLMEAKMTIEKLREDNDLYRKDCNLaAQLLQCNKSHYRAQLSELPAEFQER 152
Cdd:COG4913   704 LE-----------EELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL-ELRALLEERFAAALGDAVERELREN 770
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 2-204 7.16e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 7.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306   2 QTISSLQEQKEDLRKRLSYTTHKLELLEREFDSTRQ----------YLETELRRAQEELDKFTDKL-RRIQSSYSALQRI 70
Cdd:COG3883   23 KELSELQAELEAAQAELDALQAELEELNEEYNELQAelealqaeidKLQAEIAEAEAEIEERREELgERARALYRSGGSV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306  71 N-----------QDLEDKIHRNSQHHDDEKRALsREIIVLNNHLMEAKMTIEKLREDNDLYRKDCNLAAQLLQCNKSHYR 139
Cdd:COG3883  103 SyldvllgsesfSDFLDRLSALSKIADADADLL-EELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQE 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 113677306 140 AQLSELPAEFQERVSLHMEGSSLCHSPYADTVPASVIAKVLEKPEEACSSQASRSPSPQPQERQG 204
Cdd:COG3883  182 ALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 26-152 7.40e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 39.43  E-value: 7.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306  26 ELLEREFDStRQYLETE-------LRRAQEELDKFTDKLRRIQSSY----SALQRINQdLEDKIHR-NSQHHDDEKR--- 90
Cdd:PRK04778 296 DILEREVKA-RKYVEKNsdtlpdfLEHAKEQNKELKEEIDRVKQSYtlneSELESVRQ-LEKQLESlEKQYDEITERiae 373

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 113677306  91 ------ALSREIIVLNNHLMEAKMTIEKLREDNDLYRKDCNLAAQLLQcnksHYRAQLSE------------LPAEFQER 152
Cdd:PRK04778 374 qeiaysELQEELEEILKQLEEIEKEQEKLSEMLQGLRKDELEAREKLE----RYRNKLHEikryleksnlpgLPEDYLEM 449
 
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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