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Conserved domains on  [gi|10047205|dbj|BAB13396|]
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KIAA1570 protein, partial [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
DRWD-C_Knl1 cd22892
C-terminal double-RWD domain of kinetochore scaffold 1 and related proteins; Kinetochore ...
 1256-1354 3.75e-50

C-terminal double-RWD domain of kinetochore scaffold 1 and related proteins; Kinetochore scaffold 1 (KNL1 or Knl1, also known as Spc105, Spc7, and Blinkin) coordinates the spindle assembly checkpoint (SAC), a signaling pathway that delays chromosome segregation until all sister chromatids are properly attached to spindle microtubules (MTs). Knl1 is part of the KMN network, a conserved kinetochore protein complex that connects kinetochores to MTs. Knl1 has been shown to play an effective role in decreasing apoptosis and promoting the proliferation of colorectal cancer cells, suggesting that its inhibition may represent a promising therapeutic approach for colorectal cancer patients. Knl1 contains tandem RWD domains, also known as a double-RWD domain, DRWD, which has been shown to bind the Mis12 complex, consisting of Dsn1 and Nsl1, that tethers directly onto the underlying chromatin layer and mediates kinetochore targeting of Knl1. The model corresponds to the C-terminal double-RWD domain (DRWD-C).


:

Pssm-ID: 467644  Cd Length: 99  Bit Score: 172.18  E-value: 3.75e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1256 LLGEEIEYLKRWGPNYNLMNIDINNNELRLLFSSSAAFAKFEITLFLSAYYPSVPLPSTIQNHVGNTSQDDIATILSKVP 1335
Cdd:cd22892    1 LLGEEIEYLKRWGGKYNILKIDINDTNVHLLFSSSAAFAKFEITLSLTSGYPSVPLPFTFENHIGNTSQDQIEEVISKVP 80

                         90
                 ....*....|....*....
gi 10047205 1336 LENNYLKNVVKQIYQDLFQ 1354
Cdd:cd22892   81 PGKNYLKRVVKKIHQDLLQ 99
DRWD-N_Knl1 cd22817
N-terminal double-RWD domain of kinetochore scaffold 1 and related proteins; Kinetochore ...
 1142-1249 4.44e-45

N-terminal double-RWD domain of kinetochore scaffold 1 and related proteins; Kinetochore scaffold 1 (KNL1 or Knl1, also known as Spc105, Spc7, and Blinkin) coordinates the spindle assembly checkpoint (SAC), a signaling pathway that delays chromosome segregation until all sister chromatids are properly attached to spindle microtubules (MTs). Knl1 is part of the KMN network, a conserved kinetochore protein complex that connects kinetochores to MTs. Knl1 has been shown to play an effective role in decreasing apoptosis and promoting the proliferation of colorectal cancer cells, suggesting that its inhibition may represent a promising therapeutic approach for colorectal cancer patients. Knl1 contains tandem RWD domains, also known as a double-RWD domain, DRWD, which has been shown to bind the Mis12 complex, consisting of Dsn1 and Nsl1, that tethers directly onto the underlying chromatin layer and mediates kinetochore targeting of Knl1. The model corresponds to N-terminal double-RWD domain (DRWD-N).


:

Pssm-ID: 467642  Cd Length: 112  Bit Score: 158.21  E-value: 4.44e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1142 EELLDQL-SLSEWDVVEWSDDQAVFTFVYDTIQLTITFEESVVGFPFlDKRYRKIVDVNFQSLLDEDQAPPSSLLVHKLI 1220
Cdd:cd22817    5 ESHLELLnSLSEWRLEEWDENQAVFTFLYDSLELEVKFEDSKDGTAF-EKPERKIVDISFQSLLDEEKAPPSARLVHKLI 83

                         90       100
                 ....*....|....*....|....*....
gi 10047205 1221 FQYVEEKESWKKTCTTQHQLPKMLEEFSL 1249
Cdd:cd22817   84 FQFIESKESWKETYPTQRDLPKLLHDVSL 112
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1043-1152 5.41e-07

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


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 53.61  E-value: 5.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1043 QSAQNEREKLQIKIDEMDKILKKIDNCLTEMETETKNLEDE--EKNNPVEEWDSEMRAAEKELEQLKTEEEELQRnllEL 1120
Cdd:COG4942   23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiaALARRIRALEQELAALEAELAELEKEIAELRA---EL 99

                         90       100       110
                 ....*....|....*....|....*....|....
gi 10047205 1121 EVQKEQTLAQIDFMQK--QRNRTEELLDQLSLSE 1152
Cdd:COG4942  100 EAQKEELAELLRALYRlgRQPPLALLLSPEDFLD 133
MELT pfam19221
MELT motif; The outer kinetochore protein scaffold KNL1 is essential for error-free chromosome ...
 115-140 3.44e-06

MELT motif; The outer kinetochore protein scaffold KNL1 is essential for error-free chromosome segregation during mitosis and meiosis. A critical feature of KNL1 is an array of repeats containing MELT-like motifs. When phosphorylated, these motifs form docking sites for the BUB1-BUB3 dimer that regulates chromosome biorientation and the spindle assembly checkpoint. This entry mainly represents vertebrate proteins although MELT motifs are found much more widely.


:

Pssm-ID: 466004  Cd Length: 25  Bit Score: 44.73  E-value: 3.44e-06
                           10        20
                   ....*....|....*....|....*.
gi 10047205    115 KNDKTIVFSENHkNDMDITQSCMVEI 140
Cdd:pfam19221    1 PGDKTVVFSSDA-NDMDITKSHTVNI 25
MELT pfam19221
MELT motif; The outer kinetochore protein scaffold KNL1 is essential for error-free chromosome ...
 194-218 3.22e-04

MELT motif; The outer kinetochore protein scaffold KNL1 is essential for error-free chromosome segregation during mitosis and meiosis. A critical feature of KNL1 is an array of repeats containing MELT-like motifs. When phosphorylated, these motifs form docking sites for the BUB1-BUB3 dimer that regulates chromosome biorientation and the spindle assembly checkpoint. This entry mainly represents vertebrate proteins although MELT motifs are found much more widely.


:

Pssm-ID: 466004  Cd Length: 25  Bit Score: 38.96  E-value: 3.22e-04
                           10        20
                   ....*....|....*....|....*
gi 10047205    194 PMDKTVLFTDNYSDLEVTDSHTVFI 218
Cdd:pfam19221    1 PGDKTVVFSSDANDMDITKSHTVNI 25
MELT pfam19221
MELT motif; The outer kinetochore protein scaffold KNL1 is essential for error-free chromosome ...
 159-180 6.65e-04

MELT motif; The outer kinetochore protein scaffold KNL1 is essential for error-free chromosome segregation during mitosis and meiosis. A critical feature of KNL1 is an array of repeats containing MELT-like motifs. When phosphorylated, these motifs form docking sites for the BUB1-BUB3 dimer that regulates chromosome biorientation and the spindle assembly checkpoint. This entry mainly represents vertebrate proteins although MELT motifs are found much more widely.


:

Pssm-ID: 466004  Cd Length: 25  Bit Score: 38.19  E-value: 6.65e-04
                           10        20
                   ....*....|....*....|..
gi 10047205    159 KTILYSCGQDDMEITRSHTTAL 180
Cdd:pfam19221    4 KTVVFSSDANDMDITKSHTVNI 25
 
Name Accession Description Interval E-value
DRWD-C_Knl1 cd22892
C-terminal double-RWD domain of kinetochore scaffold 1 and related proteins; Kinetochore ...
 1256-1354 3.75e-50

C-terminal double-RWD domain of kinetochore scaffold 1 and related proteins; Kinetochore scaffold 1 (KNL1 or Knl1, also known as Spc105, Spc7, and Blinkin) coordinates the spindle assembly checkpoint (SAC), a signaling pathway that delays chromosome segregation until all sister chromatids are properly attached to spindle microtubules (MTs). Knl1 is part of the KMN network, a conserved kinetochore protein complex that connects kinetochores to MTs. Knl1 has been shown to play an effective role in decreasing apoptosis and promoting the proliferation of colorectal cancer cells, suggesting that its inhibition may represent a promising therapeutic approach for colorectal cancer patients. Knl1 contains tandem RWD domains, also known as a double-RWD domain, DRWD, which has been shown to bind the Mis12 complex, consisting of Dsn1 and Nsl1, that tethers directly onto the underlying chromatin layer and mediates kinetochore targeting of Knl1. The model corresponds to the C-terminal double-RWD domain (DRWD-C).


Pssm-ID: 467644  Cd Length: 99  Bit Score: 172.18  E-value: 3.75e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1256 LLGEEIEYLKRWGPNYNLMNIDINNNELRLLFSSSAAFAKFEITLFLSAYYPSVPLPSTIQNHVGNTSQDDIATILSKVP 1335
Cdd:cd22892    1 LLGEEIEYLKRWGGKYNILKIDINDTNVHLLFSSSAAFAKFEITLSLTSGYPSVPLPFTFENHIGNTSQDQIEEVISKVP 80

                         90
                 ....*....|....*....
gi 10047205 1336 LENNYLKNVVKQIYQDLFQ 1354
Cdd:cd22892   81 PGKNYLKRVVKKIHQDLLQ 99
DRWD-N_Knl1 cd22817
N-terminal double-RWD domain of kinetochore scaffold 1 and related proteins; Kinetochore ...
 1142-1249 4.44e-45

N-terminal double-RWD domain of kinetochore scaffold 1 and related proteins; Kinetochore scaffold 1 (KNL1 or Knl1, also known as Spc105, Spc7, and Blinkin) coordinates the spindle assembly checkpoint (SAC), a signaling pathway that delays chromosome segregation until all sister chromatids are properly attached to spindle microtubules (MTs). Knl1 is part of the KMN network, a conserved kinetochore protein complex that connects kinetochores to MTs. Knl1 has been shown to play an effective role in decreasing apoptosis and promoting the proliferation of colorectal cancer cells, suggesting that its inhibition may represent a promising therapeutic approach for colorectal cancer patients. Knl1 contains tandem RWD domains, also known as a double-RWD domain, DRWD, which has been shown to bind the Mis12 complex, consisting of Dsn1 and Nsl1, that tethers directly onto the underlying chromatin layer and mediates kinetochore targeting of Knl1. The model corresponds to N-terminal double-RWD domain (DRWD-N).


Pssm-ID: 467642  Cd Length: 112  Bit Score: 158.21  E-value: 4.44e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1142 EELLDQL-SLSEWDVVEWSDDQAVFTFVYDTIQLTITFEESVVGFPFlDKRYRKIVDVNFQSLLDEDQAPPSSLLVHKLI 1220
Cdd:cd22817    5 ESHLELLnSLSEWRLEEWDENQAVFTFLYDSLELEVKFEDSKDGTAF-EKPERKIVDISFQSLLDEEKAPPSARLVHKLI 83

                         90       100
                 ....*....|....*....|....*....
gi 10047205 1221 FQYVEEKESWKKTCTTQHQLPKMLEEFSL 1249
Cdd:cd22817   84 FQFIESKESWKETYPTQRDLPKLLHDVSL 112
Knl1_RWD_C pfam18210
Knl1 RWD C-terminal domain; This domain is found in Knl1, a sub-unit of the KMN network, ...
 1105-1258 9.17e-37

Knl1 RWD C-terminal domain; This domain is found in Knl1, a sub-unit of the KMN network, present in Homo sapiens. The KMN network is the core of the outer kinetochore which is responsible for microtubule binding/stabilization and controls the spindle assembly checkpoint. This domain is the second of two RING finger, WD repeat, DEAD-like helicase (RWD) domains. The tandem RWD domains mediate kinetochore targeting of the microtubule-binding subunits by interacting with the Mis12 complex. The Mis12 complex is a KMN sub-complex that tethers directly onto the underlying chromatin layer.


Pssm-ID: 465680 [Multi-domain]  Cd Length: 152  Bit Score: 136.04  E-value: 9.17e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205   1105 QLKTEEEELQRNLLELEVQKEQTLAQIDFMQKQRN---------RTEELLDQL-SLSEWDVVEWSDDQAVFTFVYDtIQL 1174
Cdd:pfam18210    1 ELKEELEELEEKLEELEERKQELLAAIGEAERIREecwtseevlRLKEELEALeSLHGWRITEVSDDTLVFTYLSD-IEL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205   1175 TITFEESvvgfpfldkryRKIVDVNFQSLLDEDQAPPSSLLVHKLIFQYVEEKESWKKTCTTQHQLPKMLEEFSLVVHHC 1254
Cdd:pfam18210   80 TFDFGAS-----------PKISSIDLESYLDDEKAPPSSLLVHRLAFFFLQSARDWVRKYPTQTSLPKLLQDVSLVWSRC 148


                   ....
gi 10047205   1255 RLLG 1258
Cdd:pfam18210  149 RLLG 152
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1043-1152 5.41e-07

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: 53.61  E-value: 5.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1043 QSAQNEREKLQIKIDEMDKILKKIDNCLTEMETETKNLEDE--EKNNPVEEWDSEMRAAEKELEQLKTEEEELQRnllEL 1120
Cdd:COG4942   23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiaALARRIRALEQELAALEAELAELEKEIAELRA---EL 99

                         90       100       110
                 ....*....|....*....|....*....|....
gi 10047205 1121 EVQKEQTLAQIDFMQK--QRNRTEELLDQLSLSE 1152
Cdd:COG4942  100 EAQKEELAELLRALYRlgRQPPLALLLSPEDFLD 133
MELT pfam19221
MELT motif; The outer kinetochore protein scaffold KNL1 is essential for error-free chromosome ...
 115-140 3.44e-06

MELT motif; The outer kinetochore protein scaffold KNL1 is essential for error-free chromosome segregation during mitosis and meiosis. A critical feature of KNL1 is an array of repeats containing MELT-like motifs. When phosphorylated, these motifs form docking sites for the BUB1-BUB3 dimer that regulates chromosome biorientation and the spindle assembly checkpoint. This entry mainly represents vertebrate proteins although MELT motifs are found much more widely.


Pssm-ID: 466004  Cd Length: 25  Bit Score: 44.73  E-value: 3.44e-06
                           10        20
                   ....*....|....*....|....*.
gi 10047205    115 KNDKTIVFSENHkNDMDITQSCMVEI 140
Cdd:pfam19221    1 PGDKTVVFSSDA-NDMDITKSHTVNI 25
APG6_N pfam17675
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
 1067-1153 7.52e-05

Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.


Pssm-ID: 465452 [Multi-domain]  Cd Length: 127  Bit Score: 43.74  E-value: 7.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205   1067 DNCLTEMETETKNLEDEEK------NNPVEEWDSEMRAAEKELEQLKTEEEELQRNLLELEVQKEQTLAQIDFMQKQrnr 1140
Cdd:pfam17675    8 DLLLEELDKQLEDAEKERDayisflKKLEKETPEELEELEKELEKLEKEEEELLQELEELEKEREELDAELEALEEE--- 84

                           90
                   ....*....|...
gi 10047205   1141 tEELLDQLSLSEW 1153
Cdd:pfam17675   85 -LEALDEEEEEFW 96
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1034-1148 7.85e-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: 47.36  E-value: 7.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205   1034 KVALYGKLVQSAQNEREKLQIKIDEMDKILKKIDNCLTEMETEtknledeeknnpVEEWDSEMRAAEKELEQLKTEEEEL 1113
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEK------------LEELRLEVSELEEEIEELQKELYAL 293

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 10047205   1114 QRNLLELEVQKEQTLAQIDFMQKQRNRTEELLDQL 1148
Cdd:TIGR02168  294 ANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
MELT pfam19221
MELT motif; The outer kinetochore protein scaffold KNL1 is essential for error-free chromosome ...
 194-218 3.22e-04

MELT motif; The outer kinetochore protein scaffold KNL1 is essential for error-free chromosome segregation during mitosis and meiosis. A critical feature of KNL1 is an array of repeats containing MELT-like motifs. When phosphorylated, these motifs form docking sites for the BUB1-BUB3 dimer that regulates chromosome biorientation and the spindle assembly checkpoint. This entry mainly represents vertebrate proteins although MELT motifs are found much more widely.


Pssm-ID: 466004  Cd Length: 25  Bit Score: 38.96  E-value: 3.22e-04
                           10        20
                   ....*....|....*....|....*
gi 10047205    194 PMDKTVLFTDNYSDLEVTDSHTVFI 218
Cdd:pfam19221    1 PGDKTVVFSSDANDMDITKSHTVNI 25
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1040-1144 5.19e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 5.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205  1040 KLVQSAQNEREKLQIKIDEMDKILKKIDNCLTEMETETKNLEDEEKNNPVEEWDSEMRAAEKELEQLKTEEEELQRNLLE 1119
Cdd:PRK03918  619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698

                          90       100
                  ....*....|....*....|....*...
gi 10047205  1120 LEVQKE---QTLAQIDFMQKQRNRTEEL 1144
Cdd:PRK03918  699 LKEELEereKAKKELEKLEKALERVEEL 726
MELT pfam19221
MELT motif; The outer kinetochore protein scaffold KNL1 is essential for error-free chromosome ...
 159-180 6.65e-04

MELT motif; The outer kinetochore protein scaffold KNL1 is essential for error-free chromosome segregation during mitosis and meiosis. A critical feature of KNL1 is an array of repeats containing MELT-like motifs. When phosphorylated, these motifs form docking sites for the BUB1-BUB3 dimer that regulates chromosome biorientation and the spindle assembly checkpoint. This entry mainly represents vertebrate proteins although MELT motifs are found much more widely.


Pssm-ID: 466004  Cd Length: 25  Bit Score: 38.19  E-value: 6.65e-04
                           10        20
                   ....*....|....*....|..
gi 10047205    159 KTILYSCGQDDMEITRSHTTAL 180
Cdd:pfam19221    4 KTVVFSSDANDMDITKSHTVNI 25
 
Name Accession Description Interval E-value
DRWD-C_Knl1 cd22892
C-terminal double-RWD domain of kinetochore scaffold 1 and related proteins; Kinetochore ...
 1256-1354 3.75e-50

C-terminal double-RWD domain of kinetochore scaffold 1 and related proteins; Kinetochore scaffold 1 (KNL1 or Knl1, also known as Spc105, Spc7, and Blinkin) coordinates the spindle assembly checkpoint (SAC), a signaling pathway that delays chromosome segregation until all sister chromatids are properly attached to spindle microtubules (MTs). Knl1 is part of the KMN network, a conserved kinetochore protein complex that connects kinetochores to MTs. Knl1 has been shown to play an effective role in decreasing apoptosis and promoting the proliferation of colorectal cancer cells, suggesting that its inhibition may represent a promising therapeutic approach for colorectal cancer patients. Knl1 contains tandem RWD domains, also known as a double-RWD domain, DRWD, which has been shown to bind the Mis12 complex, consisting of Dsn1 and Nsl1, that tethers directly onto the underlying chromatin layer and mediates kinetochore targeting of Knl1. The model corresponds to the C-terminal double-RWD domain (DRWD-C).


Pssm-ID: 467644  Cd Length: 99  Bit Score: 172.18  E-value: 3.75e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1256 LLGEEIEYLKRWGPNYNLMNIDINNNELRLLFSSSAAFAKFEITLFLSAYYPSVPLPSTIQNHVGNTSQDDIATILSKVP 1335
Cdd:cd22892    1 LLGEEIEYLKRWGGKYNILKIDINDTNVHLLFSSSAAFAKFEITLSLTSGYPSVPLPFTFENHIGNTSQDQIEEVISKVP 80

                         90
                 ....*....|....*....
gi 10047205 1336 LENNYLKNVVKQIYQDLFQ 1354
Cdd:cd22892   81 PGKNYLKRVVKKIHQDLLQ 99
DRWD-N_Knl1 cd22817
N-terminal double-RWD domain of kinetochore scaffold 1 and related proteins; Kinetochore ...
 1142-1249 4.44e-45

N-terminal double-RWD domain of kinetochore scaffold 1 and related proteins; Kinetochore scaffold 1 (KNL1 or Knl1, also known as Spc105, Spc7, and Blinkin) coordinates the spindle assembly checkpoint (SAC), a signaling pathway that delays chromosome segregation until all sister chromatids are properly attached to spindle microtubules (MTs). Knl1 is part of the KMN network, a conserved kinetochore protein complex that connects kinetochores to MTs. Knl1 has been shown to play an effective role in decreasing apoptosis and promoting the proliferation of colorectal cancer cells, suggesting that its inhibition may represent a promising therapeutic approach for colorectal cancer patients. Knl1 contains tandem RWD domains, also known as a double-RWD domain, DRWD, which has been shown to bind the Mis12 complex, consisting of Dsn1 and Nsl1, that tethers directly onto the underlying chromatin layer and mediates kinetochore targeting of Knl1. The model corresponds to N-terminal double-RWD domain (DRWD-N).


Pssm-ID: 467642  Cd Length: 112  Bit Score: 158.21  E-value: 4.44e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1142 EELLDQL-SLSEWDVVEWSDDQAVFTFVYDTIQLTITFEESVVGFPFlDKRYRKIVDVNFQSLLDEDQAPPSSLLVHKLI 1220
Cdd:cd22817    5 ESHLELLnSLSEWRLEEWDENQAVFTFLYDSLELEVKFEDSKDGTAF-EKPERKIVDISFQSLLDEEKAPPSARLVHKLI 83

                         90       100
                 ....*....|....*....|....*....
gi 10047205 1221 FQYVEEKESWKKTCTTQHQLPKMLEEFSL 1249
Cdd:cd22817   84 FQFIESKESWKETYPTQRDLPKLLHDVSL 112
Knl1_RWD_C pfam18210
Knl1 RWD C-terminal domain; This domain is found in Knl1, a sub-unit of the KMN network, ...
 1105-1258 9.17e-37

Knl1 RWD C-terminal domain; This domain is found in Knl1, a sub-unit of the KMN network, present in Homo sapiens. The KMN network is the core of the outer kinetochore which is responsible for microtubule binding/stabilization and controls the spindle assembly checkpoint. This domain is the second of two RING finger, WD repeat, DEAD-like helicase (RWD) domains. The tandem RWD domains mediate kinetochore targeting of the microtubule-binding subunits by interacting with the Mis12 complex. The Mis12 complex is a KMN sub-complex that tethers directly onto the underlying chromatin layer.


Pssm-ID: 465680 [Multi-domain]  Cd Length: 152  Bit Score: 136.04  E-value: 9.17e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205   1105 QLKTEEEELQRNLLELEVQKEQTLAQIDFMQKQRN---------RTEELLDQL-SLSEWDVVEWSDDQAVFTFVYDtIQL 1174
Cdd:pfam18210    1 ELKEELEELEEKLEELEERKQELLAAIGEAERIREecwtseevlRLKEELEALeSLHGWRITEVSDDTLVFTYLSD-IEL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205   1175 TITFEESvvgfpfldkryRKIVDVNFQSLLDEDQAPPSSLLVHKLIFQYVEEKESWKKTCTTQHQLPKMLEEFSLVVHHC 1254
Cdd:pfam18210   80 TFDFGAS-----------PKISSIDLESYLDDEKAPPSSLLVHRLAFFFLQSARDWVRKYPTQTSLPKLLQDVSLVWSRC 148


                   ....
gi 10047205   1255 RLLG 1258
Cdd:pfam18210  149 RLLG 152
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 1043-1152 5.41e-07

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: 53.61  E-value: 5.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1043 QSAQNEREKLQIKIDEMDKILKKIDNCLTEMETETKNLEDE--EKNNPVEEWDSEMRAAEKELEQLKTEEEELQRnllEL 1120
Cdd:COG4942   23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiaALARRIRALEQELAALEAELAELEKEIAELRA---EL 99

                         90       100       110
                 ....*....|....*....|....*....|....
gi 10047205 1121 EVQKEQTLAQIDFMQK--QRNRTEELLDQLSLSE 1152
Cdd:COG4942  100 EAQKEELAELLRALYRlgRQPPLALLLSPEDFLD 133
MELT pfam19221
MELT motif; The outer kinetochore protein scaffold KNL1 is essential for error-free chromosome ...
 115-140 3.44e-06

MELT motif; The outer kinetochore protein scaffold KNL1 is essential for error-free chromosome segregation during mitosis and meiosis. A critical feature of KNL1 is an array of repeats containing MELT-like motifs. When phosphorylated, these motifs form docking sites for the BUB1-BUB3 dimer that regulates chromosome biorientation and the spindle assembly checkpoint. This entry mainly represents vertebrate proteins although MELT motifs are found much more widely.


Pssm-ID: 466004  Cd Length: 25  Bit Score: 44.73  E-value: 3.44e-06
                           10        20
                   ....*....|....*....|....*.
gi 10047205    115 KNDKTIVFSENHkNDMDITQSCMVEI 140
Cdd:pfam19221    1 PGDKTVVFSSDA-NDMDITKSHTVNI 25
APG6_N pfam17675
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
 1067-1153 7.52e-05

Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.


Pssm-ID: 465452 [Multi-domain]  Cd Length: 127  Bit Score: 43.74  E-value: 7.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205   1067 DNCLTEMETETKNLEDEEK------NNPVEEWDSEMRAAEKELEQLKTEEEELQRNLLELEVQKEQTLAQIDFMQKQrnr 1140
Cdd:pfam17675    8 DLLLEELDKQLEDAEKERDayisflKKLEKETPEELEELEKELEKLEKEEEELLQELEELEKEREELDAELEALEEE--- 84

                           90
                   ....*....|...
gi 10047205   1141 tEELLDQLSLSEW 1153
Cdd:pfam17675   85 -LEALDEEEEEFW 96
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1034-1148 7.85e-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: 47.36  E-value: 7.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205   1034 KVALYGKLVQSAQNEREKLQIKIDEMDKILKKIDNCLTEMETEtknledeeknnpVEEWDSEMRAAEKELEQLKTEEEEL 1113
Cdd:TIGR02168  226 ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEK------------LEELRLEVSELEEEIEELQKELYAL 293

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 10047205   1114 QRNLLELEVQKEQTLAQIDFMQKQRNRTEELLDQL 1148
Cdd:TIGR02168  294 ANEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 1040-1148 7.99e-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: 45.69  E-value: 7.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1040 KLVQSAQNEREKLQIKIDEMDKILKKIDNCLTEMETETKNLED---EEKNNpveewdSEMRAAEKELEQLKTEEEELQRN 1116
Cdd:COG1579   38 DELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEqlgNVRNN------KEYEALQKEIESLKRRISDLEDE 111

                         90       100       110
                 ....*....|....*....|....*....|..
gi 10047205 1117 LLELEVQKEQTLAQIDFMQKQRNRTEELLDQL 1148
Cdd:COG1579  112 ILELMERIEELEEELAELEAELAELEAELEEK 143
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1034-1148 9.10e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 9.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1034 KVALYGKLVQSAQNEREKLQIKIDEMDKILKKIDNCLTEMETE---------TKNLEDEEKNNPVEEWDSEMRAAEKELE 1104
Cdd:COG1196  226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAEleelrleleELELELEEAQAEEYELLAELARLEQDIA 305

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 10047205 1105 QLKTEEEELQRNLLELEVQKEQTLAQIDFMQKQRNRTEELLDQL 1148
Cdd:COG1196  306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1043-1148 1.56e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 1.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1043 QSAQNEREKLQIKIDEMDKILKKIDNCLTEMETETKNLEDEEknnpvEEWDSEMRAAEKELEQLKTEEEELQRNLLELEV 1122
Cdd:COG4372   69 EQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA-----EELQEELEELQKERQDLEQQRKQLEAQIAELQS 143

                         90       100
                 ....*....|....*....|....*.
gi 10047205 1123 QKEQTLAQIDFMQKQRNRTEELLDQL 1148
Cdd:COG4372  144 EIAEREEELKELEEQLESLQEELAAL 169
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1042-1148 2.45e-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: 45.83  E-value: 2.45e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205   1042 VQSAQNEREKLQIKIDEMDKILKKIDNCLTEMETETKNLEDE--EKNNPVEEWDSEMRAAEKELEQLKTEEEELQRNLLE 1119
Cdd:TIGR02169  793 IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEiqELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872

                           90       100
                   ....*....|....*....|....*....
gi 10047205   1120 LEVQKEQTLAQIDFMQKQRNRTEELLDQL 1148
Cdd:TIGR02169  873 LEAALRDLESRLGDLKKERDELEAQLREL 901
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 960-1149 2.91e-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: 45.44  E-value: 2.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205    960 KIQIYREDCEARRQKIEELKLsasnqdklLVDINKNLWEKMRHCSDKELKAFGIYLNKIKSCFT-KMTKVFTHQGKVALY 1038
Cdd:TIGR02169  171 KKEKALEELEEVEENIERLDL--------IIDEKRQQLERLRREREKAERYQALLKEKREYEGYeLLKEKEALERQKEAI 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205   1039 GKLVQSAQNEREKLQIKIDEMDKILKKIDNCLTEMETETKNLEDEeknnpveewdsEMRAAEKELEQLKTEEEELQRNLL 1118
Cdd:TIGR02169  243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEE-----------EQLRVKEKIGELEAEIASLERSIA 311

                          170       180       190
                   ....*....|....*....|....*....|.
gi 10047205   1119 ELEVQKEQTLAQIDFMQKQRNRTEELLDQLS 1149
Cdd:TIGR02169  312 EKERELEDAEERLAKLEAEIDKLLAEIEELE 342
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 1045-1148 3.01e-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: 45.43  E-value: 3.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205   1045 AQNEREKLQIKIDEMDKILKKIDNCLTEMETETKNLED--EEKNNPVEEWDSEMRAAEKELEQLKTEEEELQRNLLELEV 1122
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKelEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761

                           90       100
                   ....*....|....*....|....*.
gi 10047205   1123 QKEQTLAQIDFMQKQRNRTEELLDQL 1148
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEEL 787
MELT pfam19221
MELT motif; The outer kinetochore protein scaffold KNL1 is essential for error-free chromosome ...
 194-218 3.22e-04

MELT motif; The outer kinetochore protein scaffold KNL1 is essential for error-free chromosome segregation during mitosis and meiosis. A critical feature of KNL1 is an array of repeats containing MELT-like motifs. When phosphorylated, these motifs form docking sites for the BUB1-BUB3 dimer that regulates chromosome biorientation and the spindle assembly checkpoint. This entry mainly represents vertebrate proteins although MELT motifs are found much more widely.


Pssm-ID: 466004  Cd Length: 25  Bit Score: 38.96  E-value: 3.22e-04
                           10        20
                   ....*....|....*....|....*
gi 10047205    194 PMDKTVLFTDNYSDLEVTDSHTVFI 218
Cdd:pfam19221    1 PGDKTVVFSSDANDMDITKSHTVNI 25
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1043-1152 3.35e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 3.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1043 QSAQNER-EKLQIKIDEMDK--ILKKIDNCLTEMETETKNLEDEEKNnpVEEWDSEMRAAEKELEQLKT-------EEEE 1112
Cdd:COG1196  208 QAEKAERyRELKEELKELEAelLLLKLRELEAELEELEAELEELEAE--LEELEAELAELEAELEELRLeleelelELEE 285

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 10047205 1113 LQRNLLELEVQKEQTLAQIDFMQKQRNRTEELLDQLSLSE 1152
Cdd:COG1196  286 AQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL 325
Nuf2_DHR10-like pfam18595
Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This ...
 1045-1143 3.37e-04

Nuf2, DHR10-like domain; This domain is found at the C-terminal region of Nuf2 proteins. This domain was identified as MazG related domain also designated as Designed helical repeat protein 10 (DHR10) that actually adopts a coiled-coil structure. Nuf2 is part of the Ndc80 complex, which binds to the spindle and is required for chromosome segregation and spindle checkpoint activity.


Pssm-ID: 465814 [Multi-domain]  Cd Length: 117  Bit Score: 41.80  E-value: 3.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205   1045 AQNERE--KLQIKIDEMDKILKKIDNCLTEMETETKNLEDEEKnnpveewdsemraAEKELEQLKTEEEELQRNLLELEV 1122
Cdd:pfam18595   12 AELERKarELQAKIDALQVVEKDLRSCIKLLEEIEAELAKLEE-------------AKKKLKELRDALEEKEIELRELER 78

                           90       100
                   ....*....|....*....|.
gi 10047205   1123 QKEQTLAQIDFMQKQRNRTEE 1143
Cdd:pfam18595   79 REERLQRQLENAQEKLERLRE 99
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 1032-1148 4.59e-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: 44.67  E-value: 4.59e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205   1032 QGKVALYGKLVQSAQNEREKLQIKIDEMDKILKKIDNCLTE-------METETKNLED---------EEKNNPVEEWDSE 1095
Cdd:TIGR02169  307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEerkrrdkLTEEYAELKEeledlraelEEVDKEFAETRDE 386

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 10047205   1096 MRAAEKELEQLKTEEEELQRNLLELEVQKEQTLAQIDFMQKQRNRTEELLDQL 1148
Cdd:TIGR02169  387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINEL 439
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1040-1144 5.19e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 5.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205  1040 KLVQSAQNEREKLQIKIDEMDKILKKIDNCLTEMETETKNLEDEEKNNPVEEWDSEMRAAEKELEQLKTEEEELQRNLLE 1119
Cdd:PRK03918  619 KELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEK 698

                          90       100
                  ....*....|....*....|....*...
gi 10047205  1120 LEVQKE---QTLAQIDFMQKQRNRTEEL 1144
Cdd:PRK03918  699 LKEELEereKAKKELEKLEKALERVEEL 726
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1050-1148 6.38e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 6.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1050 EKLQIKIDEMDKILKKIDNCLTEMETETKNLEDEEknnpveewdSEMRAAEKELEQLKTEEEELQRNLLELEVQKEQTLA 1129
Cdd:COG4372   31 EQLRKALFELDKLQEELEQLREELEQAREELEQLE---------EELEQARSELEQLEEELEELNEQLQAAQAELAQAQE 101

                         90
                 ....*....|....*....
gi 10047205 1130 QIDFMQKQRNRTEELLDQL 1148
Cdd:COG4372  102 ELESLQEEAEELQEELEEL 120
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1042-1148 6.38e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 43.74  E-value: 6.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1042 VQSAQNEREKLQIKIDEMDKILKKIDNCLTEMETE--TKNLEDEEKNNPVEEWDSEMRAAEKELEQLKTEEEELQRNLLE 1119
Cdd:COG4372   54 LEQAREELEQLEEELEQARSELEQLEEELEELNEQlqAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ 133

                         90       100
                 ....*....|....*....|....*....
gi 10047205 1120 LEVQKEQTLAQIDFMQKQRNRTEELLDQL 1148
Cdd:COG4372  134 LEAQIAELQSEIAEREEELKELEEQLESL 162
MELT pfam19221
MELT motif; The outer kinetochore protein scaffold KNL1 is essential for error-free chromosome ...
 159-180 6.65e-04

MELT motif; The outer kinetochore protein scaffold KNL1 is essential for error-free chromosome segregation during mitosis and meiosis. A critical feature of KNL1 is an array of repeats containing MELT-like motifs. When phosphorylated, these motifs form docking sites for the BUB1-BUB3 dimer that regulates chromosome biorientation and the spindle assembly checkpoint. This entry mainly represents vertebrate proteins although MELT motifs are found much more widely.


Pssm-ID: 466004  Cd Length: 25  Bit Score: 38.19  E-value: 6.65e-04
                           10        20
                   ....*....|....*....|..
gi 10047205    159 KTILYSCGQDDMEITRSHTTAL 180
Cdd:pfam19221    4 KTVVFSSDANDMDITKSHTVNI 25
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1040-1154 7.79e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 43.99  E-value: 7.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1040 KLVQSAQNEREKLQIKIDEMDKILKKIDNC---LTEMETETKNLEDEEKNNPVEEwdsEMRAAEKELEQLKTEEEELQRN 1116
Cdd:COG4717   78 EELKEAEEKEEEYAELQEELEELEEELEELeaeLEELREELEKLEKLLQLLPLYQ---ELEALEAELAELPERLEELEER 154

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 10047205 1117 LL---ELEVQKEQTLAQIdfmQKQRNRTEELLDQLSLSEWD 1154
Cdd:COG4717  155 LEelrELEEELEELEAEL---AELQEELEELLEQLSLATEE 192
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1032-1157 7.95e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 7.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1032 QGKVALYGKLVQSAQNEREKLQIKIDEMDKILKKIDNCLTEMET--ETKNLEDEEKNNPVEEWDSEMRAAEKELEQLKTE 1109
Cdd:COG1196  238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELelEEAQAEEYELLAELARLEQDIARLEERRRELEER 317

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 10047205 1110 EEELQRNLLELEVQKEQTLAQIDFMQKQRNRTEELLDQLSLSEWDVVE 1157
Cdd:COG1196  318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1034-1148 1.32e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1034 KVALYGKLVQSAQNEREKLQIKIDEMDKILKKIDN---------CLTEMETETKNLEDEeknnpVEEWDSEMRAAEK--- 1101
Cdd:COG4913  611 KLAALEAELAELEEELAEAEERLEALEAELDALQErrealqrlaEYSWDEIDVASAERE-----IAELEAELERLDAssd 685

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 10047205 1102 ELEQLKTEEEELQRNLLELEVQKEQTLAQIDFMQKQRNRTEELLDQL 1148
Cdd:COG4913  686 DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDEL 732
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
966-1152 1.42e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205   966 EDCEARRQKIEELKlsasnqdKLLVDINKNLWE-KMRHCSDKELKAFGIYLNKIKSCFTKMTKvfthqGKVALYGKLVQS 1044
Cdd:PRK03918  331 KELEEKEERLEELK-------KKLKELEKRLEElEERHELYEEAKAKKEELERLKKRLTGLTP-----EKLEKELEELEK 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205  1045 A----QNEREKLQIKIDEMDKILKKIDNCLTEMETET-------KNLEDEEKNNPVEEWDSEMRAAEKELEQLKTEEEEL 1113
Cdd:PRK03918  399 AkeeiEEEISKITARIGELKKEIKELKKAIEELKKAKgkcpvcgRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKL 478

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 10047205  1114 QRNLLELE--VQKEQTLAQIDFMQKQRNRTEELLDQLSLSE 1152
Cdd:PRK03918  479 RKELRELEkvLKKESELIKLKELAEQLKELEEKLKKYNLEE 519
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
1042-1148 1.97e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.59  E-value: 1.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1042 VQSAQNEREKLQIKIDEMDKILKKIDncLTEMETETKNLEDEeknnpVEEWDSEMRAAEKELEQLKTEEEELQRNLLELE 1121
Cdd:COG4913  257 IRELAERYAAARERLAELEYLRAALR--LWFAQRRLELLEAE-----LEELRAELARLEAELERLEARLDALREELDELE 329

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 10047205 1122 VQ--------KEQTLAQIDFMQKQRNRTEELLDQL 1148
Cdd:COG4913  330 AQirgnggdrLEQLEREIERLERELEERERRRARL 364
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 958-1149 2.32e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.36  E-value: 2.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205    958 RPKIQIYREDCEARRQKIEELKLSASNQDKLLVDINKNLWEKMRHCSDKELKAFGIYLNKIKSCFTKMTKVFTH------ 1031
Cdd:TIGR02169  743 EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREieqkln 822

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205   1032 --QGKVALYGKLVQSAQNEREKLQIKIDEMDKILKKIDNCLTEMETETKNLEDEeknnpVEEWDSEMRAAEKELEQLKTE 1109
Cdd:TIGR02169  823 rlTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAA-----LRDLESRLGDLKKERDELEAQ 897

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 10047205   1110 EEELQRNLLELEVQKEQTLAQIDFMQKQRnrtEELLDQLS 1149
Cdd:TIGR02169  898 LRELERKIEELEAQIEKKRKRLSELKAKL---EALEEELS 934
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 1059-1144 2.33e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 39.87  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205   1059 MDKILKKIDncltEMETETKNLEDEEKnnpveEWDSEMRAAEKELEQLkteEEELQRNLLELEVQKEQTLAQI-----DF 1133
Cdd:pfam03938    7 MQKILEESP----EGKAAQAQLEKKFK-----KRQAELEAKQKELQKL---YEELQKDGALLEEEREEKEQELqkkeqEL 74

                           90
                   ....*....|.
gi 10047205   1134 MQKQRNRTEEL 1144
Cdd:pfam03938   75 QQLQQKAQQEL 85
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1081-1148 2.34e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 2.34e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 10047205 1081 EDEEKNNPVEEWDSEMRAAEKELEQLKTEEEELQRNLLELEVQKEQTLAQIDFMQKQRNRTEELLDQL 1148
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEER 84
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1032-1152 2.35e-03

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: 2.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1032 QGKVALYGKLVQSAQNEREKLQIKIDEMDKILKKIDNCLTEMETETKNLEDEEknnpvEEWDSEMRAAEKELEQLKTEEE 1111
Cdd:COG1196  287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEEL-----EELEEELEEAEEELEEAEAELA 361

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 10047205 1112 ELQRNLLELEVQKEQTLAQID-----FMQKQRNRTEELLDQLSLSE 1152
Cdd:COG1196  362 EAEEALLEAEAELAEAEEELEelaeeLLEALRAAAELAAQLEELEE 407
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
1031-1156 3.07e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.77  E-value: 3.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1031 HQGKVALYGKLVQSAQNEREKLQIKIDEMDKILKKIDNCLTEMETETKnlEDEEKNNPVEEWDSEMRAAEKELEQLKTEE 1110
Cdd:COG2433  411 EEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEER--REIRKDREISRLDREIERLERELEEERERI 488

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 10047205 1111 EELQRNLLELEvqkeqTLAQIDFMQKQ----------RNRTEELLDQLSLSEWDVV 1156
Cdd:COG2433  489 EELKRKLERLK-----ELWKLEHSGELvpvkvvekftKEAIRRLEEEYGLKEGDVV 539
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 1051-1156 3.31e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.99  E-value: 3.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1051 KLQIKIDEMDKILKKIDNCLTEMETETKNLEDEEKNNPVE---EWDSEMRAAEKELEQLKT---EEEELQRNLLELEVQK 1124
Cdd:COG0542  401 RVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFErlaELRDELAELEEELEALKArweAEKELIEEIQELKEEL 480

                         90       100       110
                 ....*....|....*....|....*....|..
gi 10047205 1125 EQTLAQIDFMQKQRNRTEELLDQLSLSEWDVV 1156
Cdd:COG0542  481 EQRYGKIPELEKELAELEEELAELAPLLREEV 512
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1039-1148 3.58e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.68  E-value: 3.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1039 GKLVQSAQNEREKLQIKIDEMDKILKKIDNCLTEMETETKNLEDEEKNnpVEEWDSEMRAAEKELE--QLKTEEEELQRN 1116
Cdd:COG4717   63 GRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE--LEELREELEKLEKLLQllPLYQELEALEAE 140

                         90       100       110
                 ....*....|....*....|....*....|..
gi 10047205 1117 LLELEVQKEQTLAQIDFMQKQRNRTEELLDQL 1148
Cdd:COG4717  141 LAELPERLEELEERLEELRELEEELEELEAEL 172
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 1093-1148 3.79e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.35  E-value: 3.79e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 10047205 1093 DSEMRAAEKELEQLKTEEEELQRNLLELEVQKEQTLAQIDFMQKQRNRTEELLDQL 1148
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL 70
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1038-1148 4.52e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 4.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1038 YGKLVQSAQNEREKLQIKIDEMDKILKKIDNCLTEMETETKNLEDEeknnpVEEWDSEMRAAEKELEQLKTEEEELQRNL 1117
Cdd:COG4372    8 VGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREE-----LEQAREELEQLEEELEQARSELEQLEEEL 82

                         90       100       110
                 ....*....|....*....|....*....|.
gi 10047205 1118 LELEVQKEQTLAQIDFMQKQRNRTEELLDQL 1148
Cdd:COG4372   83 EELNEQLQAAQAELAQAQEELESLQEEAEEL 113
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1041-1144 5.47e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 5.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1041 LVQSAQNEREKLQIKIDEMDKILKKIDNcLTEMETETKNLE----------DEEKNNPVEEWDSEMRAAEKELEQLKTEE 1110
Cdd:COG4717  130 LYQELEALEAELAELPERLEELEERLEE-LRELEEELEELEaelaelqeelEELLEQLSLATEEELQDLAEELEELQQRL 208

                         90       100       110
                 ....*....|....*....|....*....|....
gi 10047205 1111 EELQRNLLELEVQKEQTLAQIDFMQKQRNRTEEL 1144
Cdd:COG4717  209 AELEEELEEAQEELEELEEELEQLENELEAAALE 242
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1017-1154 5.52e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 5.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1017 KIKSCFTKMTKVFTHQGKVALYGKLVQSAQNEREKLQIKIDEMDKIL---------KKIDNCLTEMETETKNLEDEEKnn 1087
Cdd:COG4717   79 ELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqllplyqelEALEAELAELPERLEELEERLE-- 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1088 PVEEWDSEMRAAEKELEQLKTEEEELQR---------------NLLELEVQKEQTLAQIDFMQKQRNRTEELLDQLSLSE 1152
Cdd:COG4717  157 ELRELEEELEELEAELAELQEELEELLEqlslateeelqdlaeELEELQQRLAELEEELEEAQEELEELEEELEQLENEL 236


                 ..
gi 10047205 1153 WD 1154
Cdd:COG4717  237 EA 238
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 1043-1148 7.00e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 7.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 10047205 1043 QSAQNEREKLQIKIDEMDKILKKIDNCLTEMETETKNLEDEEKNNpvEEWDSEMRAAEKELEQLKTEEEELQRNLLELEV 1122
Cdd:COG1196  281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL--AELEEELEELEEELEELEEELEEAEEELEEAEA 358

                         90       100
                 ....*....|....*....|....*.
gi 10047205 1123 QKEQTLAQIDFMQKQRNRTEELLDQL 1148
Cdd:COG1196  359 ELAEAEEALLEAEAELAEAEEELEEL 384
PilO COG3167
Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];
1095-1149 7.98e-03

Type IV pilus assembly protein PilO [Cell motility, Extracellular structures];


Pssm-ID: 442400 [Multi-domain]  Cd Length: 202  Bit Score: 39.16  E-value: 7.98e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 10047205 1095 EMRAAEKELEQLKTEEEELQR---NLLELEVQKEQTLAQIDFMQKQ---RNRTEELLDQLS 1149
Cdd:COG3167   47 ELEELEAEEAQLKQELEKKQAkaaNLPALKAQLEELEQQLGELLKQlpsKAEVPALLDDIS 107
 
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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