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Conserved domains on  [gi|386869306|ref|NP_001248322|]
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calcium-binding and coiled-coil domain-containing protein 2 isoform 4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SKICH pfam17751
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ...
 23-125 9.72e-46

SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The functions of the SKICH domains of NDP52 and CALCOCO1 are not known.


:

Pssm-ID: 465482  Cd Length: 102  Bit Score: 152.78  E-value: 9.72e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   23 VIFNSVEKFYIPGGDVTCHYTFTQHFIPRRKDWIGIFRVGWKTTREYYTFMWVtlPIDLNNKSAKQQEVQFKAYYLPKDD 102
Cdd:pfam17751   1 VVFQNVGEWYPPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWA--KDDEVEGSNSVRQVLFKASYLPKEP 78

                          90       100
                  ....*....|....*....|....
gi 386869306  103 -EYYQFCYVDEDGVVRGASIPFQF 125
Cdd:pfam17751  79 eGFYQFCYVSNLGSVVGISTPFQF 102
Zn-C2H2_CALCOCO2 cd21968
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ...
 378-404 1.15e-09

C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing protein 2 (CALCOCO2) and similar proteins; CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an Xenophagy-specific receptor required for autophagy-mediated intracellular bacteria degradation. It acts as an effector protein of galectin-sensed membrane damage that restricts the proliferation of infecting pathogens such as Salmonella typhimurium upon entry into the cytosol by targeting LGALS8-associated bacteria for autophagy. It may play a role in ruffle formation and actin cytoskeleton organization and seems to negatively regulate constitutive secretion. CALCOCO2 contains a C2H2-type zinc binding domain.


:

Pssm-ID: 412014  Cd Length: 27  Bit Score: 53.22  E-value: 1.15e-09
                         10        20
                 ....*....|....*....|....*..
gi 386869306 378 FNCPICDKIFPATEKQIFEDHVFCHSL 404
Cdd:cd21968    1 FECPICSKIFEATSKQEFEDHVFCHSL 27
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 138-299 6.42e-08

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: 54.00  E-value: 6.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 138 TQEELETLQSINKKLELKVKEQKDywetELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLE 217
Cdd:COG4942   81 LEAELAELEKEIAELRAELEAQKE----ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 218 QLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDEnfdLSKRLSENEIICNALQRQKERLEGENDLLK 297
Cdd:COG4942  157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLE 233


                 ..
gi 386869306 298 RE 299
Cdd:COG4942  234 AE 235
 
Name Accession Description Interval E-value
SKICH pfam17751
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ...
 23-125 9.72e-46

SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The functions of the SKICH domains of NDP52 and CALCOCO1 are not known.


Pssm-ID: 465482  Cd Length: 102  Bit Score: 152.78  E-value: 9.72e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   23 VIFNSVEKFYIPGGDVTCHYTFTQHFIPRRKDWIGIFRVGWKTTREYYTFMWVtlPIDLNNKSAKQQEVQFKAYYLPKDD 102
Cdd:pfam17751   1 VVFQNVGEWYPPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWA--KDDEVEGSNSVRQVLFKASYLPKEP 78

                          90       100
                  ....*....|....*....|....
gi 386869306  103 -EYYQFCYVDEDGVVRGASIPFQF 125
Cdd:pfam17751  79 eGFYQFCYVSNLGSVVGISTPFQF 102
Zn-C2H2_CALCOCO2 cd21968
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ...
 378-404 1.15e-09

C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing protein 2 (CALCOCO2) and similar proteins; CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an Xenophagy-specific receptor required for autophagy-mediated intracellular bacteria degradation. It acts as an effector protein of galectin-sensed membrane damage that restricts the proliferation of infecting pathogens such as Salmonella typhimurium upon entry into the cytosol by targeting LGALS8-associated bacteria for autophagy. It may play a role in ruffle formation and actin cytoskeleton organization and seems to negatively regulate constitutive secretion. CALCOCO2 contains a C2H2-type zinc binding domain.


Pssm-ID: 412014  Cd Length: 27  Bit Score: 53.22  E-value: 1.15e-09
                         10        20
                 ....*....|....*....|....*..
gi 386869306 378 FNCPICDKIFPATEKQIFEDHVFCHSL 404
Cdd:cd21968    1 FECPICSKIFEATSKQEFEDHVFCHSL 27
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 138-299 6.42e-08

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: 54.00  E-value: 6.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 138 TQEELETLQSINKKLELKVKEQKDywetELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLE 217
Cdd:COG4942   81 LEAELAELEKEIAELRAELEAQKE----ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 218 QLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDEnfdLSKRLSENEIICNALQRQKERLEGENDLLK 297
Cdd:COG4942  157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLE 233


                 ..
gi 386869306 298 RE 299
Cdd:COG4942  234 AE 235
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 128-305 1.72e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.52  E-value: 1.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   128 ENEEDILVVTTQEELETLQSINKKLELKVKEQkdywETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQ 207
Cdd:TIGR02168  255 LEELTAELQELEEKLEELRLEVSELEEEIEEL----QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   208 GDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKE 287
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410

                          170
                   ....*....|....*...
gi 386869306   288 RLEGENDLLKRENSRLLS 305
Cdd:TIGR02168  411 RLEDRRERLQQEIEELLK 428
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 155-263 4.38e-05

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 44.28  E-value: 4.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  155 KVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQ---AQLSTQEKEMEKLVQGDQDKT-EQLEQLKKENDHLFLSL 230
Cdd:pfam05010  12 KARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEktiAQMIEEKQKQKELEHAEIQKVlEEKDQALADLNSVEKSF 91

                          90       100       110
                  ....*....|....*....|....*....|...
gi 386869306  231 TEQRKDQKKLEQTVEQMKQNETTAMKKQQELMD 263
Cdd:pfam05010  92 SDLFKRYEKQKEVISGYKKNEESLKKCAQDYLA 124
PTZ00121 PTZ00121
MAEBL; Provisional
 111-299 8.73e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 8.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  111 DEDGVVRGASIPFQFRPENEEDILVVTTQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQ 190
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  191 LQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKleqtVEQMKQNETTAMKKQQELMDENfdlsk 270
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK----AEELKKKEAEEKKKAEELKKAE----- 1725

                         170       180
                  ....*....|....*....|....*....
gi 386869306  271 rlSENEIICNALQRQKERLEGENDLLKRE 299
Cdd:PTZ00121 1726 --EENKIKAEEAKKEAEEDKKKAEEAKKD 1752
Zn-C2H2_12 pfam18112
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ...
 380-402 5.62e-03

Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and coiled-coil domain 2/NDP25 (CALCOCO2/NDP25) found in Homo sapiens. CALCOCO2/NDP25 is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. This domain is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.


Pssm-ID: 407946  Cd Length: 27  Bit Score: 34.16  E-value: 5.62e-03
                          10        20
                  ....*....|....*....|....
gi 386869306  380 CPICDKIFPA-TEKQIFEDHVFCH 402
Cdd:pfam18112   3 CPLCGEMFSPnIDQSEFEEHVESH 26
 
Name Accession Description Interval E-value
SKICH pfam17751
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ...
 23-125 9.72e-46

SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The functions of the SKICH domains of NDP52 and CALCOCO1 are not known.


Pssm-ID: 465482  Cd Length: 102  Bit Score: 152.78  E-value: 9.72e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   23 VIFNSVEKFYIPGGDVTCHYTFTQHFIPRRKDWIGIFRVGWKTTREYYTFMWVtlPIDLNNKSAKQQEVQFKAYYLPKDD 102
Cdd:pfam17751   1 VVFQNVGEWYPPDEDIECSYTLTPDFTPSSWDWIGLFKVGWKSVNDYVTYVWA--KDDEVEGSNSVRQVLFKASYLPKEP 78

                          90       100
                  ....*....|....*....|....
gi 386869306  103 -EYYQFCYVDEDGVVRGASIPFQF 125
Cdd:pfam17751  79 eGFYQFCYVSNLGSVVGISTPFQF 102
Zn-C2H2_CALCOCO2 cd21968
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ...
 378-404 1.15e-09

C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing protein 2 (CALCOCO2) and similar proteins; CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an Xenophagy-specific receptor required for autophagy-mediated intracellular bacteria degradation. It acts as an effector protein of galectin-sensed membrane damage that restricts the proliferation of infecting pathogens such as Salmonella typhimurium upon entry into the cytosol by targeting LGALS8-associated bacteria for autophagy. It may play a role in ruffle formation and actin cytoskeleton organization and seems to negatively regulate constitutive secretion. CALCOCO2 contains a C2H2-type zinc binding domain.


Pssm-ID: 412014  Cd Length: 27  Bit Score: 53.22  E-value: 1.15e-09
                         10        20
                 ....*....|....*....|....*..
gi 386869306 378 FNCPICDKIFPATEKQIFEDHVFCHSL 404
Cdd:cd21968    1 FECPICSKIFEATSKQEFEDHVFCHSL 27
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 138-299 6.42e-08

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: 54.00  E-value: 6.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 138 TQEELETLQSINKKLELKVKEQKDywetELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLE 217
Cdd:COG4942   81 LEAELAELEKEIAELRAELEAQKE----ELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 218 QLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDEnfdLSKRLSENEIICNALQRQKERLEGENDLLK 297
Cdd:COG4942  157 ADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLE 233


                 ..
gi 386869306 298 RE 299
Cdd:COG4942  234 AE 235
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
180-311 1.48e-07

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 53.32  E-value: 1.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 180 ENEKMGIRVDQLQAQLSTQEKEMEKLvqgdqdkTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQ 259
Cdd:COG2433  393 EEPEAEREKEHEERELTEEEEEIRRL-------EEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDR 465

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 386869306 260 ELmdenfdlSKRlsENEIicNALQRQKERLEGENDLLKRENSRLLSYMGLDF 311
Cdd:COG2433  466 EI-------SRL--DREI--ERLERELEEERERIEELKRKLERLKELWKLEH 506
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 128-305 1.72e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.52  E-value: 1.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   128 ENEEDILVVTTQEELETLQSINKKLELKVKEQkdywETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQ 207
Cdd:TIGR02168  255 LEELTAELQELEEKLEELRLEVSELEEEIEEL----QKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   208 GDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKE 287
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410

                          170
                   ....*....|....*...
gi 386869306   288 RLEGENDLLKRENSRLLS 305
Cdd:TIGR02168  411 RLEDRRERLQQEIEELLK 428
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
139-303 2.00e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.38  E-value: 2.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  139 QEELETLQSINKKLElkvkEQKDYWETELLQLkeQNQKMSSENEkmgIRVDQLQAQLSTQEKEMEKLVQGDQD---KTEQ 215
Cdd:COG4913   623 EEELAEAEERLEALE----AELDALQERREAL--QRLAEYSWDE---IDVASAEREIAELEAELERLDASSDDlaaLEEQ 693

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  216 LEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDE-----NFDLSKRLsENEIICNALQRQKERLE 290
Cdd:COG4913   694 LEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarlelRALLEERF-AAALGDAVERELRENLE 772

                         170
                  ....*....|...
gi 386869306  291 GENDLLKRENSRL 303
Cdd:COG4913   773 ERIDALRARLNRA 785
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 139-303 2.50e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 2.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   139 QEELETLQSINKKLELKVKEQkdywETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQG-------DQD 211
Cdd:TIGR02168  683 EEKIEELEEKIAELEKALAEL----RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlskeLTE 758

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   212 KTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEG 291
Cdd:TIGR02168  759 LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838

                          170
                   ....*....|..
gi 386869306   292 ENDLLKRENSRL 303
Cdd:TIGR02168  839 RLEDLEEQIEEL 850
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 138-349 3.28e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 51.75  E-value: 3.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 138 TQEELETLQ----SINKKLElKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEM----------- 202
Cdd:COG3883   28 LQAELEAAQaeldALQAELE-ELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALyrsggsvsyld 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 203 ------------------EKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDe 264
Cdd:COG3883  107 vllgsesfsdfldrlsalSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLA- 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 265 nfdlskRLSENEiicNALQRQKERLEGENDLLKRENSRLLSYmGLDFNSLPYQVPTSDEGGARQNPGLAYGNPYSGIQES 344
Cdd:COG3883  186 ------QLSAEE---AAAEAQLAELEAELAAAEAAAAAAAAA-AAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAA 255


                 ....*
gi 386869306 345 SSPSP 349
Cdd:COG3883  256 GAAAG 260
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
139-303 5.02e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.44  E-value: 5.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 139 QEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQ 218
Cdd:COG4372   12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 219 LKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKR 298
Cdd:COG4372   92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171


                 ....*
gi 386869306 299 ENSRL 303
Cdd:COG4372  172 ELQAL 176
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 138-303 8.02e-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: 50.53  E-value: 8.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 138 TQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEkmgiRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLE 217
Cdd:COG4942   25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALAR----RIRALEQELAALEAELAELEKEIAELRAELE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 218 QLKKE---------------------------------------NDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQ 258
Cdd:COG4942  101 AQKEElaellralyrlgrqpplalllspedfldavrrlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALL 180

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 386869306 259 QELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 303
Cdd:COG4942  181 AELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
143-302 2.93e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 49.13  E-value: 2.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 143 ETLQSINKKLElKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKE 222
Cdd:COG4372   31 EQLRKALFELD-KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEE 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 223 NDHLFLSLTEQRKDQKKLEQTVEQMKQnettamkKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSR 302
Cdd:COG4372  110 AEELQEELEELQKERQDLEQQRKQLEA-------QIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE 182
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 139-304 9.25e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 9.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 139 QEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKM---GIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQ 215
Cdd:COG1196  266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRrelEERLEELEEELAELEEELEELEEELEELEEE 345

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 216 LEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDL 295
Cdd:COG1196  346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEE 425


                 ....*....
gi 386869306 296 LKRENSRLL 304
Cdd:COG1196  426 LEEALAELE 434
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 146-299 1.12e-05

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 47.71  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  146 QSINKKLELKVKEQKDYWETELLQLKEQNQKMSS--------ENEKMGIRVD--QLQAQLSTQEKEMEKLVQGDQDKTEQ 215
Cdd:TIGR04523 306 QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQlneqisqlKKELTNSESEnsEKQRELEEKQNEIEKLKKENQSYKQE 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  216 LEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENF-------DLSKRLSENEIICNALQRQKER 288
Cdd:TIGR04523 386 IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIknnseikDLTNQDSVKELIIKNLDNTRES 465

                         170
                  ....*....|.
gi 386869306  289 LEGENDLLKRE 299
Cdd:TIGR04523 466 LETQLKVLSRS 476
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 139-305 1.16e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 139 QEELETLQSINKKLELK-VKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLE 217
Cdd:COG1196  219 KEELKELEAELLLLKLReLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELA 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 218 QLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEiicNALQRQKERLEGENDLLK 297
Cdd:COG1196  299 RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE---AELAEAEEALLEAEAELA 375


                 ....*...
gi 386869306 298 RENSRLLS 305
Cdd:COG1196  376 EAEEELEE 383
Zn-C2H2_CALCOCO1_TAX1BP1_like cd21965
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ...
 380-402 1.17e-05

autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil domain-containing proteins, TAX1BP1 and similar proteins; The family includes calcium-binding and coiled-coil domain-containing proteins (CALCOCO1 and CALCOCO2), TAX1BP1 and similar proteins. CALCOCO1, also called calphoglin, or coiled-coil coactivator protein, or Sarcoma antigen NY-SAR-3, functions as a coactivator for aryl hydrocarbon and nuclear receptors (NR). CALCOCO2, also called antigen nuclear dot 52 kDa protein, or nuclear domain 10 protein NDP52, or nuclear domain 10 protein 52, or nuclear dot protein 52, is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. TAX1BP1, also called TRAF6-binding protein (T6BP), is a novel ubiquitin-binding adaptor protein involved in the negative regulation of the NF-kappaB transcription factor, a key player in inflammatory responses, immunity and tumorigenesis. The family also includes Drosophila melanogaster Spindle-F (Spn-F) that is the central mediator of IK2 kinase-dependent dendrite pruning in drosophila sensory neurons. This model corresponds to the C2H2-type zinc binding domain found in family members. It is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.


Pssm-ID: 412012  Cd Length: 24  Bit Score: 41.79  E-value: 1.17e-05
                         10        20
                 ....*....|....*....|....
gi 386869306 380 CPICDKIFPATEKQ-IFEDHVFCH 402
Cdd:cd21965    1 CPICNKQFPPQVDQeAFEDHVESH 24
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 128-304 1.73e-05

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: 46.98  E-value: 1.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   128 ENEEDILVVTTQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSEnekmgirVDQLQAQLSTQEKEMEKLVQ 207
Cdd:TIGR02169  250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAE-------IASLERSIAEKERELEDAEE 322

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   208 GDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEqtvEQMKQNETTAMKKQQELMDEnfdlSKRLSENEIICNALQRQKE 287
Cdd:TIGR02169  323 RLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT---EEYAELKEELEDLRAELEEV----DKEFAETRDELKDYREKLE 395

                          170
                   ....*....|....*..
gi 386869306   288 RLEGENDLLKRENSRLL 304
Cdd:TIGR02169  396 KLKREINELKRELDRLQ 412
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
135-303 2.32e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 2.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  135 VVTTQEELETLQSINKKLE--LKVKEQKD----------YW--ETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEK 200
Cdd:COG4913   244 LEDAREQIELLEPIRELAEryAAARERLAeleylraalrLWfaQRRLELLEAELEELRAELARLEAELERLEARLDALRE 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  201 EMEKL-VQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMK-------------QNETTAMK-----KQQEL 261
Cdd:COG4913   324 ELDELeAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGlplpasaeefaalRAEAAALLealeeELEAL 403

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 386869306  262 MDENFDLSKRLSEneiicnaLQRQKERLEGENDLLKRENSRL 303
Cdd:COG4913   404 EEALAEAEAALRD-------LRRELRELEAEIASLERRKSNI 438
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 139-299 2.43e-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: 46.59  E-value: 2.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   139 QEELETLQSINKKLELKVKE---QKDYWETELLQLKEQNQKMSSEnekmgirVDQLQAQLSTQEKEMEKLVQGDQDKTEQ 215
Cdd:TIGR02168  238 REELEELQEELKEAEEELEEltaELQELEEKLEELRLEVSELEEE-------IEELQKELYALANEISRLEQQKQILRER 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   216 LEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDL 295
Cdd:TIGR02168  311 LANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQ 390


                   ....
gi 386869306   296 LKRE 299
Cdd:TIGR02168  391 LELQ 394
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 139-305 2.53e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 2.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 139 QEELETLQSINKKLElKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQ 218
Cdd:COG1196  284 EEAQAEEYELLAELA-RLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 219 LKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKR 298
Cdd:COG1196  363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE 442


                 ....*..
gi 386869306 299 ENSRLLS 305
Cdd:COG1196  443 ALEEAAE 449
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 139-297 3.62e-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: 3.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   139 QEELETLQSINKKLELKVKEQKDYWET---ELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQgdqdkteq 215
Cdd:TIGR02168  357 EAELEELEAELEELESRLEELEEQLETlrsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK-------- 428

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   216 lEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDL 295
Cdd:TIGR02168  429 -KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEG 507


                   ..
gi 386869306   296 LK 297
Cdd:TIGR02168  508 VK 509
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 178-301 3.95e-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: 45.82  E-value: 3.95e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   178 SSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKK 257
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 386869306   258 QQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENS 301
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 155-263 4.38e-05

Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.


Pssm-ID: 461517 [Multi-domain]  Cd Length: 201  Bit Score: 44.28  E-value: 4.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  155 KVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQ---AQLSTQEKEMEKLVQGDQDKT-EQLEQLKKENDHLFLSL 230
Cdd:pfam05010  12 KARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEktiAQMIEEKQKQKELEHAEIQKVlEEKDQALADLNSVEKSF 91

                          90       100       110
                  ....*....|....*....|....*....|...
gi 386869306  231 TEQRKDQKKLEQTVEQMKQNETTAMKKQQELMD 263
Cdd:pfam05010  92 SDLFKRYEKQKEVISGYKKNEESLKKCAQDYLA 124
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 140-274 4.48e-05

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: 45.78  E-value: 4.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  140 EELETLQSINKKLELKvkEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQL 219
Cdd:TIGR04523 545 DELNKDDFELKKENLE--KEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKA 622

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386869306  220 KKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSE 274
Cdd:TIGR04523 623 KKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDD 677
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 132-262 9.98e-05

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 44.29  E-value: 9.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  132 DILVVTTQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQK----MSSENEKMGIRVDQLQAQLstqeKEMEKLVQ 207
Cdd:pfam05622 274 EIMPAEIREKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRrkneLETQNRLANQRILELQQQV----EELQKALQ 349

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 386869306  208 GDQDKTEQLEQLKKENDHLFLSLTE-QRKDQKKLEQTVEQMKQNETTAMKKQQELM 262
Cdd:pfam05622 350 EQGSKAEDSSLLKQKLEEHLEKLHEaQSELQKKKEQIEELEPKQDSNLAQKIDELQ 405
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 128-299 1.08e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.58  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   128 ENEEDILVVTTQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLvq 207
Cdd:pfam02463  848 LEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKE-- 925

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   208 gdqdktEQLEQLKKENDHLFLSLtEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKE 287
Cdd:pfam02463  926 ------EAEILLKYEEEPEELLL-EEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKE 998

                          170
                   ....*....|..
gi 386869306   288 RLEGENDLLKRE 299
Cdd:pfam02463  999 RLEEEKKKLIRA 1010
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 139-305 1.36e-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: 44.24  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  139 QEELETLQSIN--KKLELK-VKEQKDYWETELLQLKEQNQKMSsenekmgIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQ 215
Cdd:TIGR04523 369 QNEIEKLKKENqsYKQEIKnLESQINDLESKIQNQEKLNQQKD-------EQIKKLQQEKELLEKEIERLKETIIKNNSE 441

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  216 LEQLKKENDHLFLSLTEQRKDQKKLEQTVE----QMKQNETTAMKKQQELMDENFDLSKrlseneiicnaLQRQKERLEG 291
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKNLDNTRESLETQLKvlsrSINKIKQNLEQKQKELKSKEKELKK-----------LNEEKKELEE 510

                         170
                  ....*....|....
gi 386869306  292 ENDLLKRENSRLLS 305
Cdd:TIGR04523 511 KVKDLTKKISSLKE 524
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 139-303 1.66e-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: 43.86  E-value: 1.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  139 QEELETLQSINKKLE---LKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQ 215
Cdd:TIGR04523 411 DEQIKKLQQEKELLEkeiERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKE 490

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  216 LEQLKKEndhlFLSLTEQRKD----QKKLEQTVEQMKQN----ETTAMKKQQELMD-------ENFDLSKRLSENEIicN 280
Cdd:TIGR04523 491 LKSKEKE----LKKLNEEKKEleekVKDLTKKISSLKEKieklESEKKEKESKISDledelnkDDFELKKENLEKEI--D 564

                         170       180
                  ....*....|....*....|...
gi 386869306  281 ALQRQKERLEGENDLLKRENSRL 303
Cdd:TIGR04523 565 EKNKEIEELKQTQKSLKKKQEEK 587
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 36-298 1.71e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 43.81  E-value: 1.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306    36 GDVTCHYTFTQHFIPRRKDWIGIFR-VGWKTTREYYtfmwvtlpidLNNKSAKQQEVQ--FKAYYLPKDDEYYQfcyVDE 112
Cdd:pfam02463   75 AEVEITFDNEDHELPIDKEEVSIRRrVYRGGDSEYY----------INGKNVTKKEVAelLESQGISPEAYNFL---VQG 141

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   113 DGVVRGASIPFQFRPENEEDILV--------------VTTQEELETLQSINKKLELKV--------KEQKDYWETELLQL 170
Cdd:pfam02463  142 GKIEIIAMMKPERRLEIEEEAAGsrlkrkkkealkklIEETENLAELIIDLEELKLQElklkeqakKALEYYQLKEKLEL 221

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   171 KEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQN 250
Cdd:pfam02463  222 EEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSE 301

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 386869306   251 ETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKR 298
Cdd:pfam02463  302 LLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEI 349
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 139-305 3.03e-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: 43.09  E-value: 3.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  139 QEELETL----QSINKKLELKVKEQKDYwETELLQLKEQNQKMSSEnekmgirVDQLQAQLSTQEKEMEKLVQGDQDKTE 214
Cdd:TIGR04523 467 ETQLKVLsrsiNKIKQNLEQKQKELKSK-EKELKKLNEEKKELEEK-------VKDLTKKISSLKEKIEKLESEKKEKES 538

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  215 QLEQLKKE----NDHLFLSLTEQRKDQKklEQTVEQMKQNETTAMKKQ-------QELMDENFDLSKRLSENEIicnalq 283
Cdd:TIGR04523 539 KISDLEDElnkdDFELKKENLEKEIDEK--NKEIEELKQTQKSLKKKQeekqeliDQKEKEKKDLIKEIEEKEK------ 610

                         170       180
                  ....*....|....*....|..
gi 386869306  284 rQKERLEGENDLLKRENSRLLS 305
Cdd:TIGR04523 611 -KISSLEKELEKAKKENEKLSS 631
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 139-305 3.06e-04

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: 41.83  E-value: 3.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 139 QEELETLQSINKKLElKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQE---KEMEKLVQGDQDK--- 212
Cdd:COG1579    6 LRALLDLQELDSELD-RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLEleiEEVEARIKKYEEQlgn 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 213 ---TEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDEnfdLSKRLSENEIICNALQRQKERL 289
Cdd:COG1579   85 vrnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAE---LEEKKAELDEELAELEAELEEL 161

                        170
                 ....*....|....*..
gi 386869306 290 EGE-NDLLKRENSRLLS 305
Cdd:COG1579  162 EAErEELAAKIPPELLA 178
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 130-301 3.24e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 42.79  E-value: 3.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  130 EEDILVVTTQEELETLQSINKKLELKVKEQKDyweTELL----QLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKL 205
Cdd:pfam05483 456 EIQLTAIKTSEEHYLKEVEDLKTELEKEKLKN---IELTahcdKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERM 532

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  206 VQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQK-KLEQTVEQMKQNETTAMKKQqelmdenfdlsKRLSENEIICNALQR 284
Cdd:pfam05483 533 LKQIENLEEKEMNLRDELESVREEFIQKGDEVKcKLDKSEENARSIEYEVLKKE-----------KQMKILENKCNNLKK 601

                         170       180
                  ....*....|....*....|....
gi 386869306  285 QK-------ERLEGENDLLKRENS 301
Cdd:pfam05483 602 QIenknkniEELHQENKALKKKGS 625
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 137-260 3.46e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 3.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 137 TTQEELETLQSINKKLELKVKEQKD-----------------YWE--------TELL-------QLKEQNQKMSSENEKM 184
Cdd:COG3883   62 ALQAEIDKLQAEIAEAEAEIEERREelgeraralyrsggsvsYLDvllgsesfSDFLdrlsalsKIADADADLLEELKAD 141

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386869306 185 GIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKD-QKKLEQTVEQMKQNETTAMKKQQE 260
Cdd:COG3883  142 KAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAaEAQLAELEAELAAAEAAAAAAAAA 218
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 126-294 3.60e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.80  E-value: 3.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  126 RPENEEDILVVTTQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKM-GIRVDQLQAQL-------ST 197
Cdd:pfam17380 364 RIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMeQIRAEQEEARQrevrrleEE 443

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  198 QEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLS-ENE 276
Cdd:pfam17380 444 RAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEkEME 523

                         170
                  ....*....|....*...
gi 386869306  277 IICNALQRQKERLEGEND 294
Cdd:pfam17380 524 ERQKAIYEEERRREAEEE 541
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 128-289 4.29e-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: 42.74  E-value: 4.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   128 ENEEDILvvTTQEELETLQSINKKLELKVKEQKDywetELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQ-------EK 200
Cdd:TIGR02168  786 ELEAQIE--QLKEELKALREALDELRAELTLLNE----EAANLRERLESLERRIAATERRLEDLEEQIEELsedieslAA 859

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   201 EMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEiicN 280
Cdd:TIGR02168  860 EIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE---V 936


                   ....*....
gi 386869306   281 ALQRQKERL 289
Cdd:TIGR02168  937 RIDNLQERL 945
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
142-301 4.30e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 4.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 142 LETLQSINKKLELKVKEQKDYWE--TELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQE--KEMEKLVQGDQDKTEQLE 217
Cdd:COG4717   70 LKELKELEEELKEAEEKEEEYAElqEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLE 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 218 QLKKEND---HLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQ--------QELMDENFDLSKRLSENEIICNALQRQK 286
Cdd:COG4717  150 ELEERLEelrELEEELEELEAELAELQEELEELLEQLSLATEEElqdlaeelEELQQRLAELEEELEEAQEELEELEEEL 229

                        170
                 ....*....|....*
gi 386869306 287 ERLEGENDLLKRENS 301
Cdd:COG4717  230 EQLENELEAAALEER 244
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 124-249 4.39e-04

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 42.53  E-value: 4.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  124 QFRPENEEDILVvTTQEELETLQSI-NKKLELK--VKEQKDYWETELLQLKEQNQKMSSE----------NEKMGIRVDQ 190
Cdd:pfam06160 255 NLELDEAEEALE-EIEERIDQLYDLlEKEVDAKkyVEKNLPEIEDYLEHAEEQNKELKEElervqqsytlNENELERVRG 333

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386869306  191 LQAQLSTQEKEMEKLVQGDQDKT--------------EQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQ 249
Cdd:pfam06160 334 LEKQLEELEKRYDEIVERLEEKEvayselqeeleeilEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKL 406
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 130-305 6.40e-04

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.80  E-value: 6.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  130 EEDILVVTTQEELETLQSINKKLELKVKEQKDYWETellqLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLvQGD 209
Cdd:pfam07888 105 ELSASSEELSEEKDALLAQRAAHEARIRELEEDIKT----LTQRVLERETELERMKERAKKAGAQRKEEEAERKQL-QAK 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  210 QDKTEQ-LEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQqelmdenfdlskrlSENEIICNALQRQKER 288
Cdd:pfam07888 180 LQQTEEeLRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKE--------------AENEALLEELRSLQER 245

                         170       180
                  ....*....|....*....|
gi 386869306  289 L---EGENDLLKRENSRLLS 305
Cdd:pfam07888 246 LnasERKVEGLGEELSSMAA 265
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 128-303 7.14e-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: 41.93  E-value: 7.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  128 ENEEDILVVTTQEELETLQSINKKL--------ELKVKEQK-DYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQ 198
Cdd:TIGR04523 172 ENELNLLEKEKLNIQKNIDKIKNKLlklelllsNLKKKIQKnKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNT 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  199 EKEMEKLVQGDQDKTEQLEQLKKE---NDHLFLSLTEQRKDQK-KLEQTVEQMKQNETTAMKKQQELMDENF-DLSKRLS 273
Cdd:TIGR04523 252 QTQLNQLKDEQNKIKKQLSEKQKEleqNNKKIKELEKQLNQLKsEISDLNNQKEQDWNKELKSELKNQEKKLeEIQNQIS 331

                         170       180       190
                  ....*....|....*....|....*....|
gi 386869306  274 ENEIICNALQRQKERLEGENDLLKRENSRL 303
Cdd:TIGR04523 332 QNNKIISQLNEQISQLKKELTNSESENSEK 361
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 164-301 7.37e-04

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: 7.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 164 ETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHL----------------- 226
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAeaeieerreelgerara 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 227 ----------------------FLS---------------LTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLS 269
Cdd:COG3883   95 lyrsggsvsyldvllgsesfsdFLDrlsalskiadadadlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174

                        170       180       190
                 ....*....|....*....|....*....|..
gi 386869306 270 KRLSENEIICNALQRQKERLEGENDLLKRENS 301
Cdd:COG3883  175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
138-316 7.41e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.43  E-value: 7.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 138 TQEELETLQSINKKLE---LKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTE 214
Cdd:COG4372   85 LNEQLQAAQAELAQAQeelESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQE 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 215 QLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGEND 294
Cdd:COG4372  165 ELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244

                        170       180
                 ....*....|....*....|..
gi 386869306 295 LLKRENSRLLSYMGLDFNSLPY 316
Cdd:COG4372  245 EEDKEELLEEVILKEIEELELA 266
PTZ00121 PTZ00121
MAEBL; Provisional
 111-299 8.73e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 8.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  111 DEDGVVRGASIPFQFRPENEEDILVVTTQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQ 190
Cdd:PTZ00121 1575 DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKK 1654

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  191 LQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKleqtVEQMKQNETTAMKKQQELMDENfdlsk 270
Cdd:PTZ00121 1655 AEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKK----AEELKKKEAEEKKKAEELKKAE----- 1725

                         170       180
                  ....*....|....*....|....*....
gi 386869306  271 rlSENEIICNALQRQKERLEGENDLLKRE 299
Cdd:PTZ00121 1726 --EENKIKAEEAKKEAEEDKKKAEEAKKD 1752
PTZ00121 PTZ00121
MAEBL; Provisional
 87-294 8.88e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 8.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   87 KQQEVQFKAYYLPKDDEyyqfcyvdedgvVRGASIPFQFRPENEedilvVTTQEELETLQSIN--KKLELKVKEQKDYWE 164
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEE------------EKKKVEQLKKKEAEE-----KKKAEELKKAEEENkiKAAEEAKKAEEDKKK 1676

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  165 TELLQLKEQNQKMSSENEKmgirvdqlqaQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTV 244
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAEALK----------KEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA 1746

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386869306  245 EQMKQNETTAMKKQQELMDENFDLSKRLSENE-IICNALQRQKERLEGEND 294
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEaVIEEELDEEDEKRRMEVD 1797
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 156-249 9.00e-04

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 41.36  E-value: 9.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 156 VKEQKDYWETELLQLKEQNQKMSSE----------NEKMGIRVDQLQAQLSTQEKEMEKLVQ--GDQDKT---------- 213
Cdd:PRK04778 308 VEKNSDTLPDFLEHAKEQNKELKEEidrvkqsytlNESELESVRQLEKQLESLEKQYDEITEriAEQEIAyselqeelee 387

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 386869306 214 --EQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQ 249
Cdd:PRK04778 388 ilKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRN 425
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
124-298 1.03e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.16  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 124 QFRPENEEDILVVTTQEELETLQSINKKLElKVKEQKDYWETELLQLKEQNQKMSSENEKMGI--RVDQLQAQLSTQEKE 201
Cdd:COG3206  200 EFRQKNGLVDLSEEAKLLLQQLSELESQLA-EARAELAEAEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAE 278

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 202 MEKLVQGDQDKTEQLEQLKKENDHLFLSL-TEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDEnfdlSKRLSENEIICN 280
Cdd:COG3206  279 LAELSARYTPNHPDVIALRAQIAALRAQLqQEAQRILASLEAELEALQAREASLQAQLAQLEAR----LAELPELEAELR 354

                        170
                 ....*....|....*....
gi 386869306 281 ALQRQKERLEGE-NDLLKR 298
Cdd:COG3206  355 RLEREVEVARELyESLLQR 373
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
123-297 1.10e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 123 FQFRPENEEDILVVTtqEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKM---GIRVDQLQAQLSTQE 199
Cdd:PRK03918 174 IKRRIERLEKFIKRT--ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELeelKEEIEELEKELESLE 251

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 200 KEMEKLVQGDQDKTEQLEQLKKENDhlflSLTEQRKDQKKLEQTVEqmkqnETTAMKK-QQELMDENFDLSKRLSENEII 278
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIE----ELEEKVKELKELKEKAE-----EYIKLSEfYEEYLDELREIEKRLSRLEEE 322

                        170
                 ....*....|....*....
gi 386869306 279 CNALQRQKERLEGENDLLK 297
Cdd:PRK03918 323 INGIEERIKELEEKEERLE 341
PRK12704 PRK12704
phosphodiesterase; Provisional
 157-264 1.11e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 157 KEQKDYWETELLQLKEQNQKMSSENEKmgirvdqlqaQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKD 236
Cdd:PRK12704  49 KEAEAIKKEALLEAKEEIHKLRNEFEK----------ELRERRNELQKLEKRLLQKEENLDRKLELLEKREEELEKKEKE 118

                         90       100
                 ....*....|....*....|....*...
gi 386869306 237 QKKLEQTVEQMKQNETTAMKKQQELMDE 264
Cdd:PRK12704 119 LEQKQQELEKKEEELEELIEEQLQELER 146
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 164-257 1.28e-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: 40.52  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 164 ETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQT 243
Cdd:COG4942  149 REQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228

                         90
                 ....*....|....
gi 386869306 244 VEQMKQNETTAMKK 257
Cdd:COG4942  229 IARLEAEAAAAAER 242
DUF3450 pfam11932
Protein of unknown function (DUF3450); This family of proteins are functionally ...
 142-246 1.42e-03

Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.


Pssm-ID: 432198 [Multi-domain]  Cd Length: 238  Bit Score: 39.91  E-value: 1.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  142 LETLQSINKkLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLvqgdQDKTEQLEQLKK 221
Cdd:pfam11932  19 LDLAEKAVA-AAAQSQKKIDKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASL----ERQIEEIERTER 93

                          90       100
                  ....*....|....*....|....*
gi 386869306  222 ENDHLFLSLTEQrkdqkkLEQTVEQ 246
Cdd:pfam11932  94 ELVPLMLKMLDR------LEQFVAL 112
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 128-292 1.47e-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: 40.82  E-value: 1.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   128 ENEE--DILVVTTQEELETLQ-SINKKLELKV--KEQKDYWETELLqlkeqNQKMSSENEKmgirvDQLQAQLSTQEKEM 202
Cdd:TIGR02169  184 ENIErlDLIIDEKRQQLERLRrEREKAERYQAllKEKREYEGYELL-----KEKEALERQK-----EAIERQLASLEEEL 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   203 EKLVQGDQDKTEQLEQLKKENDHLF-----LSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMdenfDLSKRLSENEI 277
Cdd:TIGR02169  254 EKLTEEISELEKRLEEIEQLLEELNkkikdLGEEEQLRVKEKIGELEAEIASLERSIAEKERELE----DAEERLAKLEA 329

                          170
                   ....*....|....*
gi 386869306   278 ICNALQRQKERLEGE 292
Cdd:TIGR02169  330 EIDKLLAEIEELERE 344
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
157-303 1.55e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.79  E-value: 1.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 157 KEQKDYWETELLQLKEQNQKMSSENE------KMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSL 230
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLEraedlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA 553

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386869306 231 TEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSK---RLSENEIICNALQRQKERLEGENDLLKRENSRL 303
Cdd:PRK02224 554 EEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirtLLAAIADAEDEIERLREKREALAELNDERRERL 629
DUF4175 pfam13779
Domain of unknown function (DUF4175);
139-269 1.66e-03

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 40.74  E-value: 1.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  139 QEELETL-----QSINKKL-ELKvkEQKDYWETELLQLKEQNQKMssenekmgIRVDQLQAQLstqeKEMEKLVQ-GDQD 211
Cdd:pfam13779 508 DEEIAKLmqelrEALDDYMqALA--EQAQQNPQDLQQPDDPNAQE--------MTQQDLQRML----DRIEELARsGRRA 573

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386869306  212 KTEQ-LEQLKKENDHLFLSLTEQRKDQKKlEQTVEQMKQNETTaMKKQQELMDENFDLS 269
Cdd:pfam13779 574 EAQQmLSQLQQMLENLQAGQPQQQQQQGQ-SEMQQAMDELGDL-LREQQQLLDETFRQL 630
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 88-293 1.69e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 40.48  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   88 QQEVQFKAYYLPKDDEYYQFCYVDEDGVVRGASIPFQFRPENEEDILV-----------VTTQEELEtLQSINKKLELKV 156
Cdd:pfam05483 137 EEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVymdlnnniekmILAFEELR-VQAENARLEMHF 215

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  157 KEQKDYweTELLQLKEQNQKMSSENEKmgiRVDQLQAQLSTQEKEMEKL---VQGDQDKTEQLEQLKKENDHlflSLTEQ 233
Cdd:pfam05483 216 KLKEDH--EKIQHLEEEYKKEINDKEK---QVSLLLIQITEKENKMKDLtflLEESRDKANQLEEKTKLQDE---NLKEL 287

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  234 RKDQKKLEQTVEQMKQNETTAMKKQQELmDENFDLSKRlseneIICNALQRQKERLEGEN 293
Cdd:pfam05483 288 IEKKDHLTKELEDIKMSLQRSMSTQKAL-EEDLQIATK-----TICQLTEEKEAQMEELN 341
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 139-299 1.76e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 40.59  E-value: 1.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 139 QEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSEN---EKMGI--RVDQLQAQLSTQEKEMEKLvqgDQDKT 213
Cdd:PRK04778 204 EEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEEGyhlDHLDIekEIQDLKEQIDENLALLEEL---DLDEA 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 214 E-QLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDE--NFDLSKRLSENEI-ICNALQRQKERL 289
Cdd:PRK04778 281 EeKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEidRVKQSYTLNESELeSVRQLEKQLESL 360

                        170
                 ....*....|
gi 386869306 290 EGENDLLKRE 299
Cdd:PRK04778 361 EKQYDEITER 370
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 140-292 2.27e-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: 40.44  E-value: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   140 EELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDktEQLEQL 219
Cdd:TIGR02169  719 GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEI 796

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386869306   220 KKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGE 292
Cdd:TIGR02169  797 QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 137-297 2.30e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 40.22  E-value: 2.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  137 TTQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSEN---EKMGI--RVDQLQAQLstqEKEMEKLVQGDQD 211
Cdd:pfam06160 183 KLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGyalEHLNVdkEIQQLEEQL---EENLALLENLELD 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  212 KTEQ-LEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDE--NFDLSKRLSENEI-ICNALQRQKE 287
Cdd:pfam06160 260 EAEEaLEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEEleRVQQSYTLNENELeRVRGLEKQLE 339

                         170
                  ....*....|
gi 386869306  288 RLEGENDLLK 297
Cdd:pfam06160 340 ELEKRYDEIV 349
mukB PRK04863
chromosome partition protein MukB;
139-298 2.38e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 40.33  E-value: 2.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  139 QEELETLQS---INKKLELKVKEQKDYWeTELLQLK-----EQNQKMSSENekmgirvDQLQAQLStqekemEKLVQGDQ 210
Cdd:PRK04863  934 PEQFEQLKQdyqQAQQTQRDAKQQAFAL-TEVVQRRahfsyEDAAEMLAKN-------SDLNEKLR------QRLEQAEQ 999

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  211 DKTEQLEQLKK------ENDHLFLSLTE--QRKDQ--KKLEQTVEQMKQNETTAMKKQQELMDEnfDLSKRLSENEIICN 280
Cdd:PRK04863 1000 ERTRAREQLRQaqaqlaQYNQVLASLKSsyDAKRQmlQELKQELQDLGVPADSGAEERARARRD--ELHARLSANRSRRN 1077

                         170
                  ....*....|....*....
gi 386869306  281 ALQRQKERLEGE-NDLLKR 298
Cdd:PRK04863 1078 QLEKQLTFCEAEmDNLTKK 1096
PRK12704 PRK12704
phosphodiesterase; Provisional
 192-328 2.82e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 2.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 192 QAQLSTQEKEMEKLVQGDQDKTEQLEQLKKEndhlflsLTEQRKD----QKKLEQTVEQMKQNETTAMKKQQELMDENFD 267
Cdd:PRK12704  46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKE-------LRERRNElqklEKRLLQKEENLDRKLELLEKREEELEKKEKE 118

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386869306 268 LSKRLSEneiicnaLQRQKERLEgenDLLKRENSRLLSYMGLdfnslpyqvpTSDEggARQ 328
Cdd:PRK12704 119 LEQKQQE-------LEKKEEELE---ELIEEQLQELERISGL----------TAEE--AKE 157
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 159-270 2.92e-03

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.10  E-value: 2.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   159 QKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQK 238
Cdd:pfam15921  591 EKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELN 670

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 386869306   239 KLEQTVEQMKQN--------ETTAMKKQQELMDENFDLSK 270
Cdd:pfam15921  671 SLSEDYEVLKRNfrnkseemETTTNKLKMQLKSAQSELEQ 710
PRK12705 PRK12705
hypothetical protein; Provisional
 139-287 3.09e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 39.69  E-value: 3.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 139 QEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKmgirVDQLQAQLSTQEKEMEklvqgdqDKTEQLEQ 218
Cdd:PRK12705  55 LEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEK----LDNLENQLEEREKALS-------ARELELEE 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386869306 219 LKKENDHLFLSLTEQRKDQ------KKLEQTVEQMKQNETTAMKkqqelmdENFDLSKRLSENEIICNALQRQKE 287
Cdd:PRK12705 124 LEKQLDNELYRVAGLTPEQarklllKLLDAELEEEKAQRVKKIE-------EEADLEAERKAQNILAQAMQRIAS 191
PRK12704 PRK12704
phosphodiesterase; Provisional
 146-284 3.53e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.38  E-value: 3.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 146 QSINKKLELKVKE----QKDYWETEL-------------LQLKEQN--------QKMSSENEKMGIRVDQLQAQLSTQEK 200
Cdd:PRK12704  52 EAIKKEALLEAKEeihkLRNEFEKELrerrnelqklekrLLQKEENldrklellEKREEELEKKEKELEQKQQELEKKEE 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 201 EMEKLVQGDQDKTEQLEQLKKEndhlflsltEQRKDQkkLEQTVEQMKQnETTAMKKQQElmDENFDLSKRLSeNEIICN 280
Cdd:PRK12704 132 ELEELIEEQLQELERISGLTAE---------EAKEIL--LEKVEEEARH-EAAVLIKEIE--EEAKEEADKKA-KEILAQ 196


                 ....
gi 386869306 281 ALQR 284
Cdd:PRK12704 197 AIQR 200
mukB PRK04863
chromosome partition protein MukB;
129-310 3.95e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.56  E-value: 3.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  129 NEEDILVVTTQEELETLQSINKKLELKVKEQKDywetellQLKEQNQKMSSENEkmgiRVDQLQAQLSTQEKEMEKL-VQ 207
Cdd:PRK04863  981 AKNSDLNEKLRQRLEQAEQERTRAREQLRQAQA-------QLAQYNQVLASLKS----SYDAKRQMLQELKQELQDLgVP 1049

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  208 GDQDKTEQLEQLKKENDHLfLSLTEQRKDQKKLEQTVEQMkqnETTAMKKQQELMDENFDLSKRLSENE--IICNALqrq 285
Cdd:PRK04863 1050 ADSGAEERARARRDELHAR-LSANRSRRNQLEKQLTFCEA---EMDNLTKKLRKLERDYHEMREQVVNAkaGWCAVL--- 1122

                         170       180
                  ....*....|....*....|....*
gi 386869306  286 keRLEGENDLLKRENSRLLSYMGLD 310
Cdd:PRK04863 1123 --RLVKDNGVERRLHRRELAYLSAD 1145
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 130-305 4.03e-03

HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 39.29  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  130 EEDILVVTTQEELETLQSINKKLELKVKEQKDYWET-------------ELLQLKEQNQKMSSENEKMGIRVDQLQAQLS 196
Cdd:pfam05622  18 ELDQQVSLLQEEKNSLQQENKKLQERLDQLESGDDSgtpggkkylllqkQLEQLQEENFRLETARDDYRIKCEELEKEVL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  197 TQEKEMEKLvqgdQDKTEQLEQLKKENDhlflSLTEQRKDQKKLEQTVE--------------QMKQNE----------- 251
Cdd:pfam05622  98 ELQHRNEEL----TSLAEEAQALKDEMD----ILRESSDKVKKLEATVEtykkkledlgdlrrQVKLLEernaeymqrtl 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386869306  252 --------TTAMKKQQELMDENF-DLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLS 305
Cdd:pfam05622 170 qleeelkkANALRGQLETYKRQVqELHGKLSEESKKADKLEFEYKKLEEKLEALQKEKERLII 232
COG5022 COG5022
Myosin heavy chain [General function prediction only];
140-297 4.50e-03

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 39.29  E-value: 4.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  140 EELETLQSINKKLELKVKEQKDYWET-ELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQ 218
Cdd:COG5022   928 ELIARLKKLLNNIDLEEGPSIEYVKLpELNKLHEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQ 1007

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386869306  219 LKKENDHlfLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLK 297
Cdd:COG5022  1008 YGALQES--TKQLKELPVEVAELQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLY 1084
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
 158-314 5.10e-03

SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an RNA-binding protein that binds specific mRNAs, including the mRNA of Ash1, which is invalid in cell-fate determination. She3 acts as an adapter protein that docks the myosin motor Myo4p onto an Ash1-She2p ribonucleoprotein complex. She3 seems to bind to Myo4p and Shep2p via different domains.


Pssm-ID: 293683 [Multi-domain]  Cd Length: 228  Bit Score: 38.18  E-value: 5.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  158 EQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQ 237
Cdd:pfam17078  10 DQIDALTKTNLQLTVQSQNLLSKLEIAQQKESKFLENLASLKHENDNLSSMLNRKERRLKDLEDQLSELKNSYEELTESN 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  238 KKLEQTVEQMKQNETTaMKKQQELMDENFD-------LSKRLSENEIicNALQRQKERLEGENDLLKRENSRLLSYMGLD 310
Cdd:pfam17078  90 KQLKKRLENSSASETT-LEAELERLQIQYDalvdsqnEYKDHYQQEI--NTLQESLEDLKLENEKQLENYQQRISSNDKD 166


                  ....
gi 386869306  311 FNSL 314
Cdd:pfam17078 167 IDTK 170
Zn-C2H2_12 pfam18112
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ...
 380-402 5.62e-03

Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and coiled-coil domain 2/NDP25 (CALCOCO2/NDP25) found in Homo sapiens. CALCOCO2/NDP25 is an ubiquitin-binding autophagy receptor involved in the selective autophagic degradation of invading pathogens. This domain is a typical C2H2-type zinc finger which specifically recognizes mono-ubiquitin or poly-ubiquitin chain. The overall ubiquitin-binding mode utilizes the C-terminal alpha-helix to interact with the solvent-exposed surface of the central beta-sheet of ubiquitin, similar to that observed in the RABGEF1/Rabex-5 or POLN/Pol-eta zinc finger.


Pssm-ID: 407946  Cd Length: 27  Bit Score: 34.16  E-value: 5.62e-03
                          10        20
                  ....*....|....*....|....
gi 386869306  380 CPICDKIFPA-TEKQIFEDHVFCH 402
Cdd:pfam18112   3 CPLCGEMFSPnIDQSEFEEHVESH 26
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 169-310 6.25e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 38.78  E-value: 6.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  169 QLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTE-------QRKDQKKLE 241
Cdd:COG3096   988 KLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQELEELGVQADAeaeerarIRRDELHEE 1067

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306  242 QTVEQMKQNETTAMKKQQEL-MDEnfdLSKRLSENEIICNALQRQKE----------RLEGENDLLKRENSRLLSYMGLD 310
Cdd:COG3096  1068 LSQNRSRRSQLEKQLTRCEAeMDS---LQKRLRKAERDYKQEREQVVqakagwcavlRLARDNDVERRLHRRELAYLSAD 1144
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
138-307 6.33e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.34  E-value: 6.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 138 TQEELEtlqSINKKLELKVKEQKDYwETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLE 217
Cdd:COG4372   78 LEEELE---ELNEQLQAAQAELAQA-QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK 153

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306 218 QLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLK 297
Cdd:COG4372  154 ELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233

                        170
                 ....*....|
gi 386869306 298 RENSRLLSYM 307
Cdd:COG4372  234 ALSALLDALE 243
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 139-276 6.53e-03

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 38.87  E-value: 6.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   139 QEELETLQSINKKLELKVKEQKDYW----ETEL----LQLKEQNQKMSSENEKMGIRVDQLQAQlstqeKEMEKLVQGD- 209
Cdd:TIGR00606  947 KEKVKNIHGYMKDIENKIQDGKDDYlkqkETELntvnAQLEECEKHQEKINEDMRLMRQDIDTQ-----KIQERWLQDNl 1021

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386869306   210 -----QDKTEQLEQLKKENDHLF--LSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENE 276
Cdd:TIGR00606 1022 tlrkrENELKEVEEELKQHLKEMgqMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
CCDC73 pfam15818
Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil ...
 164-278 7.16e-03

Coiled-coil domain-containing protein 73 family; CCDC73 is a family of eukaryotic coiled-coil containing proteins. The function is not known. The alternative name is sarcoma antigen NY-SAR-79.


Pssm-ID: 464893 [Multi-domain]  Cd Length: 1048  Bit Score: 38.77  E-value: 7.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   164 ETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTE-QRKDQKKLEQ 242
Cdd:pfam15818  277 EAELKALKENNQTLERDNELQREKVKENEEKFLNLQNEHEKALGTWKKHVEELNGEINEIKNELSSLKEtHIKLQEHYNK 356

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 386869306   243 TVEQMKQNETTAMKKQQELMDENFDLSKRLSENEII 278
Cdd:pfam15818  357 LCNQKKFEEDKKFQNVPEVNNENSEMSTEKSENLII 392
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 139-294 9.05e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 38.23  E-value: 9.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   139 QEELETLQSIN-------KKLELKVKE-QKDYWETEL--LQLKEQNQKMSSENE--------------KMGIRVDQLQAQ 194
Cdd:pfam01576  390 QAELRTLQQAKqdsehkrKKLEGQLQElQARLSESERqrAELAEKLSKLQSELEsvssllneaegkniKLSKDVSSLESQ 469

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869306   195 LS-TQEKEME----------KLVQGDQDKTEQLEQL------KKENDHLFLSLTEQRKD-QKKLEQTVEQMKQNETTAMK 256
Cdd:pfam01576  470 LQdTQELLQEetrqklnlstRLRQLEDERNSLQEQLeeeeeaKRNVERQLSTLQAQLSDmKKKLEEDAGTLEALEEGKKR 549

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 386869306   257 KQQELMdenfDLSKRLSENEIICNALQRQKERLEGEND 294
Cdd:pfam01576  550 LQRELE----ALTQQLEEKAAAYDKLEKTKNRLQQELD 583
 
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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