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Conserved domains on  [gi|386869294|ref|NP_001248320|]
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calcium-binding and coiled-coil domain-containing protein 2 isoform 2 [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 ...
 23-146 5.55e-41

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: 141.61  E-value: 5.55e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   23 VIFNSVEKFYIPGGDVTCHYTFTQHFIPRRKDWIGIFRcslnqtiqllitpdtgsiwhqVGWKTTREYYTFMWVtlPIDL 102
Cdd:pfam17751   1 VVFQNVGEWYPPDEDIECSYTLTPDFTPSSWDWIGLFK---------------------VGWKSVNDYVTYVWA--KDDE 57

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 386869294  103 NNKSAKQQEVQFKAYYLPKDD-EYYQFCYVDEDGVVRGASIPFQF 146
Cdd:pfam17751  58 VEGSNSVRQVLFKASYLPKEPeGFYQFCYVSNLGSVVGISTPFQF 102
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 159-362 1.39e-12

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: 69.02  E-value: 1.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 159 TQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDywetELLQLKEQNQ 238
Cdd:COG4942   39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE----ELAELLRALY 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 239 KMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAM 318
Cdd:COG4942  115 RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 386869294 319 KKQQELMDEnfdLSKRLSENEIICNALQRQKERLEGENDLLKRE 362
Cdd:COG4942  195 AERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLEAE 235
Zn-C2H2_CALCOCO2 cd21968
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ...
 441-467 2.29e-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: 52.45  E-value: 2.29e-09
                         10        20
                 ....*....|....*....|....*..
gi 386869294 441 FNCPICDKIFPATEKQIFEDHVFCHSL 467
Cdd:cd21968    1 FECPICSKIFEATSKQEFEDHVFCHSL 27
 
Name Accession Description Interval E-value
SKICH pfam17751
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ...
 23-146 5.55e-41

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: 141.61  E-value: 5.55e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   23 VIFNSVEKFYIPGGDVTCHYTFTQHFIPRRKDWIGIFRcslnqtiqllitpdtgsiwhqVGWKTTREYYTFMWVtlPIDL 102
Cdd:pfam17751   1 VVFQNVGEWYPPDEDIECSYTLTPDFTPSSWDWIGLFK---------------------VGWKSVNDYVTYVWA--KDDE 57

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 386869294  103 NNKSAKQQEVQFKAYYLPKDD-EYYQFCYVDEDGVVRGASIPFQF 146
Cdd:pfam17751  58 VEGSNSVRQVLFKASYLPKEPeGFYQFCYVSNLGSVVGISTPFQF 102
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 159-362 1.39e-12

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: 69.02  E-value: 1.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 159 TQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDywetELLQLKEQNQ 238
Cdd:COG4942   39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE----ELAELLRALY 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 239 KMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAM 318
Cdd:COG4942  115 RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 386869294 319 KKQQELMDEnfdLSKRLSENEIICNALQRQKERLEGENDLLKRE 362
Cdd:COG4942  195 AERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLEAE 235
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 165-368 9.43e-11

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: 64.31  E-value: 9.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   165 EIEQHNKELckenQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQkdywETELLQLKEQNQKMSSEN 244
Cdd:TIGR02168  233 RLEELREEL----EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL----QKELYALANEISRLEQQK 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   245 EKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQEL 324
Cdd:TIGR02168  305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 386869294   325 MDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLS 368
Cdd:TIGR02168  385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
Zn-C2H2_CALCOCO2 cd21968
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ...
 441-467 2.29e-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: 52.45  E-value: 2.29e-09
                         10        20
                 ....*....|....*....|....*..
gi 386869294 441 FNCPICDKIFPATEKQIFEDHVFCHSL 467
Cdd:cd21968    1 FECPICSKIFEATSKQEFEDHVFCHSL 27
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
144-361 2.59e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.14  E-value: 2.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 144 FQFRPENEEDILVVTtqgevEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLElkvkeqk 223
Cdd:PRK03918 174 IKRRIERLEKFIKRT-----ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE------- 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 224 dywetellQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLvqgdQDKTEQLEQLKKENDhLFLSLTEQRKDQKKL 303
Cdd:PRK03918 242 --------ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL----EEKVKELKELKEKAE-EYIKLSEFYEEYLDE 308

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 386869294 304 EQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKR 361
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEE 366
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 149-362 4.28e-07

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: 52.67  E-value: 4.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   149 ENEEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVK--EQKDYW 226
Cdd:pfam02463  807 EEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEEleEQKLKD 886

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   227 ETELLQLKEQNQKMSSENEKmgiRVDQLQAQLSTQEKEMEKLvqgdqdktEQLEQLKKENDHLFLSLtEQRKDQKKLEQT 306
Cdd:pfam02463  887 ELESKEEKEKEEKKELEEES---QKLNLLEEKENEIEERIKE--------EAEILLKYEEEPEELLL-EEADEKEKEENN 954

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 386869294   307 VEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRE 362
Cdd:pfam02463  955 KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRA 1010
Zn-C2H2_12 pfam18112
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ...
 443-465 7.58e-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: 33.77  E-value: 7.58e-03
                          10        20
                  ....*....|....*....|....
gi 386869294  443 CPICDKIFPA-TEKQIFEDHVFCH 465
Cdd:pfam18112   3 CPLCGEMFSPnIDQSEFEEHVESH 26
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 163-366 7.72e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 38.33  E-value: 7.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 163 VEEIEQHNKELCKENQElkdscISLQKqnsdMQAELQKKQEELEtlQSINKKLELKVKEQKDYwetellqLKEQNQKMSS 242
Cdd:cd16269   96 MEQLEEKKEEFCKQNEE-----ASSKR----CQALLQELSAPLE--EKISQGSYSVPGGYQLY-------LEDREKLVEK 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 243 ENEKM--GIRVDQ-LQAQLSTQEKEMEKLVQGDQDKTE---QLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETT 316
Cdd:cd16269  158 YRQVPrkGVKAEEvLQEFLQSKEAEAEAILQADQALTEkekEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEE 237

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 386869294 317 AMKKQQELMDEnfDLSKRLSENEIICNALQRQKERL-----EGENDLLKRENSRL 366
Cdd:cd16269  238 HLRQLKEKMEE--ERENLLKEQERALESKLKEQEALleegfKEQAELLQEEIRSL 290
 
Name Accession Description Interval E-value
SKICH pfam17751
SKICH domain; The SKICH domains of SKIP and PIPP mediate plasma membrane localization. The ...
 23-146 5.55e-41

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: 141.61  E-value: 5.55e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   23 VIFNSVEKFYIPGGDVTCHYTFTQHFIPRRKDWIGIFRcslnqtiqllitpdtgsiwhqVGWKTTREYYTFMWVtlPIDL 102
Cdd:pfam17751   1 VVFQNVGEWYPPDEDIECSYTLTPDFTPSSWDWIGLFK---------------------VGWKSVNDYVTYVWA--KDDE 57

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 386869294  103 NNKSAKQQEVQFKAYYLPKDD-EYYQFCYVDEDGVVRGASIPFQF 146
Cdd:pfam17751  58 VEGSNSVRQVLFKASYLPKEPeGFYQFCYVSNLGSVVGISTPFQF 102
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 159-362 1.39e-12

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: 69.02  E-value: 1.39e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 159 TQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDywetELLQLKEQNQ 238
Cdd:COG4942   39 LEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKE----ELAELLRALY 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 239 KMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAM 318
Cdd:COG4942  115 RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 386869294 319 KKQQELMDEnfdLSKRLSENEIICNALQRQKERLEGENDLLKRE 362
Cdd:COG4942  195 AERQKLLAR---LEKELAELAAELAELQQEAEELEALIARLEAE 235
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 165-368 9.43e-11

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: 64.31  E-value: 9.43e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   165 EIEQHNKELckenQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQkdywETELLQLKEQNQKMSSEN 244
Cdd:TIGR02168  233 RLEELREEL----EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL----QKELYALANEISRLEQQK 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   245 EKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQEL 324
Cdd:TIGR02168  305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 386869294   325 MDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLS 368
Cdd:TIGR02168  385 RSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-367 7.91e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.49  E-value: 7.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 160 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQkdywETELLQLKEQNQK 239
Cdd:COG1196  252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL----EERLEELEEELAE 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 240 MSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMK 319
Cdd:COG1196  328 LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE 407

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 386869294 320 KQQELMDEnfdLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLL 367
Cdd:COG1196  408 AEEALLER---LERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 165-412 1.15e-09

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 59.84  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 165 EIEQHNKELckenQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDywetellQLKEQNQKMSSEN 244
Cdd:COG3883   17 QIQAKQKEL----SELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQA-------EIAEAEAEIEERR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 245 EKMGIRVDQLQ------------------AQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQT 306
Cdd:COG3883   86 EELGERARALYrsggsvsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 307 VEQMKQNETTAMKKQQELMDenfdlskRLSENEiicNALQRQKERLEGENDLLKRENSRLLSYmGLDFNSLPYQVPTSDE 386
Cdd:COG3883  166 LEAAKAELEAQQAEQEALLA-------QLSAEE---AAAEAQLAELEAELAAAEAAAAAAAAA-AAAAAAAAAAAAAAAA 234

                        250       260
                 ....*....|....*....|....*.
gi 386869294 387 GGARQNPGLAYGNPYSGIQESSSPSP 412
Cdd:COG3883  235 AAAAAAAAAASAAGAGAAGAAGAAAG 260
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 160-367 1.65e-09

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: 60.47  E-value: 1.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   160 QGEVEEIEQhnKELCKENQELKDSCISLQKQNSDMQAELQKKQEELE----TLQSINKKLELKVKEQKDYWETELLQLKE 235
Cdd:TIGR02169  217 LKEKREYEG--YELLKEKEALERQKEAIERQLASLEEELEKLTEEISelekRLEEIEQLLEELNKKIKDLGEEEQLRVKE 294

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   236 QNQKMSSEnekmgirVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEqtvEQMKQNET 315
Cdd:TIGR02169  295 KIGELEAE-------IASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLT---EEYAELKE 364

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 386869294   316 TAMKKQQELMDEnfdlSKRLSENEIICNALQRQKERLEGENDLLKRENSRLL 367
Cdd:TIGR02169  365 ELEDLRAELEEV----DKEFAETRDELKDYREKLEKLKREINELKRELDRLQ 412
Zn-C2H2_CALCOCO2 cd21968
C2H2-type zinc binding domain found in calcium-binding and coiled-coil domain-containing ...
 441-467 2.29e-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: 52.45  E-value: 2.29e-09
                         10        20
                 ....*....|....*....|....*..
gi 386869294 441 FNCPICDKIFPATEKQIFEDHVFCHSL 467
Cdd:cd21968    1 FECPICSKIFEATSKQEFEDHVFCHSL 27
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 162-368 2.53e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.57  E-value: 2.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 162 EVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMS 241
Cdd:COG1196  296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELA 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 242 SENEkmgiRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQ 321
Cdd:COG1196  376 EAEE----ELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 386869294 322 QELMDENFDLSKRLSENEiicNALQRQKERLEGENDLLKRENSRLLS 368
Cdd:COG1196  452 AELEEEEEALLELLAELL---EEAALLEAALAELLEELAEAAARLLL 495
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 154-366 3.28e-09

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: 58.62  E-value: 3.28e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 154 ILVVTTQGEVEEIEQHNKELckenqelkdscISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQkdywETELLQL 233
Cdd:COG4942   10 LLALAAAAQADAAAEAEAEL-----------EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAAL----ARRIRAL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 234 KEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLV-----QGDQDKTE-------------QLEQLKKENDHLFLSLTE 295
Cdd:COG4942   75 EQELAALEAELAELEKEIAELRAELEAQKEELAELLralyrLGRQPPLAlllspedfldavrRLQYLKYLAPARREQAEE 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386869294 296 QRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 366
Cdd:COG4942  155 LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEL 225
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 149-366 4.75e-09

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: 58.93  E-value: 4.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   149 ENEEDILvvttQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELET----LQSINKKLELKVKEQKD 224
Cdd:TIGR02169  687 KRELSSL----QSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEleedLSSLEQEIENVKSELKE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   225 YwETELLQLKEQNQKMSSENEKM-----GIRVDQLQAQLSTQEKE----------MEKLVQGDQDKTEQLEQLKKENDHL 289
Cdd:TIGR02169  763 L-EARIEELEEDLHKLEEALNDLearlsHSRIPEIQAELSKLEEEvsriearlreIEQKLNRLTLEKEYLEKEIQELQEQ 841

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   290 FLSLTEQRKDQKK----LEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSR 365
Cdd:TIGR02169  842 RIDLKEQIKSIEKeienLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSE 921


                   .
gi 386869294   366 L 366
Cdd:TIGR02169  922 L 922
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
195-366 5.11e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 58.77  E-value: 5.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  195 QAELQKKQEELETLQSINKKLElkvkEQKDYWETELLQLkeQNQKMSSENEkmgIRVDQLQAQLSTQEKEMEKLVQGDQD 274
Cdd:COG4913   616 EAELAELEEELAEAEERLEALE----AELDALQERREAL--QRLAEYSWDE---IDVASAEREIAELEAELERLDASSDD 686

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  275 ---KTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDE-----NFDLSKRLsENEIICNALQ 346
Cdd:COG4913   687 laaLEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLarlelRALLEERF-AAALGDAVER 765

                         170       180
                  ....*....|....*....|
gi 386869294  347 RQKERLEGENDLLKRENSRL 366
Cdd:COG4913   766 ELRENLEERIDALRARLNRA 785
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 160-366 6.39e-09

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: 58.53  E-value: 6.39e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   160 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETL----QSINKKLELKVKEQKDYwETELLQLKE 235
Cdd:TIGR02168  252 EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeqqkQILRERLANLERQLEEL-EAQLEELES 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   236 QNQKMSSENEKMGIRVDQLQ-------AQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVE 308
Cdd:TIGR02168  331 KLDELAEELAELEEKLEELKeelesleAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 386869294   309 QMKQNettamkkQQELMDENFDLSKRLSENEIicNALQRQKERLEGENDLLKRENSRL 366
Cdd:TIGR02168  411 RLEDR-------RERLQQEIEELLKKLEEAEL--KELQAELEELEEELEELQEELERL 459
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 162-337 8.47e-09

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: 57.72  E-value: 8.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  162 EVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKvkEQKDYWETELLQLKEQNQKMS 241
Cdd:TIGR04523 504 EKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLE--KEIDEKNKEIEELKQTQKSLK 581

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  242 SENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQ 321
Cdd:TIGR04523 582 KKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKW 661

                         170
                  ....*....|....*.
gi 386869294  322 QELMDENFDLSKRLSE 337
Cdd:TIGR04523 662 PEIIKKIKESKTKIDD 677
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 164-366 1.54e-08

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: 57.39  E-value: 1.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   164 EEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELET-LQSINKKLELKVKEQKDYWET------ELLQLKEQ 236
Cdd:TIGR02169  258 EEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAeIASLERSIAEKERELEDAEERlakleaEIDKLLAE 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   237 NQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQ--GDQDKT------------EQLEQLKKENDHLFLSLTEQRKDQKK 302
Cdd:TIGR02169  338 IEELEREIEEERKRRDKLTEEYAELKEELEDLRAelEEVDKEfaetrdelkdyrEKLEKLKREINELKRELDRLQEELQR 417

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386869294   303 LEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 366
Cdd:TIGR02169  418 LSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 171-368 1.83e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.87  E-value: 1.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 171 KELcKENQELKDSCISLQKQNsDMQAELQKKQEELETLQSINKKLELKVKEqkdyWETELLQLKEQNQKMSSENEKMGIR 250
Cdd:COG1196  216 REL-KEELKELEAELLLLKLR-ELEAELEELEAELEELEAELEELEAELAE----LEAELEELRLELEELELELEEAQAE 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 251 VDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKEndhlflsLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFD 330
Cdd:COG1196  290 EYELLAELARLEQDIARLEERRRELEERLEELEEE-------LAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 386869294 331 LSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLS 368
Cdd:COG1196  363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 150-360 2.40e-08

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: 56.60  E-value: 2.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   150 NEEDILVVTTQGEVEEIEQHNKelcKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWET- 228
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELE---SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETl 384

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   229 --ELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQgdqdkteqlEQLKKENDHLFLSLTEQRKDQKKLEQT 306
Cdd:TIGR02168  385 rsKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK---------KLEEAELKELQAELEELEEELEELQEE 455

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 386869294   307 VEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLK 360
Cdd:TIGR02168  456 LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVK 509
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 160-366 3.68e-08

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: 55.80  E-value: 3.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  160 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLE----LKVKEQKDYWETELLQ--- 232
Cdd:TIGR04523 362 QRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQqekeLLEKEIERLKETIIKNnse 441

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  233 ---LKEQNQKMSSENEKMGIRVDQLQAQLSTQEKE-------MEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKK 302
Cdd:TIGR04523 442 ikdLTNQDSVKELIIKNLDNTRESLETQLKVLSRSinkikqnLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISS 521

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386869294  303 LEQTVEQM----KQNETTAMKKQQELMDENFDLSKRLSENEIicNALQRQKERLEGENDLLKRENSRL 366
Cdd:TIGR04523 522 LKEKIEKLesekKEKESKISDLEDELNKDDFELKKENLEKEI--DEKNKEIEELKQTQKSLKKKQEEK 587
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 160-362 3.78e-08

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: 55.80  E-value: 3.78e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  160 QGEVEEIEQHNKELCKENQELKDSCISLQKQ-----NSDMQAELQKKQEELETLQSINKKLELKVKEQKDywetELLQLK 234
Cdd:TIGR04523 273 QKELEQNNKKIKELEKQLNQLKSEISDLNNQkeqdwNKELKSELKNQEKKLEEIQNQISQNNKIISQLNE----QISQLK 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  235 EQNQKMSSENEKmgirvdqLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNE 314
Cdd:TIGR04523 349 KELTNSESENSE-------KQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK 421

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386869294  315 TTAMKKQQELMDENF-------DLSKRLSENEIICNALQRQKERLEGENDLLKRE 362
Cdd:TIGR04523 422 ELLEKEIERLKETIIknnseikDLTNQDSVKELIIKNLDNTRESLETQLKVLSRS 476
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 165-367 4.09e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 4.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 165 EIEQHNKELCKENQELKDscisLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSEN 244
Cdd:COG1196  233 KLRELEAELEELEAELEE----LEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLE 308

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 245 EKM---GIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQ 321
Cdd:COG1196  309 ERRrelEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEEL 388

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 386869294 322 QELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLL 367
Cdd:COG1196  389 LEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 165-366 6.95e-08

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: 55.06  E-value: 6.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   165 EIEQHNKELckenQELKDSCISLQKQnsdmQAELQKKQEELETLQSinkklelKVKEQKDYWETELLQLKEQNQKMSSEN 244
Cdd:TIGR02168  678 EIEELEEKI----EELEEKIAELEKA----LAELRKELEELEEELE-------QLRKELEELSRQISALRKDLARLEAEV 742

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   245 EKMGIRVDQLQAQLSTQEKEMEklvqgdqdktEQLEQLKKENDHLflslTEQRKDQKKLEQTVEQMKQNETTAMKKQQEL 324
Cdd:TIGR02168  743 EQLEERIAQLSKELTELEAEIE----------ELEERLEEAEEEL----AEAEAEIEELEAQIEQLKEELKALREALDEL 808

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 386869294   325 MDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 366
Cdd:TIGR02168  809 RAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 156-368 1.18e-07

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: 54.26  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  156 VVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSIN--KKLELK-VKEQKDYWETELLQ 232
Cdd:TIGR04523 323 LEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENqsYKQEIKnLESQINDLESKIQN 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  233 LKEQNQKMSsenekmgIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVE---- 308
Cdd:TIGR04523 403 QEKLNQQKD-------EQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKvlsr 475

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  309 QMKQNETTAMKKQQELMDENFDLSKrlseneiicnaLQRQKERLEGENDLLKRENSRLLS 368
Cdd:TIGR04523 476 SINKIKQNLEQKQKELKSKEKELKK-----------LNEEKKELEEKVKDLTKKISSLKE 524
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
243-374 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: 53.71  E-value: 1.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 243 ENEKMGIRVDQLQAQLSTQEKEMEKLvqgdqdkTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQ 322
Cdd:COG2433  393 EEPEAEREKEHEERELTEEEEEIRRL-------EEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERREIRKDR 465

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 386869294 323 ELmdenfdlSKRlsENEIicNALQRQKERLEGENDLLKRENSRLLSYMGLDF 374
Cdd:COG2433  466 EI-------SRL--DREI--ERLERELEEERERIEELKRKLERLKELWKLEH 506
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
194-366 2.28e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.60  E-value: 2.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 194 MQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQ 273
Cdd:COG4372    4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 274 DKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLE 353
Cdd:COG4372   84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163

                        170
                 ....*....|...
gi 386869294 354 GENDLLKRENSRL 366
Cdd:COG4372  164 EELAALEQELQAL 176
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
144-361 2.59e-07

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 53.14  E-value: 2.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 144 FQFRPENEEDILVVTtqgevEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLElkvkeqk 223
Cdd:PRK03918 174 IKRRIERLEKFIKRT-----ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIE------- 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 224 dywetellQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLvqgdQDKTEQLEQLKKENDhLFLSLTEQRKDQKKL 303
Cdd:PRK03918 242 --------ELEKELESLEGSKRKLEEKIRELEERIEELKKEIEEL----EEKVKELKELKEKAE-EYIKLSEFYEEYLDE 308

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 386869294 304 EQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKR 361
Cdd:PRK03918 309 LREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEE 366
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
158-379 2.84e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.60  E-value: 2.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 158 TTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLE---LKVKEQKDYWETELLQLK 234
Cdd:COG4372   42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQeelESLQEEAEELQEELEELQ 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 235 EQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNE 314
Cdd:COG4372  122 KERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEE 201

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386869294 315 TTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLSYMGLDFNSLPY 379
Cdd:COG4372  202 LAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 159-323 3.93e-07

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 52.14  E-value: 3.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 159 TQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQ----------KDYWE- 227
Cdd:COG3883   28 LQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERaralyrsggsVSYLDv 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 228 -------TELL-------QLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSL 293
Cdd:COG3883  108 llgsesfSDFLdrlsalsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQL 187

                        170       180       190
                 ....*....|....*....|....*....|.
gi 386869294 294 TEQRKD-QKKLEQTVEQMKQNETTAMKKQQE 323
Cdd:COG3883  188 SAEEAAaEAQLAELEAELAAAEAAAAAAAAA 218
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 149-362 4.28e-07

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: 52.67  E-value: 4.28e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   149 ENEEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVK--EQKDYW 226
Cdd:pfam02463  807 EEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEEleEQKLKD 886

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   227 ETELLQLKEQNQKMSSENEKmgiRVDQLQAQLSTQEKEMEKLvqgdqdktEQLEQLKKENDHLFLSLtEQRKDQKKLEQT 306
Cdd:pfam02463  887 ELESKEEKEKEEKKELEEES---QKLNLLEEKENEIEERIKE--------EAEILLKYEEEPEELLL-EEADEKEKEENN 954

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 386869294   307 VEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRE 362
Cdd:pfam02463  955 KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRA 1010
COG5022 COG5022
Myosin heavy chain [General function prediction only];
159-360 4.40e-07

Myosin heavy chain [General function prediction only];


Pssm-ID: 227355 [Multi-domain]  Cd Length: 1463  Bit Score: 52.77  E-value: 4.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  159 TQGEVEEIEQ-HNKELCKENQELKDSCislqKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQ----- 232
Cdd:COG5022   887 LKIDVKSISSlKLVNLELESEIIELKK----SLSSDLIENLEFKTELIARLKKLLNNIDLEEGPSIEYVKLPELNklhev 962

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  233 ---LKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQG------DQDKTEQLEQLKKENDHLflslteqrkdqkkl 303
Cdd:COG5022   963 eskLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELskqygaLQESTKQLKELPVEVAEL-------------- 1028

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 386869294  304 eQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLK 360
Cdd:COG5022  1029 -QSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLY 1084
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 160-368 7.42e-07

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: 51.43  E-value: 7.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  160 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETellqLKEQNQK 239
Cdd:pfam07888  72 ERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKT----LTQRVLE 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  240 MSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMK 319
Cdd:pfam07888 148 RETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHR 227

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 386869294  320 KQqelmdenfdlskrlSENEIICNALQRQKERL---EGENDLLKRENSRLLS 368
Cdd:pfam07888 228 KE--------------AENEALLEELRSLQERLnasERKVEGLGEELSSMAA 265
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-357 8.29e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 51.48  E-value: 8.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 160 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSinkKLELKVKEQKDYWETELLQLKEQNQK 239
Cdd:COG1196  322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA---ELAEAEEELEELAEELLEALRAAAEL 398

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 240 MSsenekmgiRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMK 319
Cdd:COG1196  399 AA--------QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 386869294 320 KQQELMDENFDLSKRLSENEIICNALQRQKERLEGEND 357
Cdd:COG1196  471 EAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLE 508
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 159-352 1.02e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.60  E-value: 1.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   159 TQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLElkvkEQKDYWETELLQLKEQNQ 238
Cdd:TIGR02168  773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE----RRIAATERRLEDLEEQIE 848

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   239 KMSSENEKmgirvdqLQAQLSTQEKEMEKLvqgdqdkTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAM 318
Cdd:TIGR02168  849 ELSEDIES-------LAAEIEELEELIEEL-------ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914

                          170       180       190
                   ....*....|....*....|....*....|....
gi 386869294   319 KKQQELMDENFDLSKRLSENEiicNALQRQKERL 352
Cdd:TIGR02168  915 RELEELREKLAQLELRLEGLE---VRIDNLQERL 945
PTZ00121 PTZ00121
MAEBL; Provisional
 151-357 1.32e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 51.30  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  151 EEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQnsdmQAELQKKQEELETLQSIN--KKLELKVKEQKDYWET 228
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKK----EAEEKKKAEELKKAEEENkiKAAEEAKKAEEDKKKA 1677

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  229 ELLQLKEQNQKMSSENEKmgirvdqlqaQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVE 308
Cdd:PTZ00121 1678 EEAKKAEEDEKKAAEALK----------KEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAE 1747

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 386869294  309 QMKQNETTAMKKQQELMDENFDLSKRLSENE-IICNALQRQKERLEGEND 357
Cdd:PTZ00121 1748 EAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEaVIEEELDEEDEKRRMEVD 1797
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 158-357 1.82e-06

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: 50.56  E-value: 1.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   158 TTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELK-VKEQKDY--WETELLQLK 234
Cdd:pfam01576  395 TLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKnIKLSKDVssLESQLQDTQ 474

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   235 EQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEqlkkendhlflSLTEQRKD-QKKLEQTVEQMKQN 313
Cdd:pfam01576  475 ELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLS-----------TLQAQLSDmKKKLEEDAGTLEAL 543

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 386869294   314 ETTAMKKQQELMdenfDLSKRLSENEIICNALQRQKERLEGEND 357
Cdd:pfam01576  544 EEGKKRLQRELE----ALTQQLEEKAAAYDKLEKTKNRLQQELD 583
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 149-353 2.21e-06

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 50.44  E-value: 2.21e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   149 ENEEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWET 228
Cdd:TIGR02168  721 LEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA 800

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   229 ELLQLKEQNQKMSSENEKMG---IRVDQLQAQLSTQEKEMEKLVQgdqdkteQLEQLKKENDHLFLSLTEQRKDQKKLEQ 305
Cdd:TIGR02168  801 LREALDELRAELTLLNEEAAnlrERLESLERRIAATERRLEDLEE-------QIEELSEDIESLAAEIEELEELIEELES 873

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 386869294   306 TVE-------QMKQNETTAMKKQQELMDENFDLSKRLSENEiicNALQRQKERLE 353
Cdd:TIGR02168  874 ELEallneraSLEEALALLRSELEELSEELRELESKRSELR---RELEELREKLA 925
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 149-375 3.29e-06

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: 49.66  E-value: 3.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   149 ENEEDILVVTTQGEVEEIEQHNKELckenQELKDScisLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKD---- 224
Cdd:TIGR00606  722 EKRRDEMLGLAPGRQSIIDLKEKEI----PELRNK---LQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDvtim 794

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   225 ---YWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQG-------DQDKTEQLEQLKKENDHL---FL 291
Cdd:TIGR00606  795 erfQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKielnrklIQDQQEQIQHLKSKTNELkseKL 874

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   292 SLTEQRKDQKKL-EQTVEQMKQ----NETTAMKKQQELMDENFdLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 366
Cdd:TIGR00606  875 QIGTNLQRRQQFeEQLVELSTEvqslIREIKDAKEQDSPLETF-LEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNI 953


                   ....*....
gi 386869294   367 LSYMGLDFN 375
Cdd:TIGR00606  954 HGYMKDIEN 962
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
144-370 4.00e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 48.75  E-value: 4.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 144 FQFRPENEEDILVV--TTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDM---QAELQKKQEEletLQSINKKLELK 218
Cdd:COG4372   16 FGLRPKTGILIAALseQLRKALFELDKLQEELEQLREELEQAREELEQLEEELeqaRSELEQLEEE---LEELNEQLQAA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 219 VKEQKDYwETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRK 298
Cdd:COG4372   93 QAELAQA-QEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386869294 299 DQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLSYM 370
Cdd:COG4372  172 ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
SHE3 pfam17078
SWI5-dependent HO expression protein 3; SWI5-dependent HO expression protein 3 (She3) is an ...
 163-314 5.76e-06

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: 47.43  E-value: 5.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  163 VEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSS 242
Cdd:pfam17078  68 LKDLEDQLSELKNSYEELTESNKQLKKRLENSSASETTLEAELERLQIQYDALVDSQNEYKDHYQQEINTLQESLEDLKL 147

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386869294  243 ENEKmgiRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNE 314
Cdd:pfam17078 148 ENEK---QLENYQQRISSNDKDIDTKLDSYNNKFKNLDNIYVNKNNKLLTKLDSLAQLLDLPSWLNLYPESR 216
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 131-357 5.80e-06

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: 48.97  E-value: 5.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  131 VDEDGVVRGASIPFQFRPENEEDILVVTTQGEVEEIEQHNKElcKENQELKDSCISLQ----KQNSDMQAELQKKQEELE 206
Cdd:pfam17380 318 LEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERK--RELERIRQEEIAMEisrmRELERLQMERQQKNERVR 395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  207 TLQSINKKLELKVKEQkdywETELLQLKEQNQKMSSENEKMgiRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKEN 286
Cdd:pfam17380 396 QELEAARKVKILEEER----QRKIQQQKVEMEQIRAEQEEA--RQREVRRLEEERAREMERVRLEEQERQQQVERLRQQE 469

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386869294  287 DHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLS-ENEIICNALQRQKERLEGEND 357
Cdd:pfam17380 470 EERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEkEMEERQKAIYEEERRREAEEE 541
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 162-368 8.73e-06

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.09  E-value: 8.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  162 EVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELEtlqsiNKKLELKVKEQkdywetELLQLKEQNQKMS 241
Cdd:TIGR04523 441 EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLE-----QKQKELKSKEK------ELKKLNEEKKELE 509

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  242 SENEKMgirvDQLQAQLSTQEKEMEKLVQGDQDKTEQLE-QLKKENDHLFLSLTEQRKDQKklEQTVEQMKQNETTAMKK 320
Cdd:TIGR04523 510 EKVKDL----TKKISSLKEKIEKLESEKKEKESKISDLEdELNKDDFELKKENLEKEIDEK--NKEIEELKQTQKSLKKK 583

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 386869294  321 Q-------QELMDENFDLSKRLSENEIicnalqrQKERLEGENDLLKRENSRLLS 368
Cdd:TIGR04523 584 QeekqeliDQKEKEKKDLIKEIEEKEK-------KISSLEKELEKAKKENEKLSS 631
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 140-353 1.00e-05

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: 48.04  E-value: 1.00e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   140 ASIPFQFRPENEEDILVvttQGEVEEIEQHNKELCKENQELKdscislQKQNSDMQAELQKKQEELETLQSINKKLELKV 219
Cdd:pfam02463  148 AMMKPERRLEIEEEAAG---SRLKRKKKEALKKLIEETENLA------ELIIDLEELKLQELKLKEQAKKALEYYQLKEK 218

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   220 KEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKD 299
Cdd:pfam02463  219 LELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEEL 298

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 386869294   300 QKKLEQTveqmKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLE 353
Cdd:pfam02463  299 KSELLKL----ERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELE 348
PTZ00121 PTZ00121
MAEBL; Provisional
 162-362 1.02e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 1.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  162 EVEEIEQHNKELCKENQELK-------------DSCISLQKQNSDMQAELQKKQEElETLQSINKKLELKVKEQKDYWET 228
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRkaeeakkaeeariEEVMKLYEEEKKMKAEEAKKAEE-AKIKAEELKKAEEEKKKVEQLKK 1640

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  229 ELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDhlflsltEQRKdqkkleqtVE 308
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE-------EAKK--------AE 1705

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 386869294  309 QMKQNETTAMKKQQELMDENfdlskrlSENEIICNALQRQKERLEGENDLLKRE 362
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAE-------EENKIKAEEAKKEAEEDKKKAEEAKKD 1752
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 153-366 1.32e-05

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 47.81  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  153 DILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQE-ELETLQSINKKLELKVKEQK----DYWE 227
Cdd:pfam05557 124 ELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKElEFEIQSQEQDSEIVKNSKSElariPELE 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  228 TELLQLKEQNQKMSSENEKMGI---RVDQLQAQLSTQEKEMEKLVQGDQDKtEQLEQLKKENDHLFLSLTEQRKDQKKLE 304
Cdd:pfam05557 204 KELERLREHNKHLNENIENKLLlkeEVEDLKRKLEREEKYREEAATLELEK-EKLEQELQSWVKLAQDTGLNLRSPEDLS 282

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386869294  305 QTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 366
Cdd:pfam05557 283 RRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRL 344
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
195-366 1.32e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.99  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  195 QAELQKKQEELETLQSINKKLELKVKEQK-DYWETELLQLKEqnqkmssENEKMGIRVDQLQAQLSTQEKEMEKL-VQGD 272
Cdd:COG4913   261 AERYAAARERLAELEYLRAALRLWFAQRRlELLEAELEELRA-------ELARLEAELERLEARLDALREELDELeAQIR 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  273 QDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMK-------------QNETTAMK-----KQQELMDENFDLSKR 334
Cdd:COG4913   334 GNGGDRLEQLEREIERLERELEERERRRARLEALLAALGlplpasaeefaalRAEAAALLealeeELEALEEALAEAEAA 413

                         170       180       190
                  ....*....|....*....|....*....|..
gi 386869294  335 LSEneiicnaLQRQKERLEGENDLLKRENSRL 366
Cdd:COG4913   414 LRD-------LRRELRELEAEIASLERRKSNI 438
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
164-341 1.80e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 164 EEIEQHNKELcKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELL---------QLK 234
Cdd:COG4717   71 KELKELEEEL-KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALeaelaelpeRLE 149

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 235 EQNQKMSSENEKMgIRVDQLQAQLSTQEKEMEKLVQGDQDKTE-QLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQN 313
Cdd:COG4717  150 ELEERLEELRELE-EELEELEAELAELQEELEELLEQLSLATEeELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228

                        170       180
                 ....*....|....*....|....*...
gi 386869294 314 EttamkKQQELMDENFDLSKRLSENEII 341
Cdd:COG4717  229 L-----EQLENELEAAALEERLKEARLL 251
Zn-C2H2_CALCOCO1_TAX1BP1_like cd21965
autophagy receptor zinc finger-C2H2 domain found in calcium-binding and coiled-coil ...
 443-465 2.03e-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: 41.02  E-value: 2.03e-05
                         10        20
                 ....*....|....*....|....
gi 386869294 443 CPICDKIFPATEKQ-IFEDHVFCH 465
Cdd:cd21965    1 CPICNKQFPPQVDQeAFEDHVESH 24
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 159-323 2.22e-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: 2.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   159 TQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELET----LQSINKKLElKVKEQKDYWETELLQLK 234
Cdd:TIGR02169  334 LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAEtrdeLKDYREKLE-KLKREINELKRELDRLQ 412

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   235 EQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLK----KENDHLFLSLTEQRKDQKKLEQTVEQM 310
Cdd:TIGR02169  413 EELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAadlsKYEQELYDLKEEYDRVEKELSKLQREL 492

                          170
                   ....*....|...
gi 386869294   311 KQNETTAMKKQQE 323
Cdd:TIGR02169  493 AEAEAQARASEER 505
PRK12704 PRK12704
phosphodiesterase; Provisional
 175-347 2.65e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 46.69  E-value: 2.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 175 KENQELKDSCIS-----LQKQNSDMQAELQKKQEELetlqsinKKLELKVKEQKDYWETELlqlkEQNQKMSSENEKMGI 249
Cdd:PRK12704  49 KEAEAIKKEALLeakeeIHKLRNEFEKELRERRNEL-------QKLEKRLLQKEENLDRKL----ELLEKREEELEKKEK 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 250 RVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKEndhlflsltEQRKDQkkLEQTVEQMKQnETTAMKKQQElmDENF 329
Cdd:PRK12704 118 ELEQKQQELEKKEEELEELIEEQLQELERISGLTAE---------EAKEIL--LEKVEEEARH-EAAVLIKEIE--EEAK 183

                        170
                 ....*....|....*...
gi 386869294 330 DLSKRLSeNEIICNALQR 347
Cdd:PRK12704 184 EEADKKA-KEILAQAIQR 200
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 164-368 3.11e-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: 46.55  E-value: 3.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  164 EEIEQHNKELCKENQELK---DSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKdyweTELLQLKEQ---- 236
Cdd:TIGR04523 232 DNIEKKQQEINEKTTEISntqTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLK----SEISDLNNQkeqd 307

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  237 -NQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLvqgdqdkTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNET 315
Cdd:TIGR04523 308 wNKELKSELKNQEKKLEEIQNQISQNNKIISQL-------NEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQ 380

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 386869294  316 TAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLS 368
Cdd:TIGR04523 381 SYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKE 433
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 164-317 3.11e-05

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 45.98  E-value: 3.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 164 EEIEQHNKELCKENQELKDSCISLQKQ-----------NSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQ 232
Cdd:COG3883   72 AEIAEAEAEIEERREELGERARALYRSggsvsyldvllGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAE 151

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 233 LKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQ 312
Cdd:COG3883  152 LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231


                 ....*
gi 386869294 313 NETTA 317
Cdd:COG3883  232 AAAAA 236
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 160-285 3.76e-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: 46.21  E-value: 3.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   160 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLEL---------KVKEQKDYWETEL 230
Cdd:TIGR02169  888 KKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipeeelsleDVQAELQRVEEEI 967

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 386869294   231 LQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLvqgdQDKTEQLEQLKKE 285
Cdd:TIGR02169  968 RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAI----LERIEEYEKKKRE 1018
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 155-312 3.96e-05

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 45.98  E-value: 3.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 155 LVVTTQGEVEEIEQHNKELCKENQELKDscISLQKQNSDMQAELQKKQEELETL---------QSINKKLEL-------- 217
Cdd:PRK04778 224 LQTELPDQLQELKAGYRELVEEGYHLDH--LDIEKEIQDLKEQIDENLALLEELdldeaeeknEEIQERIDQlydilere 301

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 218 -----KVKEQKDYWETELLQLKEQNQKMSSE----------NEKMGIRVDQLQAQLSTQEKEMEKLVQ--GDQDKT---- 276
Cdd:PRK04778 302 vkarkYVEKNSDTLPDFLEHAKEQNKELKEEidrvkqsytlNESELESVRQLEKQLESLEKQYDEITEriAEQEIAysel 381

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 386869294 277 --------EQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQ 312
Cdd:PRK04778 382 qeeleeilKQLEEIEKEQEKLSEMLQGLRKDELEAREKLERYRN 425
PTZ00121 PTZ00121
MAEBL; Provisional
 162-362 4.40e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 46.29  E-value: 4.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  162 EVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWE-----TELLQLKE- 235
Cdd:PTZ00121 1484 KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADelkkaEELKKAEEk 1563

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  236 ---QNQKMSSENEKMGIRVDQLQAQLSTQEKEmEKLVQGDQDKTEQLEQLKKENDHLFLSltEQRKDQKKLEQTVEQMKQ 312
Cdd:PTZ00121 1564 kkaEEAKKAEEDKNMALRKAEEAKKAEEARIE-EVMKLYEEEKKMKAEEAKKAEEAKIKA--EELKKAEEEKKKVEQLKK 1640

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 386869294  313 NETTAMKKQQELMDENfdlskrlSENEIICNALQRQKERLEGENDLLKRE 362
Cdd:PTZ00121 1641 KEAEEKKKAEELKKAE-------EENKIKAAEEAKKAEEDKKKAEEAKKA 1683
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 151-368 5.66e-05

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: 45.73  E-value: 5.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   151 EEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEE-------LETLQSINKKLELKVKEQK 223
Cdd:pfam02463  223 EEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEeekekklQEEELKLLAKEEEELKSEL 302

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   224 DYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLflsltEQRKDQKKL 303
Cdd:pfam02463  303 LKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL-----EQLEEELLA 377

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386869294   304 EQTVEQmKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRLLS 368
Cdd:pfam02463  378 KKKLES-ERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIEL 441
Tropomyosin_1 pfam12718
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ...
 160-312 6.01e-05

Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.


Pssm-ID: 403808 [Multi-domain]  Cd Length: 142  Bit Score: 43.06  E-value: 6.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  160 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQkkqeeletlqsinkKLELKVKEQKdywetellQLKEQNQK 239
Cdd:pfam12718  13 QERAEELEEKVKELEQENLEKEQEIKSLTHKNQQLEEEVE--------------KLEEQLKEAK--------EKAEESEK 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386869294  240 MSSENEKMGIRVDQLQAQLSTQEKE----MEKLVQGDQdKTEQLEQLKKendhlflSLTEQR-KDQKKLEQTVEQMKQ 312
Cdd:pfam12718  71 LKTNNENLTRKIQLLEEELEESDKRlketTEKLRETDV-KAEHLERKVQ-------ALEQERdEWEKKYEELEEKYKE 140
DUF4175 pfam13779
Domain of unknown function (DUF4175);
178-332 6.60e-05

Domain of unknown function (DUF4175);


Pssm-ID: 463981 [Multi-domain]  Cd Length: 833  Bit Score: 45.36  E-value: 6.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  178 QELKDScisLQKQNSDmqAELQKKQEELEtlQSINKKL-ELKvkEQKDYWETELLQLKEQNQKMssenekmgIRVDQLQA 256
Cdd:pfam13779 496 ERLSEA---LERGASD--EEIAKLMQELR--EALDDYMqALA--EQAQQNPQDLQQPDDPNAQE--------MTQQDLQR 558

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386869294  257 QLstqeKEMEKLVQ-GDQDKTEQ-LEQLKKENDHLFLSLTEQRKDQKKlEQTVEQMKQNETTaMKKQQELMDENFDLS 332
Cdd:pfam13779 559 ML----DRIEELARsGRRAEAQQmLSQLQQMLENLQAGQPQQQQQQGQ-SEMQQAMDELGDL-LREQQQLLDETFRQL 630
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 158-353 7.05e-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: 45.43  E-value: 7.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   158 TTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVK---EQKDYWETELLQLK 234
Cdd:TIGR02168  814 LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEallNERASLEEALALLR 893

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   235 EQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVqgdqdktEQLEQLKKENDHLFLSLTEQRKDqkkleqTVEQMKQNE 314
Cdd:TIGR02168  894 SELEELSEELRELESKRSELRRELEELREKLAQLE-------LRLEGLEVRIDNLQERLSEEYSL------TLEEAEALE 960

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 386869294   315 TTAMKKQQELMDENFDLSKRLSE----NEIICNALQRQKERLE 353
Cdd:TIGR02168  961 NKIEDDEEEARRRLKRLENKIKElgpvNLAAIEEYEELKERYD 1003
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 241-364 7.75e-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: 45.43  E-value: 7.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   241 SSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKK 320
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKE 755

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 386869294   321 QQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENS 364
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK 799
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
196-364 8.48e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 45.14  E-value: 8.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 196 AELQKKQEELETLQSINKKLElKVKEQKDYWETELLQLKEQNQKMSSENEKMgirvdQLQAQLSTQEKEMEKLVQGDQDK 275
Cdd:COG4717   71 KELKELEEELKEAEEKEEEYA-ELQEELEELEEELEELEAELEELREELEKL-----EKLLQLLPLYQELEALEAELAEL 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 276 TEQLEQLKKEND---HLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQ--------QELMDENFDLSKRLSENEIICNA 344
Cdd:COG4717  145 PERLEELEERLEelrELEEELEELEAELAELQEELEELLEQLSLATEEElqdlaeelEELQQRLAELEEELEEAQEELEE 224

                        170       180
                 ....*....|....*....|
gi 386869294 345 LQRQKERLEGENDLLKRENS 364
Cdd:COG4717  225 LEEELEQLENELEAAALEER 244
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 162-339 1.00e-04

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: 45.04  E-value: 1.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   162 EVEEIEQHNKELCKENQELKDScisLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYW----ETEL----LQL 233
Cdd:TIGR00606  910 QDSPLETFLEKDQQEKEELISS---KETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDGKDDYlkqkETELntvnAQL 986

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   234 KEQNQKMSSENEKMGIRVDQLQAQlstqeKEMEKLVQGD------QDKTEQLEQLKKENDHLF--LSLTEQRKDQKKLEQ 305
Cdd:TIGR00606  987 EECEKHQEKINEDMRLMRQDIDTQ-----KIQERWLQDNltlrkrENELKEVEEELKQHLKEMgqMQVLQMKQEHQKLEE 1061

                          170       180       190
                   ....*....|....*....|....*....|....
gi 386869294   306 TVEQMKQNETTAMKKQQELMDENFDLSKRLSENE 339
Cdd:TIGR00606 1062 NIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 145-364 1.16e-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: 44.71  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  145 QFRPENEEDILVVTT------QGEVEEIEQ--HNKELckENQELK------DSCISLQKQNSDMQAELQKKQEELETLQS 210
Cdd:pfam05483 369 QQRLEKNEDQLKIITmelqkkSSELEEMTKfkNNKEV--ELEELKkilaedEKLLDEKKQFEKIAEELKGKEQELIFLLQ 446

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  211 INKK----LELK--------------VKEQKDYWETELLQLKE----------QNQKMSSENEKMGIRVDQLQAQLSTQE 262
Cdd:pfam05483 447 AREKeihdLEIQltaiktseehylkeVEDLKTELEKEKLKNIEltahcdklllENKELTQEASDMTLELKKHQEDIINCK 526

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  263 KEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQK-KLEQTVEQMKQNETTAMKKQqelmdenfdlsKRLSENEII 341
Cdd:pfam05483 527 KQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKcKLDKSEENARSIEYEVLKKE-----------KQMKILENK 595

                         250       260       270
                  ....*....|....*....|....*....|
gi 386869294  342 CNALQRQK-------ERLEGENDLLKRENS 364
Cdd:pfam05483 596 CNNLKKQIenknkniEELHQENKALKKKGS 625
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
164-366 1.16e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 44.65  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 164 EEIEQhnkelcKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWEtELLQLKEQnqkmsse 243
Cdd:PRK02224 194 AQIEE------KEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERRE-ELETLEAE------- 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 244 nekmgirVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAmkkQQE 323
Cdd:PRK02224 260 -------IEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEEL---RDR 329

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 386869294 324 LMDENFDLSKRLSENEiicnALQRQKERLEGENDLLKRENSRL 366
Cdd:PRK02224 330 LEECRVAAQAHNEEAE----SLREDADDLEERAEELREEAAEL 368
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
164-354 1.33e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.67  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 164 EEIEQHNKELCKENQELKdsciSLQKQNSDMQAELQKKQEELETLQSINKKLElKVKEQKDYWET---ELLQLKEQNQKM 240
Cdd:PRK03918 238 EEIEELEKELESLEGSKR----KLEEKIRELEERIEELKKEIEELEEKVKELK-ELKEKAEEYIKlseFYEEYLDELREI 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 241 SSENEKMGIRVDQLQAQLSTQE------KEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLE-QTVEQMKQN 313
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEekeerlEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTgLTPEKLEKE 392

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 386869294 314 ETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEG 354
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKK 433
TACC_C pfam05010
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ...
 218-326 1.36e-04

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: 42.74  E-value: 1.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  218 KVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQ---AQLSTQEKEMEKLVQGDQDKT-EQLEQLKKENDHLFLSL 293
Cdd:pfam05010  12 KARNEIEEKELEINELKAKYEELRRENLEMRKIVAEFEktiAQMIEEKQKQKELEHAEIQKVlEEKDQALADLNSVEKSF 91

                          90       100       110
                  ....*....|....*....|....*....|...
gi 386869294  294 TEQRKDQKKLEQTVEQMKQNETTAMKKQQELMD 326
Cdd:pfam05010  92 SDLFKRYEKQKEVISGYKKNEESLKKCAQDYLA 124
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
171-359 1.41e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 171 KELCKENQELKDScislQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDyweteLLQLKEQNQKMSSENEKMGIR 250
Cdd:COG4717   74 KELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELEKLEK-----LLQLLPLYQELEALEAELAEL 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 251 VDQLQaQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQ-KKLEQTVEQMKQNETTAMKKQQELMDENF 329
Cdd:COG4717  145 PERLE-ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELE 223

                        170       180       190
                 ....*....|....*....|....*....|
gi 386869294 330 DLSKRLSENEIICNALQRQKERLEGENDLL 359
Cdd:COG4717  224 ELEEELEQLENELEAAALEERLKEARLLLL 253
mukB PRK04863
chromosome partition protein MukB;
190-373 1.54e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 44.56  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  190 QNSDMQAELQKKQEELETLQSinkKLELKVKEQKDywetellQLKEQNQKMSSENEkmgiRVDQLQAQLSTQEKEMEKL- 268
Cdd:PRK04863  982 KNSDLNEKLRQRLEQAEQERT---RAREQLRQAQA-------QLAQYNQVLASLKS----SYDAKRQMLQELKQELQDLg 1047

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  269 VQGDQDKTEQLEQLKKENDHLfLSLTEQRKDQKKLEQTVEQMkqnETTAMKKQQELMDENFDLSKRLSENE--IICNALq 346
Cdd:PRK04863 1048 VPADSGAEERARARRDELHAR-LSANRSRRNQLEKQLTFCEA---EMDNLTKKLRKLERDYHEMREQVVNAkaGWCAVL- 1122

                         170       180
                  ....*....|....*....|....*..
gi 386869294  347 rqkeRLEGENDLLKRENSRLLSYMGLD 373
Cdd:PRK04863 1123 ----RLVKDNGVERRLHRRELAYLSAD 1145
Leu_zip pfam15294
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ...
 160-284 1.58e-04

Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).


Pssm-ID: 464620 [Multi-domain]  Cd Length: 276  Bit Score: 43.54  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  160 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEEL-------ETLQSINKkLELKVKEQKDYWETELLQ 232
Cdd:pfam15294 132 HMEIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQgakkdvkSNLKEISD-LEEKMAALKSDLEKTLNA 210

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386869294  233 LKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGD----------QDKTEQLEQLKK 284
Cdd:pfam15294 211 STALQKSLEEDLASTKHELLKVQEQLEMAEKELEKKFQQTaayrnmkemlTKKNEQIKELRK 272
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
187-386 1.64e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  187 LQKQNSDMQAELQKKQEELETLQSinkklELKVKEQKdywETELLQLKEQNQkmssenekmGIRVDQLQAQLSTQEKEME 266
Cdd:COG4913   293 LEAELEELRAELARLEAELERLEA-----RLDALREE---LDELEAQIRGNG---------GDRLEQLEREIERLERELE 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  267 KLVQgdqdkteQLEQLKKENDHLFLSLTEQRKD----QKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSE--NEI 340
Cdd:COG4913   356 ERER-------RRARLEALLAALGLPLPASAEEfaalRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREleAEI 428

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 386869294  341 icNALQRQKERLEGENDLLKREnsrLLSYMGLDFNSLPY-----QVPTSDE 386
Cdd:COG4913   429 --ASLERRKSNIPARLLALRDA---LAEALGLDEAELPFvgeliEVRPEEE 474
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 149-321 1.65e-04

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: 44.34  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   149 ENEEDILVVTTQGEVEE-IEQHNKELCKenqeLKDSCISLQKQNSDMQAELQKKQEE-----------LETLQSINKKLE 216
Cdd:pfam15921  255 QNKIELLLQQHQDRIEQlISEHEVEITG----LTEKASSARSQANSIQSQLEIIQEQarnqnsmymrqLSDLESTVSQLR 330

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   217 LKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVqGDQDKTEQLEQLKKEN---------- 286
Cdd:pfam15921  331 SELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLL-ADLHKREKELSLEKEQnkrlwdrdtg 409

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 386869294   287 -----DHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQ 321
Cdd:pfam15921  410 nsitiDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQ 449
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 164-355 1.89e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.29  E-value: 1.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   164 EEIEQHNKEL--CKENQELKDSCISLQKQNSDmqaELQKKQEELETLQSINKKLElkvkeqkDYWETELLqlkeqNQKMS 241
Cdd:TIGR02169  170 RKKEKALEELeeVEENIERLDLIIDEKRQQLE---RLRREREKAERYQALLKEKR-------EYEGYELL-----KEKEA 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   242 SENEKmgirvDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLF-----LSLTEQRKDQKKLEQTVEQMKQNETT 316
Cdd:TIGR02169  235 LERQK-----EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNkkikdLGEEEQLRVKEKIGELEAEIASLERS 309

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 386869294   317 AMKKQQELMdenfDLSKRLSENEIICNALQRQKERLEGE 355
Cdd:TIGR02169  310 IAEKERELE----DAEERLAKLEAEIDKLLAEIEELERE 344
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 165-312 2.01e-04

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: 43.95  E-value: 2.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   165 EIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLElKVKEQKDYWETELLQlkeqnQKMSSEN 244
Cdd:pfam15921  420 ELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLE-STKEMLRKVVEELTA-----KKMTLES 493

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   245 EKMgiRVDQLQAQLSTQEK-------EMEKLVQGDQDKTEQLEQLKKENDHLF----------LSLTEQRKDQKKLEQTV 307
Cdd:pfam15921  494 SER--TVSDLTASLQEKERaieatnaEITKLRSRVDLKLQELQHLKNEGDHLRnvqtecealkLQMAEKDKVIEILRQQI 571


                   ....*
gi 386869294   308 EQMKQ 312
Cdd:pfam15921  572 ENMTQ 576
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
187-366 2.04e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 2.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 187 LQKQNSDMQAELQKKQEELETLQSINKKLELkvKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEME 266
Cdd:COG3206  180 LEEQLPELRKELEEAEAALEEFRQKNGLVDL--SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALP 257

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 267 KLVQGD--QDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNettamkKQQElmdenfdLSKRLSENEIICNA 344
Cdd:COG3206  258 ELLQSPviQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQ------LQQE-------AQRILASLEAELEA 324

                        170       180
                 ....*....|....*....|..
gi 386869294 345 LQRQKERLEGENDLLKRENSRL 366
Cdd:COG3206  325 LQAREASLQAQLAQLEARLAEL 346
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 155-333 2.25e-04

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: 43.95  E-value: 2.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   155 LVVTTQGEVEEIEQHNKELCK----------ENQELKDSCISLQKQNSDMQA---ELQKKQEELETL-QSINKKLEL--- 217
Cdd:pfam15921  501 LTASLQEKERAIEATNAEITKlrsrvdlklqELQHLKNEGDHLRNVQTECEAlklQMAEKDKVIEILrQQIENMTQLvgq 580

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   218 ------KVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFL 291
Cdd:pfam15921  581 hgrtagAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLN 660

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 386869294   292 SLTEQRKDQKKLEQTVEQMKQN--------ETTAMKKQQELMDENFDLSK 333
Cdd:pfam15921  661 EVKTSRNELNSLSEDYEVLKRNfrnkseemETTTNKLKMQLKSAQSELEQ 710
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 193-312 2.72e-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: 43.30  E-value: 2.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  193 DMQAELQKKQEELETLQSI-NKKLELK--VKEQKDYWETELLQLKEQNQKMSSE----------NEKMGIRVDQLQAQLS 259
Cdd:pfam06160 260 EAEEALEEIEERIDQLYDLlEKEVDAKkyVEKNLPEIEDYLEHAEEQNKELKEElervqqsytlNENELERVRGLEKQLE 339

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386869294  260 TQEKEMEKLVQGDQDKT--------------EQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQ 312
Cdd:pfam06160 340 ELEKRYDEIVERLEEKEvayselqeeleeilEQLEEIEEEQEEFKESLQSLRKDELEAREKLDEFKL 406
PRK12704 PRK12704
phosphodiesterase; Provisional
 195-327 3.36e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 3.36e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 195 QAELQKKQEELEtLQSINKKLELKVKEqkdywetELLQLKEQNQKMSSENEKmgiRVDQLQAQLSTQEKEMEKlvqgdqd 274
Cdd:PRK12704  39 EAKRILEEAKKE-AEAIKKEALLEAKE-------EIHKLRNEFEKELRERRN---ELQKLEKRLLQKEENLDR------- 100

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 386869294 275 KTEQLEQLKKEndhlflsLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDE 327
Cdd:PRK12704 101 KLELLEKREEE-------LEKKEKELEQKQQELEKKEEELEELIEEQLQELER 146
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 147-340 3.37e-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: 43.19  E-value: 3.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  147 RPENEEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEEletlQSINKKLELKvKEQKDYW 226
Cdd:pfam17380 413 RKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEE----ERKRKKLELE-KEKRDRK 487

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  227 ETELL-------QLKEQNQKMSSENEKMGIrvdqlqaqlstQEKEME---KLVQGDQDKTEQLEQLKKENDhlflsLTEQ 296
Cdd:pfam17380 488 RAEEQrrkilekELEERKQAMIEEERKRKL-----------LEKEMEerqKAIYEEERRREAEEERRKQQE-----MEER 551

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 386869294  297 RKDQKKLEQTVEQMKQNEttAMKKQQELMDENFDLSKRLSENEI 340
Cdd:pfam17380 552 RRIQEQMRKATEERSRLE--AMEREREMMRQIVESEKARAEYEA 593
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 159-325 3.58e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 43.27  E-value: 3.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  159 TQGEVEEIEQHNKELCKENQELKDSCISLQKQN-SDMQAELQKKQEELETLQSINKKLELKVKEQKDYWET--------- 228
Cdd:pfam10174  85 AQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENfRRLQSEHERQAKELFLLRKTLEEMELRIETQKQTLGArdesikkll 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  229 ELLQLKEQNQKMSSENEKMGIR-------VDQLQAQLSTQEKEMEKL---------VQGDQDKTEQLEQLKKENDHLFLS 292
Cdd:pfam10174 165 EMLQSKGLPKKSGEEDWERTRRiaeaemqLGHLEVLLDQKEKENIHLreelhrrnqLQPDPAKTKALQTVIEMKDTKISS 244

                         170       180       190
                  ....*....|....*....|....*....|...
gi 386869294  293 LTEQRKDqkkLEQTVEQMKQNETTAMKKQQELM 325
Cdd:pfam10174 245 LERNIRD---LEDEVQMLKTNGLLHTEDREEEI 274
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 162-312 3.73e-04

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: 43.24  E-value: 3.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   162 EVEEIEQhnkELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLEL-------KVKEQkdywETELLQLK 234
Cdd:pfam01576   72 ELEEILH---ELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLekvtteaKIKKL----EEDILLLE 144

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386869294   235 EQNQKMSSENEKMGIRVDQLQAQLSTQEkemeklvqgdqDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQ 312
Cdd:pfam01576  145 DQNSKLSKERKLLEERISEFTSNLAEEE-----------EKAKSLSKLKNKHEAMISDLEERLKKEEKGRQELEKAKR 211
CCDC14 pfam15254
Coiled-coil domain-containing protein 14; This protein family, Coiled-coil domain-containing ...
 167-264 3.77e-04

Coiled-coil domain-containing protein 14; This protein family, Coiled-coil domain-containing protein 14 (CCDC14) is a domain of unknown function. This family of proteins is found in eukaryotes. Proteins in this family are typically between 301 and 912 amino acids in length.


Pssm-ID: 464594  Cd Length: 857  Bit Score: 43.25  E-value: 3.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  167 EQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLeLKVKE-QKDY----------WETELLQLKE 235
Cdd:pfam15254 412 EQEKTEKTSGSGDCNLELFSLQSLNMSLQNQLQESLKSQELLQSKNEEL-LKVIEnQKEEnkkltkifkeKEQTLLENKQ 490

                          90       100       110
                  ....*....|....*....|....*....|...
gi 386869294  236 Q----NQKMSSENEKMGIRVDQLQAQLSTQEKE 264
Cdd:pfam15254 491 QfdieTTRVKIELEEALVNMKSFQFKLEAAEKE 523
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 159-366 3.93e-04

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: 43.24  E-value: 3.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   159 TQGEVEEIEQHNKELCKENQELKDSC---ISLQKQNSDMQAELQKKQEELEtlqSINKKLELKVKEQkdywetellqlKE 235
Cdd:pfam01576   24 AESELKELEKKHQQLCEEKNALQEQLqaeTELCAEAEEMRARLAARKQELE---EILHELESRLEEE-----------EE 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   236 QNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLvQGDQDKTEQleQLKKENDHLfLSLTEQR----KDQKKLEQTVEQMK 311
Cdd:pfam01576   90 RSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKL-QLEKVTTEA--KIKKLEEDI-LLLEDQNsklsKERKLLEERISEFT 165

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 386869294   312 QNET---------TAMKKQQELMDEnfDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 366
Cdd:pfam01576  166 SNLAeeeekakslSKLKNKHEAMIS--DLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAEL 227
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 162-356 4.14e-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: 4.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  162 EVEEIEQHNKELCKENQELKDSCiSLQKQNSDMQAELQKKQE------------------------ELETLQSINKKLEL 217
Cdd:pfam05483 135 KLEEEIQENKDLIKENNATRHLC-NLLKETCARSAEKTKKYEyereetrqvymdlnnniekmilafEELRVQAENARLEM 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  218 KVKEQKDYweTELLQLKEQNQKMSSENEKmgiRVDQLQAQLSTQEKEMEKL---VQGDQDKTEQLEQLKKENDHlflSLT 294
Cdd:pfam05483 214 HFKLKEDH--EKIQHLEEEYKKEINDKEK---QVSLLLIQITEKENKMKDLtflLEESRDKANQLEEKTKLQDE---NLK 285

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386869294  295 EQRKDQKKLEQTVEQMKQNETTAMKKQQELmDENFDLSKRlseneIICNALQRQKERLEGEN 356
Cdd:pfam05483 286 ELIEKKDHLTKELEDIKMSLQRSMSTQKAL-EEDLQIATK-----TICQLTEEKEAQMEELN 341
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 165-324 4.29e-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: 4.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 165 EIEQHNKELCKENQELKDscisLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDywetelLQLKEQNQKMSSEN 244
Cdd:COG1579   18 ELDRLEHRLKELPAELAE----LEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEA------RIKKYEEQLGNVRN 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 245 EKMgirVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKD----QKKLEQTVEQMKQNETTAMKK 320
Cdd:COG1579   88 NKE---YEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEleekKAELDEELAELEAELEELEAE 164


                 ....
gi 386869294 321 QQEL 324
Cdd:COG1579  165 REEL 168
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 165-350 4.31e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 43.03  E-value: 4.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   165 EIEQHNKELCKENQELkdsCISLQKQNSDMQAE---LQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMS 241
Cdd:TIGR00618  708 ELETHIEEYDREFNEI---ENASSSLGSDLAARedaLNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLA 784

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   242 SENEKMGIRVDQLQAQLSTQEKEM-EKLVQGDQDKTEQLEQLKKENDHLflsLTEQRKDQKKLEQTVEQMKQNETTaMKK 320
Cdd:TIGR00618  785 AEIQFFNRLREEDTHLLKTLEAEIgQEIPSDEDILNLQCETLVQEEEQF---LSRLEEKSATLGEITHQLLKYEEC-SKQ 860

                          170       180       190
                   ....*....|....*....|....*....|
gi 386869294   321 QQELMDENFDLSKRLSENEIIcNALQRQKE 350
Cdd:TIGR00618  861 LAQLTQEQAKIIQLSDKLNGI-NQIKIQFD 889
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 194-325 5.32e-04

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: 42.37  E-value: 5.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  194 MQAELQKKQ--EELETLQSINKKLELKVKEQKDYWETELLQLKEQNQK----MSSENEKMGIRVDQLQAQLstqeKEMEK 267
Cdd:pfam05622 271 LAAEIMPAEirEKLIRLQHENKMLRLGQEGSYRERLTELQQLLEDANRrkneLETQNRLANQRILELQQQV----EELQK 346

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386869294  268 LVQGDQDKTEQLEQLKKENDHLFLSLTE-QRKDQKKLEQTVEQMKQNETTAMKKQQELM 325
Cdd:pfam05622 347 ALQEQGSKAEDSSLLKQKLEEHLEKLHEaQSELQKKKEQIEELEPKQDSNLAQKIDELQ 405
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
130-284 5.58e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 42.54  E-value: 5.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 130 YVDED----GVVRGASI----------------PFQFRPENEEDILVVTTQGEVEEIEQHNKELCKENQELKDscislqk 189
Cdd:COG2433  362 DVDRDevkaRVIRGLSIeealeeliekelpeeePEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEA------- 434

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 190 qnsdmqaELQKKQEELEtlqsinkKLELKVKEQKdywetellqlKEQNQKMSSENE--KMGIRVDQLQAQLSTQEKEMEK 267
Cdd:COG2433  435 -------ELEEKDERIE-------RLERELSEAR----------SEERREIRKDREisRLDREIERLERELEEERERIEE 490

                        170
                 ....*....|....*..
gi 386869294 268 LvqgdQDKTEQLEQLKK 284
Cdd:COG2433  491 L----KRKLERLKELWK 503
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 178-368 5.89e-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: 41.45  E-value: 5.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 178 QELKDSCISLQKQNSDMQAELQKKQEELETLQsinKKLELKvkeqkdywETELLQLKEQNQKMSSENEKMGIRVDQLQAQ 257
Cdd:COG1579   13 QELDSELDRLEHRLKELPAELAELEDELAALE---ARLEAA--------KTELEDLEKEIKRLELEIEEVEARIKKYEEQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 258 LSTQ--EKEMEKLvqgdqdkTEQLEQLKKENDHLflslteqRKDQKKLEQTVEQMKQNETTAMKKQQELMDEnfdLSKRL 335
Cdd:COG1579   82 LGNVrnNKEYEAL-------QKEIESLKRRISDL-------EDEILELMERIEELEEELAELEAELAELEAE---LEEKK 144

                        170       180       190
                 ....*....|....*....|....*....|....
gi 386869294 336 SENEIICNALQRQKERLEGE-NDLLKRENSRLLS 368
Cdd:COG1579  145 AELDEELAELEAELEELEAErEELAAKIPPELLA 178
PTZ00121 PTZ00121
MAEBL; Provisional
 188-362 6.17e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 6.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  188 QKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWE---------------------TELLQLKEQNQKMSSEN-- 244
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEedknmalrkaeeakkaeeariEEVMKLYEEEKKMKAEEak 1613

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  245 --EKMGIRVDQLQAQlSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQ 322
Cdd:PTZ00121 1614 kaEEAKIKAEELKKA-EEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAE 1692

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 386869294  323 ELMDENFD------LSKRLSENEIICNALQRQKERLEGENDLLKRE 362
Cdd:PTZ00121 1693 ALKKEAEEakkaeeLKKKEAEEKKKAEELKKAEEENKIKAEEAKKE 1738
mukB PRK04863
chromosome partition protein MukB;
194-361 6.40e-04

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 42.64  E-value: 6.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  194 MQAELQKKQEELETLQS---INKKLELKVKEQKDYWeTELLQLK-----EQNQKMSSENekmgirvDQLQAQLStqekem 265
Cdd:PRK04863  926 IVSVLQSDPEQFEQLKQdyqQAQQTQRDAKQQAFAL-TEVVQRRahfsyEDAAEMLAKN-------SDLNEKLR------ 991

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  266 EKLVQGDQDKTEQLEQLKK------ENDHLFLSLTE--QRKDQ--KKLEQTVEQMKQNETTAMKKQQELMDEnfDLSKRL 335
Cdd:PRK04863  992 QRLEQAEQERTRAREQLRQaqaqlaQYNQVLASLKSsyDAKRQmlQELKQELQDLGVPADSGAEERARARRD--ELHARL 1069

                         170       180
                  ....*....|....*....|....*..
gi 386869294  336 SENEIICNALQRQKERLEGE-NDLLKR 361
Cdd:PRK04863 1070 SANRSRRNQLEKQLTFCEAEmDNLTKK 1096
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 164-362 6.81e-04

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: 42.47  E-value: 6.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   164 EEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSinkKLElkvkeqkdywetellqlKEQNQKMSSE 243
Cdd:pfam01576  204 QELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALA---RLE-----------------EETAQKNNAL 263

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   244 NekmgiRVDQLQAQLSTQEKEME-------KLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMK---QN 313
Cdd:pfam01576  264 K-----KIRELEAQISELQEDLEseraarnKAEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKkalEE 338

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   314 ETTAMKKQ-QEL----------MDENFDLSKRLSENeiicnaLQRQKERLEGENDLLKRE 362
Cdd:pfam01576  339 ETRSHEAQlQEMrqkhtqaleeLTEQLEQAKRNKAN------LEKAKQALESENAELQAE 392
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 164-311 7.46e-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: 41.06  E-value: 7.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 164 EEIEQHNKELckenQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELK---VKEQKDY--WETELLQLKEQNQ 238
Cdd:COG1579   31 AELAELEDEL----AALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnVRNNKEYeaLQKEIESLKRRIS 106

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 386869294 239 KMSSENEKMGIRVDQLQAQLSTQEKEMEKLvqgdqdkTEQLEQLKKENDhlfLSLTEQRKDQKKLEQTVEQMK 311
Cdd:COG1579  107 DLEDEILELMERIEELEEELAELEAELAEL-------EAELEEKKAELD---EELAELEAELEELEAEREELA 169
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 164-376 8.19e-04

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 42.12  E-value: 8.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  164 EEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQsinKKLElKVKEQKDYWETELLQLKEQNQKMSSE 243
Cdd:pfam10174 355 EEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVLQ---KKIE-NLQEQLRDKDKQLAGLKERVKSLQTD 430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  244 NEKMGIRVDQLQAQLSTQEKEMEKLVQ----GDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETT--- 316
Cdd:pfam10174 431 SSNTDTALTTLEEALSEKERIIERLKEqrerEDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSlas 510

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386869294  317 -AMKKQQELMDENFDLSKRLSEneiiCNALQRQkerlegendLLKRENSRLLSYMGLDFNS 376
Cdd:pfam10174 511 sGLKKDSKLKSLEIAVEQKKEE----CSKLENQ---------LKKAHNAEEAVRTNPEIND 558
46 PHA02562
endonuclease subunit; Provisional
 152-366 9.39e-04

endonuclease subunit; Provisional


Pssm-ID: 222878 [Multi-domain]  Cd Length: 562  Bit Score: 41.54  E-value: 9.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 152 EDILVVTTQGEVEEIeqhNKELCKE-NQELKDscISLQKQNSDMQAELQKK-QEELETLQSIN-KKLELKVkeqkdyweT 228
Cdd:PHA02562 157 EDLLDISVLSEMDKL---NKDKIRElNQQIQT--LDMKIDHIQQQIKTYNKnIEEQRKKNGENiARKQNKY--------D 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 229 ELLQlKEQNQKMSsenekmgirVDQLQAQLSTQEKEME-------KLVQGDQDKTEQLEQLKKEndHLFL-------SLT 294
Cdd:PHA02562 224 ELVE-EAKTIKAE---------IEELTDELLNLVMDIEdpsaalnKLNTAAAKIKSKIEQFQKV--IKMYekggvcpTCT 291

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386869294 295 EQRKDQ-KKLEQTVEQMKQNET------TAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 366
Cdd:PHA02562 292 QQISEGpDRITKIKDKLKELQHslekldTAIDELEEIMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEEL 370
PRK04778 PRK04778
septation ring formation regulator EzrA; Provisional
 198-362 1.03e-03

septation ring formation regulator EzrA; Provisional


Pssm-ID: 179877 [Multi-domain]  Cd Length: 569  Bit Score: 41.36  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 198 LQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSEN---EKMGI--RVDQLQAQLSTQEKEMEKLvqgD 272
Cdd:PRK04778 200 LDQLEEELAALEQIMEEIPELLKELQTELPDQLQELKAGYRELVEEGyhlDHLDIekEIQDLKEQIDENLALLEEL---D 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 273 QDKTE-QLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDE--NFDLSKRLSENEI-ICNALQRQ 348
Cdd:PRK04778 277 LDEAEeKNEEIQERIDQLYDILEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEEidRVKQSYTLNESELeSVRQLEKQ 356

                        170
                 ....*....|....
gi 386869294 349 KERLEGENDLLKRE 362
Cdd:PRK04778 357 LESLEKQYDEITER 370
PRK12705 PRK12705
hypothetical protein; Provisional
 189-350 1.16e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 41.23  E-value: 1.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 189 KQNSDMQAELQKKQEELET---LQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKmgirVDQLQAQLSTQEKEM 265
Cdd:PRK12705  39 LQEAQKEAEEKLEAALLEAkelLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEK----LDNLENQLEEREKAL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 266 EklvqgdqDKTEQLEQLKKENDHLFLSLTEQRKDQ------KKLEQTVEQMKQNETTAMKkqqelmdENFDLSKRLSENE 339
Cdd:PRK12705 115 S-------ARELELEELEKQLDNELYRVAGLTPEQarklllKLLDAELEEEKAQRVKKIE-------EEADLEAERKAQN 180

                        170
                 ....*....|.
gi 386869294 340 IICNALQRQKE 350
Cdd:PRK12705 181 ILAQAMQRIAS 191
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
163-362 1.17e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 163 VEEIEQHNKELckenQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLElKVKEQKDYWETELLQLkeqnqKMSS 242
Cdd:PRK03918 517 LEELEKKAEEY----EKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLD-ELEEELAELLKELEEL-----GFES 586

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 243 ENEkmgirVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHL---FLSLTEQRKDQKKLEQTVEQMKQNETTamK 319
Cdd:PRK03918 587 VEE-----LEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELdkaFEELAETEKRLEELRKELEELEKKYSE--E 659

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 386869294 320 KQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRE 362
Cdd:PRK03918 660 EYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEE 702
FtsL2 COG4839
Cell division protein FtsL [Cell cycle control, cell division, chromosome partitioning];
184-225 1.49e-03

Cell division protein FtsL [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443867  Cd Length: 123  Bit Score: 38.40  E-value: 1.49e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 386869294 184 CISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDY 225
Cdd:COG4839   57 LLSLQASIYELNREIQSLESKISEQQKENEDLEQEVSELSSP 98
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
 163-366 1.52e-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: 41.19  E-value: 1.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   163 VEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKE----------QKDYWETELLQ 232
Cdd:TIGR00606  669 ITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEmlglapgrqsIIDLKEKEIPE 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   233 LKEQNQKMSSENEKMGIRVDQLQAQLST--QEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQrKDQKKLEQTVEQM 310
Cdd:TIGR00606  749 LRNKLQKVNRDIQRLKNDIEEQETLLGTimPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAK-LQGSDLDRTVQQV 827

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 386869294   311 KQnettamkKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSRL 366
Cdd:TIGR00606  828 NQ-------EKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQI 876
CENP-F_leu_zip pfam10473
Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, ...
 158-258 1.52e-03

Leucine-rich repeats of kinetochore protein Cenp-F/LEK1; Cenp-F, a centromeric kinetochore, microtubule-binding protein consisting of two 1,600-amino acid-long coils, is essential for the full functioning of the mitotic checkpoint pathway. There are several leucine-rich repeats along the sequence of LEK1 that are considered to be zippers, though they do not appear to be binding DNA directly in this instance.


Pssm-ID: 463102 [Multi-domain]  Cd Length: 140  Bit Score: 38.82  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  158 TTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLElkvkeqkdywetELLQLKEqn 237
Cdd:pfam10473  49 NSKAEVETLKAEIEEMAQNLRDLELDLVTLRSEKENLTKELQKKQERVSELESLNSSLE------------NLLEEKE-- 114

                          90       100
                  ....*....|....*....|.
gi 386869294  238 QKMSSENEKMGIRVDQLQAQL 258
Cdd:pfam10473 115 QEKVQMKEESKTAVEMLQTQL 135
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
186-324 1.68e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 40.77  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 186 SLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDywETELLQLKEQNQKMSSENEKMGIR-------VDQLQAQL 258
Cdd:COG3206  223 ELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQ--SPVIQQLRAQLAELEAELAELSARytpnhpdVIALRAQI 300

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386869294 259 STQEKEMEKLVQGDQDKTE--------QLEQLKKENDHL---FLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQEL 324
Cdd:COG3206  301 AALRAQLQQEAQRILASLEaelealqaREASLQAQLAQLearLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
 198-360 1.68e-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: 40.61  E-value: 1.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  198 LQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSEN---EKMGI--RVDQLQAQLstqEKEMEKLVQGD 272
Cdd:pfam06160 181 LEKLEEETDALEELMEDIPPLYEELKTELPDQLEELKEGYREMEEEGyalEHLNVdkEIQQLEEQL---EENLALLENLE 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  273 QDKTEQ-LEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDE--NFDLSKRLSENEI-ICNALQRQ 348
Cdd:pfam06160 258 LDEAEEaLEEIEERIDQLYDLLEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEEleRVQQSYTLNENELeRVRGLEKQ 337

                         170
                  ....*....|..
gi 386869294  349 KERLEGENDLLK 360
Cdd:pfam06160 338 LEELEKRYDEIV 349
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
158-341 1.74e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 40.66  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 158 TTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQ- 236
Cdd:COG4372  105 SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQa 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 237 --NQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNE 314
Cdd:COG4372  185 ldELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264

                        170       180
                 ....*....|....*....|....*..
gi 386869294 315 TTAMKKQQELMDENFDLSKRLSENEII 341
Cdd:COG4372  265 LAILVEKDTEEEELEIAALELEALEEA 291
GBP_C pfam02841
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ...
 163-366 1.78e-03

Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.


Pssm-ID: 460721 [Multi-domain]  Cd Length: 297  Bit Score: 40.35  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  163 VEEIEQHNKELCKENQELKDSCIslqkqnsdmQAELQKKQEELET--LQSINKK-------LELKVKEQKDYWET--ELL 231
Cdd:pfam02841 102 VELLEAKKDDFLKQNEEASSKYC---------SALLQDLSEPLEEkiSQGTFSKpggyklfLEERDKLEAKYNQVprKGV 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  232 QLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKlvqgDQDKTEQLEQLKKEndhlflslteQRKDQKKLEQTVEQMK 311
Cdd:pfam02841 173 KAEEVLQEFLQSKEAVEEAILQTDQALTAKEKAIEA----ERAKAEAAEAEQEL----------LREKQKEEEQMMEAQE 238

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  312 QNETTAMKKQQELMDEnfDLSKRLSENE-IICNALQRQKERL-EG---ENDLLKRENSRL 366
Cdd:pfam02841 239 RSYQEHVKQLIEKMEA--EREQLLAEQErMLEHKLQEQEELLkEGfktEAESLQKEIQDL 296
Mod_r pfam07200
Modifier of rudimentary (Mod(r)) protein; This family represents a conserved region ...
 157-285 1.88e-03

Modifier of rudimentary (Mod(r)) protein; This family represents a conserved region approximately 150 residues long within a number of eukaryotic proteins that show homology with Drosophila melanogaster Modifier of rudimentary (Mod(r)) proteins. The N-terminal half of Mod(r) proteins is acidic, whereas the C-terminal half is basic, and both of these regions are represented in this family. Members of this family include the Vps37 subunit of the endosomal sorting complex ESCRT-I, a complex involved in recruiting transport machinery for protein sorting at the multivesicular body (MVB). The yeast ESCRT-I complex consists of three proteins (Vps23, Vps28 and Vps37). The mammalian homolog of Vps37 interacts with Tsg101 (Pfam: PF05743) through its mod(r) domain and its function is essential for lysosomal sorting of EGF receptors.


Pssm-ID: 462117 [Multi-domain]  Cd Length: 146  Bit Score: 38.75  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  157 VTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSinkklelkvkeqkdYWETELLQLKEQ 236
Cdd:pfam07200  22 VHSLPQVKALQAEKEELLAENESLAEENLSLEPELEELRSQLQELLEELKALKS--------------EYEEKEQELDEL 87

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 386869294  237 NQKMSSENEKMgirvdQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKE 285
Cdd:pfam07200  88 LSKFSPDALLA-----RLQAAAAEAEEESEALAESFLEGEIDLDEFLKQ 131
PRK11281 PRK11281
mechanosensitive channel MscK;
150-365 2.23e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 40.67  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  150 NEEDILVV----TTQGEVEEIEQHNKELckenqelkdscISLQKQNSDMQAELQKKQEELETLQSINK--------KLEL 217
Cdd:PRK11281   55 EAEDKLVQqdleQTLALLDKIDRQKEET-----------EQLKQQLAQAPAKLRQAQAELEALKDDNDeetretlsTLSL 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  218 KVKEQKdyWETELLQLK--------------------EQNQKMSSENEKmgiRVDQLQAQLSTQEKEMEKLVqgdqdkTE 277
Cdd:PRK11281  124 RQLESR--LAQTLDQLQnaqndlaeynsqlvslqtqpERAQAALYANSQ---RLQQIRNLLKGGKVGGKALR------PS 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  278 QLEQLKKENDHLFLSLTEQRKDqkkLE-----QTVEQMKQNETTAmkKQQELMDENFDL-----SKRLSENEIICNALQR 347
Cdd:PRK11281  193 QRVLLQAEQALLNAQNDLQRKS---LEgntqlQDLLQKQRDYLTA--RIQRLEHQLQLLqeainSKRLTLSEKTVQEAQS 267

                         250
                  ....*....|....*....
gi 386869294  348 QKERLE-GENDLLKRENSR 365
Cdd:PRK11281  268 QDEAARiQANPLVAQELEI 286
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
220-366 2.40e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 2.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 220 KEQKDYWETELLQLKEQNQKMSSENE------KMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSL 293
Cdd:PRK02224 474 RERVEELEAELEDLEEEVEEVEERLEraedlvEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEA 553

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386869294 294 TEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSK---RLSENEIICNALQRQKERLEGENDLLKRENSRL 366
Cdd:PRK02224 554 EEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirtLLAAIADAEDEIERLREKREALAELNDERRERL 629
PTZ00121 PTZ00121
MAEBL; Provisional
 162-365 2.64e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  162 EVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWE-----TELLQLKEQ 236
Cdd:PTZ00121 1316 KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADaakkkAEEKKKADE 1395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  237 NQKMSSENEKMGIRVDQLQAQLSTQE---KEMEKLVQGDQDKTEQLEqlKKENDHLFLSLTEQRKDQKKLEQTVEQMKQN 313
Cdd:PTZ00121 1396 AKKKAEEDKKKADELKKAAAAKKKADeakKKAEEKKKADEAKKKAEE--AKKADEAKKKAEEAKKAEEAKKKAEEAKKAD 1473

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 386869294  314 EttaMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKRENSR 365
Cdd:PTZ00121 1474 E---AKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522
DUF3450 pfam11932
Protein of unknown function (DUF3450); This family of proteins are functionally ...
 205-309 2.81e-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: 39.14  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  205 LETLQSINKkLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLvqgdQDKTEQLEQLKK 284
Cdd:pfam11932  19 LDLAEKAVA-AAAQSQKKIDKWDDEKQELLAEYRALKAELESLEVYNRQLERLVASQEQEIASL----ERQIEEIERTER 93

                          90       100
                  ....*....|....*....|....*
gi 386869294  285 ENDHLFLSLTEQrkdqkkLEQTVEQ 309
Cdd:pfam11932  94 ELVPLMLKMLDR------LEQFVAL 112
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 227-364 2.93e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 2.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 227 ETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHL----------------- 289
Cdd:COG3883   15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAeaeieerreelgerara 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 290 ----------------------FLS---------------LTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLS 332
Cdd:COG3883   95 lyrsggsvsyldvllgsesfsdFLDrlsalskiadadadlLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELE 174

                        170       180       190
                 ....*....|....*....|....*....|..
gi 386869294 333 KRLSENEIICNALQRQKERLEGENDLLKRENS 364
Cdd:COG3883  175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELA 206
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 165-326 3.19e-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: 40.09  E-value: 3.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  165 EIEQHNKELCKEN----QELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKlELKVKEQKDYWETELLQLKEQNQ-- 238
Cdd:pfam05483 489 ELTAHCDKLLLENkeltQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEK-EMNLRDELESVREEFIQKGDEVKck 567

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  239 -KMSSENEK-MGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETT 316
Cdd:pfam05483 568 lDKSEENARsIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS 647

                         170
                  ....*....|
gi 386869294  317 AMKKQQELMD 326
Cdd:pfam05483 648 AKQKFEEIID 657
GAS pfam13851
Growth-arrest specific micro-tubule binding; This family is the highly conserved central ...
 166-353 3.37e-03

Growth-arrest specific micro-tubule binding; This family is the highly conserved central region of a number of metazoan proteins referred to as growth-arrest proteins. In mouse, Gas8 is predominantly a testicular protein, whose expression is developmentally regulated during puberty and spermatogenesis. In humans, it is absent in infertile males who lack the ability to generate gametes. The localization of Gas8 in the motility apparatus of post-meiotic gametocytes and mature spermatozoa, together with the detection of Gas8 also in cilia at the apical surfaces of epithelial cells lining the pulmonary bronchi and Fallopian tubes suggests that the Gas8 protein may have a role in the functioning of motile cellular appendages. Gas8 is a microtubule-binding protein localized to regions of dynein regulation in mammalian cells.


Pssm-ID: 464001 [Multi-domain]  Cd Length: 200  Bit Score: 38.73  E-value: 3.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  166 IEQHNKELckenQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKlelkvkeqkdywetELLQLKEQNQKMSSENE 245
Cdd:pfam13851   3 MKNHEKAF----NEIKNYYNDITRNNLELIKSLKEEIAELKKKEERNEK--------------LMSEIQQENKRLTEPLQ 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  246 KMGIRVDQLQAQLSTQEK---EMEKLVQGDQDKTEQLEQLKKENDHLFLSLT--EQRKDQ--KKLEQTVEQMKQ---NET 315
Cdd:pfam13851  65 KAQEEVEELRKQLENYEKdkqSLKNLKARLKVLEKELKDLKWEHEVLEQRFEkvERERDElyDKFEAAIQDVQQktgLKN 144

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 386869294  316 TAMKKQQELMDENFD-----LSKRLSENEIICNALQRQKERLE 353
Cdd:pfam13851 145 LLLEKKLQALGETLEkkeaqLNEVLAAANLDPDALQAVTEKLE 187
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 145-368 3.78e-03

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: 39.95  E-value: 3.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   145 QFRPENEEDILVvTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKD 224
Cdd:pfam02463  257 KQEIEKEEEKLA-QVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKE 335

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   225 YWETELLQLKEQNQKMSSENEKM---------------------GIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLK 283
Cdd:pfam02463  336 EIEELEKELKELEIKREAEEEEEeeleklqekleqleeellakkKLESERLSSAAKLKEEELELKSEEEKEAQLLLELAR 415

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   284 KENDHL-------FLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGEN 356
Cdd:pfam02463  416 QLEDLLkeekkeeLEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKL 495

                          250
                   ....*....|..
gi 386869294   357 DLLKRENSRLLS 368
Cdd:pfam02463  496 EERSQKESKARS 507
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 162-363 4.03e-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: 39.77  E-value: 4.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   162 EVEEIEQHNKELCKENQELKDSCISLQKQNSDMQA----ELQKKQEELEtlqsinKKLELKVKEQKDYwETELLQLKEQN 237
Cdd:pfam01576  693 QVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAqferDLQARDEQGE------EKRRQLVKQVREL-EAELEDERKQR 765

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   238 QKMSSENEKMGIRVDQLQAQLSTQE-------KEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQM 310
Cdd:pfam01576  766 AQAVAAKKKLELDLKELEAQIDAANkgreeavKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQL 845

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 386869294   311 KQNETTAMKKQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDLLKREN 363
Cdd:pfam01576  846 QEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEEL 898
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 149-341 4.05e-03

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: 39.95  E-value: 4.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   149 ENEEDILVVTTQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELEtlqsINKKLELKVKEQKDYWET 228
Cdd:pfam02463  341 EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELE----LKSEEEKEAQLLLELARQ 416

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   229 ELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKEndhlfLSLTEQRKDQKKLEQTVE 308
Cdd:pfam02463  417 LEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDL-----LKETQLVKLQEQLELLLS 491

                          170       180       190
                   ....*....|....*....|....*....|....
gi 386869294   309 QMKQNETTAM-KKQQELMDENFDLSKRLSENEII 341
Cdd:pfam02463  492 RQKLEERSQKeSKARSGLKVLLALIKDGVGGRII 525
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
149-368 4.07e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 4.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 149 ENEEDILVVTTQgEVEEIEQHNKELCKENQELKDSCISLQKQNSDmQAELQKKQEELETLQSINKKLEL----------- 217
Cdd:PRK03918 448 EHRKELLEEYTA-ELKRIEKELKEIEEKERKLRKELRELEKVLKK-ESELIKLKELAEQLKELEEKLKKynleelekkae 525

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 218 ---KVKEQKDYWETELLQLKEQNQK---MSSENEKMGIRVDQLQAQLSTQEKEMEKL----VQGDQDKTEQLEQLKKEnd 287
Cdd:PRK03918 526 eyeKLKEKLIKLKGEIKSLKKELEKleeLKKKLAELEKKLDELEEELAELLKELEELgfesVEELEERLKELEPFYNE-- 603

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 288 hlFLSLteqRKDQKKLEQTVEQMKQNETTAMKKQQELMDENFD---LSKRLSENEIICNalQRQKERLEGENDLLKRENS 364
Cdd:PRK03918 604 --YLEL---KDAEKELEREEKELKKLEEELDKAFEELAETEKRleeLRKELEELEKKYS--EEEYEELREEYLELSRELA 676


                 ....
gi 386869294 365 RLLS 368
Cdd:PRK03918 677 GLRA 680
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 189-333 4.17e-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: 39.77  E-value: 4.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   189 KQNSDMQA---ELQKKQEELETLQSINKKLELKVKEQKDywetELLQLKEQNQ---KMSSENEKMGIRVDQLQAQLSTQE 262
Cdd:pfam01576    2 RQEEEMQAkeeELQKVKERQQKAESELKELEKKHQQLCE----EKNALQEQLQaetELCAEAEEMRARLAARKQELEEIL 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386869294   263 KEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQE----LMDENFDLSK 333
Cdd:pfam01576   78 HELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLEEdillLEDQNSKLSK 152
CENP-K pfam11802
Centromere-associated protein K; CENP-K is one of seven new CENP-A-nucleosome distal (CAD) ...
 160-315 5.07e-03

Centromere-associated protein K; CENP-K is one of seven new CENP-A-nucleosome distal (CAD) centromere components (the others being CENP-L, CENP-O, CENP-P, CENP-Q, CENP-R and CENP-S) that are identified as assembling on the CENP-A nucleosome associated complex, NAC. The CENP-A NAC is essential, as disruption of the complex causes errors of chromosome alignment and segregation that preclude cell survival despite continued centromere-derived mitotic checkpoint signalling. CENP-K is centromere-associated through its interaction with one or more components of the CENP-A NAC.


Pssm-ID: 463355 [Multi-domain]  Cd Length: 263  Bit Score: 38.51  E-value: 5.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  160 QGEVEEIEQHNKELCKENQElkdSCISLQKQnsdmqaELQKKQEELETLQSInkkLELKVKEQKDYWETELLQLKEQNQK 239
Cdd:pfam11802  59 TAELEQWQKRTPEIISLNPE---VLLTLGKE------ELQKLRHQLEMVLST---IQSKNKKLKEDLEREQQWLDEQQQI 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  240 MSSENEKMGIRVDQlQAQLSTQEK--EMEKLVQGDQDKTEQLEQLKKE--NDHLFLSLTEQRKDQKKLEQTVEQMKQNET 315
Cdd:pfam11802 127 LESLNEKHKELKNQ-VVTFSEKRKfqELKTKIRKIKEYKEKLLTTLGEflDEHFPLPEENGNSVKKKRKNSQEPTINLIT 205
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
193-357 5.18e-03

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 38.27  E-value: 5.18e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 193 DMQAELQKKQEELETLQSINKKLELKVKEQKDY---WETELLQLKEQN----------QKMSSENEkmgirVDQLQAQLS 259
Cdd:COG1842   34 DMEEDLVEARQALAQVIANQKRLERQLEELEAEaekWEEKARLALEKGredlarealeRKAELEAQ-----AEALEAQLA 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 260 TQEKEMEKLVQGDQDKTEQLEQLKKENDhLFLSLTEQRKDQKKLEQTVEQMKQNETTA----MKKQQELMDENFDLSKRL 335
Cdd:COG1842  109 QLEEQVEKLKEALRQLESKLEELKAKKD-TLKARAKAAKAQEKVNEALSGIDSDDATSalerMEEKIEEMEARAEAAAEL 187

                        170       180
                 ....*....|....*....|..
gi 386869294 336 SENeiicNALQRQKERLEGEND 357
Cdd:COG1842  188 AAG----DSLDDELAELEADSE 205
mukB PRK04863
chromosome partition protein MukB;
155-368 5.18e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.56  E-value: 5.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  155 LVVTTQGEVEEIEQHN--KELCKENQELK---DSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEqkdywETE 229
Cdd:PRK04863  481 LVRKIAGEVSRSEAWDvaRELLRRLREQRhlaEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDD-----EDE 555

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  230 LLQLKEQnqkmssenekmgirvdqLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQ 309
Cdd:PRK04863  556 LEQLQEE-----------------LEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQ 618

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 386869294  310 MKQNETTAmkkqQELMdenfDLSKRLSENEiicNALQRQKERLEGENDLLKRENSRLLS 368
Cdd:PRK04863  619 SGEEFEDS----QDVT----EYMQQLLERE---RELTVERDELAARKQALDEEIERLSQ 666
PRK12704 PRK12704
phosphodiesterase; Provisional
 255-391 5.35e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 38.99  E-value: 5.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 255 QAQLSTQEKEMEKLVQGDQDKTEQLEQLKKEndhlflsLTEQRKD----QKKLEQTVEQMKQNETTAMKKQQELMDENFD 330
Cdd:PRK12704  46 EAKKEAEAIKKEALLEAKEEIHKLRNEFEKE-------LRERRNElqklEKRLLQKEENLDRKLELLEKREEELEKKEKE 118

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386869294 331 LSKRLSEneiicnaLQRQKERLEgenDLLKRENSRLLSYMGLdfnslpyqvpTSDEggARQ 391
Cdd:PRK12704 119 LEQKQQE-------LEKKEEELE---ELIEEQLQELERISGL----------TAEE--AKE 157
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 149-243 6.06e-03

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 38.56  E-value: 6.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 149 ENEEDILVVttQGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWET 228
Cdd:COG4026  132 ELREELLEL--KEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEEFDNIKSEYSDLKSRFEELLKKRLL 209

                         90
                 ....*....|....*
gi 386869294 229 ELLQLKEQNQKMSSE 243
Cdd:COG4026  210 EVFSLEELWKELFPE 224
PRK11281 PRK11281
mechanosensitive channel MscK;
185-348 6.29e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 39.12  E-value: 6.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  185 ISLQKQNSDMQAELQKKQEELetlQSINKKL-------ELKVKEQKDYWETELLQLKEQN--QKMSSENEkmgirvDQLQ 255
Cdd:PRK11281  152 VSLQTQPERAQAALYANSQRL---QQIRNLLkggkvggKALRPSQRVLLQAEQALLNAQNdlQRKSLEGN------TQLQ 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  256 AQLSTQEKEMeklvqgdqdkTEQLEQLKKENDHLFLSLTEQRKDQKklEQTVEQMKQNETTAMKK-----QQELmDENFD 330
Cdd:PRK11281  223 DLLQKQRDYL----------TARIQRLEHQLQLLQEAINSKRLTLS--EKTVQEAQSQDEAARIQanplvAQEL-EINLQ 289

                         170
                  ....*....|....*...
gi 386869294  331 LSKRLSENEIICNALQRQ 348
Cdd:PRK11281  290 LSQRLLKATEKLNTLTQQ 307
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
150-366 6.58e-03

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 38.35  E-value: 6.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 150 NEEDILVVTTQGEVEEIEQHNKELCKENQELKDscisLQKQNSDMQAELQKKQEELETLQSINKKLElKVKEQKDYWETE 229
Cdd:COG1340   43 EKRDELNAQVKELREEAQELREKRDELNEKVKE----LKEERDELNEKLNELREELDELRKELAELN-KAGGSIDKLRKE 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 230 LLQL--KEQNQKMSSENEKMGI-RVDQLQAQLSTQEKEMEKLVQGDQDKTEqLEQLKKENDHLFLSLTEQRKDQKKLEQT 306
Cdd:COG1340  118 IERLewRQQTEVLSPEEEKELVeKIKELEKELEKAKKALEKNEKLKELRAE-LKELRKEAEEIHKKIKELAEEAQELHEE 196

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386869294 307 VEQMKQNETTAMKKQQELMDENFDLSKRLSE--NEIIcnALQRQKERLEGENDLLKRENSRL 366
Cdd:COG1340  197 MIELYKEADELRKEADELHKEIVEAQEKADElhEEII--ELQKELRELRKELKKLRKKQRAL 256
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
171-353 6.87e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 6.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 171 KELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLqsinkklelkvKEQKDYWETELLQLKEQNQKMSSENEKMGIR 250
Cdd:PRK02224 505 VEAEDRIERLEERREDLEELIAERRETIEEKRERAEEL-----------RERAAELEAEAEEKREAAAEAEEEAEEAREE 573

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 251 VDQLQAQLSTQEKEMEKL--VQGDQDK-----------TEQLEQLKKENDHLFLSLTEQRKDQKKLEQT-----VEQMKQ 312
Cdd:PRK02224 574 VAELNSKLAELKERIESLerIRTLLAAiadaedeierlREKREALAELNDERRERLAEKRERKRELEAEfdearIEEARE 653

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 386869294 313 NETTAMK-------KQQELMDENFDLSKRLS--ENEIicNALQRQKERLE 353
Cdd:PRK02224 654 DKERAEEyleqveeKLDELREERDDLQAEIGavENEL--EELEELRERRE 701
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 95-302 7.36e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 38.76  E-value: 7.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  95 WVTLPIDLnnKSAKQQE-VQFKAYYLPKDdeyyqfcYVDEDGVVRGASIPFQFRPENEEDILVVTTqgEVEEIEQHNKEL 173
Cdd:PRK05771 129 WGNFDLDL--SLLLGFKyVSVFVGTVPED-------KLEELKLESDVENVEYISTDKGYVYVVVVV--LKELSDEVEEEL 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 174 CK---ENQELKDSCISLQkqnsdmqaELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEqnqKMSSENEKmgir 250
Cdd:PRK05771 198 KKlgfERLELEEEGTPSE--------LIREIKEELEEIEKERESLLEELKELAKKYLEELLALYE---YLEIELER---- 262

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 386869294 251 vdqlqAQLSTQEKEMEKL--VQG--DQDKTEQLEQL--KKENDHLFLSLTEQRKDQKK 302
Cdd:PRK05771 263 -----AEALSKFLKTDKTfaIEGwvPEDRVKKLKELidKATGGSAYVEFVEPDEEEEE 315
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 149-366 7.51e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 39.03  E-value: 7.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  149 ENEEDILVVTTQGEVEeIEQHNKELcKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSinkKLELKVKEQKDYWE- 227
Cdd:pfam10174 251 DLEDEVQMLKTNGLLH-TEDREEEI-KQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQT---KLETLTNQNSDCKQh 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  228 ----TELLQLKEQNQK-MSSEnekmgirVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKENDHLFLSL-TEQRKD-- 299
Cdd:pfam10174 326 ievlKESLTAKEQRAAiLQTE-------VDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDMLdVKERKInv 398

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  300 -QKKLEQTVEQMKQNETTAMKKQQELMDENFD----------LSKRLSENEIICNALQRQKERLE----GENDLLKRENS 364
Cdd:pfam10174 399 lQKKIENLQEQLRDKDKQLAGLKERVKSLQTDssntdtalttLEEALSEKERIIERLKEQREREDrerlEELESLKKENK 478


                  ..
gi 386869294  365 RL 366
Cdd:pfam10174 479 DL 480
Zn-C2H2_12 pfam18112
Autophagy receptor zinc finger-C2H2 domain; This domain is found in calcium-binding and ...
 443-465 7.58e-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: 33.77  E-value: 7.58e-03
                          10        20
                  ....*....|....*....|....
gi 386869294  443 CPICDKIFPA-TEKQIFEDHVFCH 465
Cdd:pfam18112   3 CPLCGEMFSPnIDQSEFEEHVESH 26
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 160-310 7.59e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 7.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 160 QGEVEEIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQK 239
Cdd:COG1196  671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386869294 240 MSSENEKMGIRVDQLQAQLSTQEKEMEKL--VqgDQDKTEQLEQLKKENDHlflsLTEQRKD----QKKLEQTVEQM 310
Cdd:COG1196  751 EALEELPEPPDLEELERELERLEREIEALgpV--NLLAIEEYEELEERYDF----LSEQREDleeaRETLEEAIEEI 821
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 188-355 7.71e-03

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 38.96  E-value: 7.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  188 QKQNSDMQAELQKKQEELETLQSINKKLELKVKEQ------KDYWETE-------LLQLKEQNQKMSSENEKMGIRVDQL 254
Cdd:pfam07111 196 QKEAELLRKQLSKTQEELEAQVTLVESLRKYVGEQvppevhSQTWELErqelldtMQHLQEDRADLQATVELLQVRVQSL 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  255 QAQLSTQEKEMEKLVQG----DQDKTEQLEQLKKENDHLFLSLTEQRKDQkKLEQTvEQMKQNETTAMKKQQELMDENfd 330
Cdd:pfam07111 276 THMLALQEEELTRKIQPsdslEPEFPKKCRSLLNRWREKVFALMVQLKAQ-DLEHR-DSVKQLRGQVAELQEQVTSQS-- 351

                         170       180
                  ....*....|....*....|....*
gi 386869294  331 lskrlSENEIICNALQRQKERLEGE 355
Cdd:pfam07111 352 -----QEQAILQRALQDKAAEVEVE 371
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 163-366 7.72e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 38.33  E-value: 7.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 163 VEEIEQHNKELCKENQElkdscISLQKqnsdMQAELQKKQEELEtlQSINKKLELKVKEQKDYwetellqLKEQNQKMSS 242
Cdd:cd16269   96 MEQLEEKKEEFCKQNEE-----ASSKR----CQALLQELSAPLE--EKISQGSYSVPGGYQLY-------LEDREKLVEK 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 243 ENEKM--GIRVDQ-LQAQLSTQEKEMEKLVQGDQDKTE---QLEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETT 316
Cdd:cd16269  158 YRQVPrkGVKAEEvLQEFLQSKEAEAEAILQADQALTEkekEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEE 237

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 386869294 317 AMKKQQELMDEnfDLSKRLSENEIICNALQRQKERL-----EGENDLLKRENSRL 366
Cdd:cd16269  238 HLRQLKEKMEE--ERENLLKEQERALESKLKEQEALleegfKEQAELLQEEIRSL 290
IFT57 pfam10498
Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles ...
 163-310 7.80e-03

Intra-flagellar transport protein 57; Eukaryotic cilia and flagella are specialized organelles found at the periphery of cells of diverse organizms. Intra-flagellar transport (IFT) is required for the assembly and maintenance of eukaryotic cilia and flagella, and consists of the bidirectional movement of large protein particles between the base and the distal tip of the organelle. IFT particles contain multiple copies of two distinct protein complexes, A and B, which contain at least 6 and 11 protein subunits. IFT57 is part of complex B but is not, however, required for the core subunits to stay associated. This protein is known as Huntington-interacting protein-1 in humans.


Pssm-ID: 463118 [Multi-domain]  Cd Length: 360  Bit Score: 38.39  E-value: 7.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  163 VEEIEQHNKELCKEnqeLKDSCISLQKqnsdMQAELQKKQEELETL-QSINKKLElkvkeqkdyweTELLQLKEQNQKMS 241
Cdd:pfam10498 224 LEQMKQHKKSIEES---LPDTKSQLDK----LHTDISKTLEKIESReKYINSQLE-----------PLIQEYREAQDELS 285

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386869294  242 SENEKMgirvDQLQAQLSTQEKEMEKLvqgdqdkTEQLEQLKKENDHLFLSLT------EQRKDQKKLEQTVEQM 310
Cdd:pfam10498 286 EVQEKY----KQLSEGVTERTRELAEI-------TEELEKVKQEMEERGSSMTdgsplvKIKQALTKLKEEIKQM 349
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 165-358 8.06e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 39.05  E-value: 8.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   165 EIEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSEN 244
Cdd:pfam12128  633 ELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREA 712

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294   245 -----EKMGIRVDQLQAQLSTQEKEMEKLVQGDQDKTEQLEQLKKeNDHLFLSLTEQR-----KDQKKLEQTVEQMKQNE 314
Cdd:pfam12128  713 rtekqAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYK-RDLASLGVDPDViaklkREIRTLERKIERIAVRR 791

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 386869294   315 TTAMK----KQQELMDENFDLSKRLSENEIICNALQRQKERLEGENDL 358
Cdd:pfam12128  792 QEVLRyfdwYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKL 839
PTZ00121 PTZ00121
MAEBL; Provisional
 108-326 8.76e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.97  E-value: 8.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  108 KQQEVQFKAYYLPKDDEYYQFCYVDEDGVVRGASIPFQFRPENEEDILVVTTQGEVEEIEQHN-KELCKENQELKDSCIS 186
Cdd:PTZ00121 1614 KAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKaEEAKKAEEDEKKAAEA 1693

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  187 LQKQnsdmqAELQKKQEELETLQS--INKKLELKVKEQKDYWETELLQLKEQNQKMSSENEKMGIRVDQLQAQLSTQEKE 264
Cdd:PTZ00121 1694 LKKE-----AEEAKKAEELKKKEAeeKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK 1768

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 386869294  265 MEKLVQGDQDKTEQlEQLKKENDHLFLSLTEQRKDQKKLEQTVEQMKQNETTAMKKQQELMD 326
Cdd:PTZ00121 1769 KAEEIRKEKEAVIE-EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMED 1829
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 166-304 9.65e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 38.65  E-value: 9.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294 166 IEQHNKELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQKDYWETELLQLKEQNQKMSSENE 245
Cdd:PRK00409 504 IEEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAK 583

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 386869294 246 KmgiRVDQLQAQLSTQEKeMEKLVQGDQDKTEQLEQLKKENDHLFLSLTEQRKDQKKLE 304
Cdd:PRK00409 584 K---EADEIIKELRQLQK-GGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
 172-289 9.73e-03

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 462536 [Multi-domain]  Cd Length: 176  Bit Score: 37.22  E-value: 9.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386869294  172 ELCKENQELKDSCISLQKQNSDMQAELQKKQEELETLQSINKKLELKVKEQkdywETELLQLKEQNQKMSSENekmgirv 251
Cdd:pfam08614  68 ELYRSRGELAQRLVDLNEELQELEKKLREDERRLAALEAERAQLEEKLKDR----EEELREKRKLNQDLQDEL------- 136

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 386869294  252 DQLQAQLSTQEkemeklvqgdqdktEQLEQLKKENDHL 289
Cdd:pfam08614 137 VALQLQLNMAE--------------EKLRKLEKENREL 160
 
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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