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Conserved domains on  [gi|564373226|ref|XP_006246966|]
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rab11 family-interacting protein 4 isoform X3 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RBD-FIP pfam09457
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of ...
 494-534 8.74e-13

FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of Rab11-interacting proteins (FIPs). The Rab proteins constitute the largest family of small GTPases (>60 members in mammals). Among them Rab11 is a well characterized regulator of endocytic and recycling pathways. Rab11 associates with a broad range of post-Golgi organelles, including recycling endosomes.


:

Pssm-ID: 462805 [Multi-domain]  Cd Length: 41  Bit Score: 62.74  E-value: 8.74e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 564373226  494 SRDELMEALKEQEEINFRLRQYMDKIILAILDHNPSILEIK 534
Cdd:pfam09457   1 SRDELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEVP 41
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 237-519 5.80e-10

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 62.38  E-value: 5.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   237 NDITEKVSFLEKKVTELENDSLASGGLKSKLKLENVQLVHRVHELEEMVKDQETTAEQALEEEARRHREVYCKLEREKST 316
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   317 ELEL----------------LNTRVQQLEEENTDLRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDK 380
Cdd:TIGR02168  767 EERLeeaeeelaeaeaeieeLEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   381 LRQNRLE---FQKEREATQELIEDLRRELEHLQMYKldcERPGRGRSSSGLGEFNARAREVELEHEVKRLKQENHKLRDQ 457
Cdd:TIGR02168  847 IEELSEDiesLAAEIEELEELIEELESELEALLNER---ASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564373226   458 NDDLNGQILSLSLyEAKNLFATQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQYMDKI 519
Cdd:TIGR02168  924 LAQLELRLEGLEV-RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
 
Name Accession Description Interval E-value
RBD-FIP pfam09457
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of ...
 494-534 8.74e-13

FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of Rab11-interacting proteins (FIPs). The Rab proteins constitute the largest family of small GTPases (>60 members in mammals). Among them Rab11 is a well characterized regulator of endocytic and recycling pathways. Rab11 associates with a broad range of post-Golgi organelles, including recycling endosomes.


Pssm-ID: 462805 [Multi-domain]  Cd Length: 41  Bit Score: 62.74  E-value: 8.74e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 564373226  494 SRDELMEALKEQEEINFRLRQYMDKIILAILDHNPSILEIK 534
Cdd:pfam09457   1 SRDELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEVP 41
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 237-519 5.80e-10

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: 62.38  E-value: 5.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   237 NDITEKVSFLEKKVTELENDSLASGGLKSKLKLENVQLVHRVHELEEMVKDQETTAEQALEEEARRHREVYCKLEREKST 316
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   317 ELEL----------------LNTRVQQLEEENTDLRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDK 380
Cdd:TIGR02168  767 EERLeeaeeelaeaeaeieeLEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   381 LRQNRLE---FQKEREATQELIEDLRRELEHLQMYKldcERPGRGRSSSGLGEFNARAREVELEHEVKRLKQENHKLRDQ 457
Cdd:TIGR02168  847 IEELSEDiesLAAEIEELEELIEELESELEALLNER---ASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564373226   458 NDDLNGQILSLSLyEAKNLFATQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQYMDKI 519
Cdd:TIGR02168  924 LAQLELRLEGLEV-RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 263-514 4.56e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 4.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 263 LKSKLK-LENVQLVHRVHELE---EMVKDQETTAEQALEEEARRHREVYCKLEREKStELELLNTRVQQLEEENTDLRTT 338
Cdd:COG1196  218 LKEELKeLEAELLLLKLRELEaelEELEAELEELEAELEELEAELAELEAELEELRL-ELEELELELEEAQAEEYELLAE 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 339 VTRLKSQTEKLDEERQRMSDRLEDTSLR---LKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRRELEHLQmykld 415
Cdd:COG1196  297 LARLEQDIARLEERRRELEERLEELEEElaeLEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE----- 371

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 416 cerpgRGRSSSGLGEFNARAREVELEHEVKRLKQENHKLRDQNDDLNGQILSLSLYEAKNLFATQTKAQSLAAEIDTASR 495
Cdd:COG1196  372 -----AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446

                        250
                 ....*....|....*....
gi 564373226 496 DELMEALKEQEEINFRLRQ 514
Cdd:COG1196  447 AAEEEAELEEEEEALLELL 465
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 270-411 4.56e-05

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 45.40  E-value: 4.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226  270 ENVQLVHRVHELEEMVK-----DQETTAEQALEEEARRHREvycKLEREKSTELELLNTRVQQLEEENTDLRTTVTRLKS 344
Cdd:pfam04849 116 EILQLRHELSKKDDLLQiysndAEESETESSCSTPLRRNES---FSSLHGCVQLDALQEKLRGLEEENLKLRSEASHLKT 192

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564373226  345 QTEKL-DEERQRMSD---RLEDTSLRLKDEMD-LYKRMMDKLRQnrlefqkereatQELIEDLRRELEHLQM 411
Cdd:pfam04849 193 ETDTYeEKEQQLMSDcveQLSEANQQMAELSEeLARKMEENLRQ------------QEEITSLLAQIVDLQH 252
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
310-513 7.29e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.80  E-value: 7.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 310 LEREKSTELELLNTRVQQLEEEN-----TDLRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRL------KDEMDLYKRMM 378
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEEKEEKDlherlNGLESELAELDEEIERYEEQREQARETRDEADEVLeeheerREELETLEAEI 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 379 DKLRQNRLEFQKEREATQELIEDLRRELEHLQmykldcERPGRGRSSSGLGEFNARA---REVELEHEVKRLKQENHKLR 455
Cdd:PRK02224 261 EDLRETIAETEREREELAEEVRDLRERLEELE------EERDDLLAEAGLDDADAEAveaRREELEDRDEELRDRLEECR 334

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564373226 456 DQNDDLNGQILSLsLYEAKNLFATQTKAQSLAAEIDT---ASRDELMEALKEQEEINFRLR 513
Cdd:PRK02224 335 VAAQAHNEEAESL-REDADDLEERAEELREEAAELESeleEAREAVEDRREEIEELEEEIE 394
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 280-410 1.74e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 40.43  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 280 ELEEMVKDQETTAEQALEEEARRHREVYCKLEREKSTELEllnTRVQQLEeenTDLRTTVTRLKSQTEKLDEERQRMSDR 359
Cdd:cd22656   95 EILELIDDLADATDDEELEEAKKTIKALLDDLLKEAKKYQ---DKAAKVV---DKLTDFENQTEKDQTALETLEKALKDL 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564373226 360 LEDTSLRL-KDEMDLYKRMMDKLRQN-RLEFQKEREATQELIEDLRRELEHLQ 410
Cdd:cd22656  169 LTDEGGAIaRKEIKDLQKELEKLNEEyAAKLKAKIDELKALIADDEAKLAAAL 221
 
Name Accession Description Interval E-value
RBD-FIP pfam09457
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of ...
 494-534 8.74e-13

FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of Rab11-interacting proteins (FIPs). The Rab proteins constitute the largest family of small GTPases (>60 members in mammals). Among them Rab11 is a well characterized regulator of endocytic and recycling pathways. Rab11 associates with a broad range of post-Golgi organelles, including recycling endosomes.


Pssm-ID: 462805 [Multi-domain]  Cd Length: 41  Bit Score: 62.74  E-value: 8.74e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 564373226  494 SRDELMEALKEQEEINFRLRQYMDKIILAILDHNPSILEIK 534
Cdd:pfam09457   1 SRDELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEVP 41
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 237-519 5.80e-10

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: 62.38  E-value: 5.80e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   237 NDITEKVSFLEKKVTELENDSLASGGLKSKLKLENVQLVHRVHELEEMVKDQETTAEQALEEEARRHREVYCKLEREKST 316
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   317 ELEL----------------LNTRVQQLEEENTDLRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDK 380
Cdd:TIGR02168  767 EERLeeaeeelaeaeaeieeLEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   381 LRQNRLE---FQKEREATQELIEDLRRELEHLQMYKldcERPGRGRSSSGLGEFNARAREVELEHEVKRLKQENHKLRDQ 457
Cdd:TIGR02168  847 IEELSEDiesLAAEIEELEELIEELESELEALLNER---ASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564373226   458 NDDLNGQILSLSLyEAKNLFATQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQYMDKI 519
Cdd:TIGR02168  924 LAQLELRLEGLEV-RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 263-514 4.56e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 56.10  E-value: 4.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 263 LKSKLK-LENVQLVHRVHELE---EMVKDQETTAEQALEEEARRHREVYCKLEREKStELELLNTRVQQLEEENTDLRTT 338
Cdd:COG1196  218 LKEELKeLEAELLLLKLRELEaelEELEAELEELEAELEELEAELAELEAELEELRL-ELEELELELEEAQAEEYELLAE 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 339 VTRLKSQTEKLDEERQRMSDRLEDTSLR---LKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRRELEHLQmykld 415
Cdd:COG1196  297 LARLEQDIARLEERRRELEERLEELEEElaeLEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE----- 371

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 416 cerpgRGRSSSGLGEFNARAREVELEHEVKRLKQENHKLRDQNDDLNGQILSLSLYEAKNLFATQTKAQSLAAEIDTASR 495
Cdd:COG1196  372 -----AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE 446

                        250
                 ....*....|....*....
gi 564373226 496 DELMEALKEQEEINFRLRQ 514
Cdd:COG1196  447 AAEEEAELEEEEEALLELL 465
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 266-514 1.29e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 1.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 266 KLKLENVQLVHRVHELEEMVKDQETTAEQALEEEARRHREVYCKLEREKSTELELLNTRVQQLEEENTDLRTTVTRLKSQ 345
Cdd:COG1196  238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 346 TEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRRELEHLQMYKLDCERPGRGRSS 425
Cdd:COG1196  318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 426 SGLGEFNARAREVELEHEVKRLKQENHKLRDQNDDLNGQILSLSLyEAKNLFATQTKAQSLAAEIDTASRDELMEALKEQ 505
Cdd:COG1196  398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE-ALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476


                 ....*....
gi 564373226 506 EEINFRLRQ 514
Cdd:COG1196  477 AALAELLEE 485
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
273-410 1.97e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 53.62  E-value: 1.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 273 QLVHRVHELEEMVKD-----QETTAEQALEEEARRHREVYCKLEREKStELELLNTRVQQLEEENTDLRTTVTRLKSQTE 347
Cdd:COG4717   92 ELQEELEELEEELEEleaelEELREELEKLEKLLQLLPLYQELEALEA-ELAELPERLEELEERLEELRELEEELEELEA 170

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564373226 348 KLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRRELEHLQ 410
Cdd:COG4717  171 ELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 246-507 2.28e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.79  E-value: 2.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 246 LEKKVTELENDSLASGGLKSKLKLENVQLVHRVHELEEmVKDQETTAEQALEEEARRhrevyckLEREKSTELELLNTRV 325
Cdd:COG1196  265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQ-DIARLEERRRELEERLEE-------LEEELAELEEELEELE 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 326 QQLEEENTDLRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQnRLEFQKEREATQELIEDLRRE 405
Cdd:COG1196  337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA-AAELAAQLEELEEAEEALLER 415

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 406 LEHLQMYKLDCERpgrgrsssglgefNARAREVELEHEVKRLKQENHKLRDQNDDLNGQILSLSLYEAKNLFATQTKAQS 485
Cdd:COG1196  416 LERLEEELEELEE-------------ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482

                        250       260
                 ....*....|....*....|..
gi 564373226 486 LAAEIDTASRDELMEALKEQEE 507
Cdd:COG1196  483 LEELAEAAARLLLLLEAEADYE 504
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 269-514 8.64e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 8.64e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   269 LENVQLVHRVHELEEMVKDQETTAEQALEEEARRHREVycKLEREKSTELELLNTRVQQLEEENTDLRTTVTRLKSQTEK 348
Cdd:TIGR02168  222 LRELELALLVLRLEELREELEELQEELKEAEEELEELT--AELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR 299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   349 LDEERQRMSDR---LEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRRELEHLQMYKldcerpgrgrss 425
Cdd:TIGR02168  300 LEQQKQILRERlanLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL------------ 367

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   426 sglgeFNARAREVELEHEVKRLKQENHKLRDQNDDLNGQILSL-SLYE--AKNLFATQTKAQSLAAEIDTASRDELMEAL 502
Cdd:TIGR02168  368 -----EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLeARLErlEDRRERLQQEIEELLKKLEEAELKELQAEL 442

                          250
                   ....*....|..
gi 564373226   503 KEQEEINFRLRQ 514
Cdd:TIGR02168  443 EELEEELEELQE 454
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
281-415 1.64e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 51.01  E-value: 1.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 281 LEEMVKDQETTAEQALEEEARRHREVYCKLEREKSTELELLNTRVQQLEEENTDLRTTVTRLKSQTEKLDEERQRMSDRl 360
Cdd:COG2433  378 IEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSE- 456

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564373226 361 EDTSLRLKDEMDLYKRMMDKLRqnrlefqKEREATQELIEDLRRELEHL-QMYKLD 415
Cdd:COG2433  457 ERREIRKDREISRLDREIERLE-------RELEEERERIEELKRKLERLkELWKLE 505
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 237-410 1.67e-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: 51.21  E-value: 1.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   237 NDITEKVSFLEKKVTELENDSLASGGLKSKLKLENVQLVHRVHELEEMVKDQET--TAEQALEEEARRHREVYCKLEREK 314
Cdd:TIGR02168  298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEelESLEAELEELEAELEELESRLEEL 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   315 STELELLNTRVQQLEEENTDLRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKD-EMDLYKRMMDKLRQNRLEFQKERE 393
Cdd:TIGR02168  378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELE 457

                          170
                   ....*....|....*..
gi 564373226   394 ATQELIEDLRRELEHLQ 410
Cdd:TIGR02168  458 RLEEALEELREELEEAE 474
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 241-513 3.41e-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: 50.06  E-value: 3.41e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   241 EKVSFLEKKVTELENDSLASGGLKSKLKLENVQLVHRVHELEEMVKD-----QETTAEQA-LEEEARRHREvycKLEREK 314
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkelYALANEISrLEQQKQILRE---RLANLE 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   315 sTELELLNTRVQQLEEENTDLRTTVTRLKSQTEKLDEERQRMSDRLEdtslRLKDEMDLYKRMMDKLRQNRLEFQKEREA 394
Cdd:TIGR02168  316 -RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE----ELEAELEELESRLEELEEQLETLRSKVAQ 390

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   395 TQELIEDLRRELEhlqmykldcerpgrgrsssglgefNARAREVELEHEVKRLKQENHKLRDQNDDLNGQILSLSLYE-- 472
Cdd:TIGR02168  391 LELQIASLNNEIE------------------------RLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEle 446

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 564373226   473 ------AKNLFATQTKAQSLAAEIDTASRdELMEALKEQEEINFRLR 513
Cdd:TIGR02168  447 eeleelQEELERLEEALEELREELEEAEQ-ALDAAERELAQLQARLD 492
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
240-451 7.22e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.14  E-value: 7.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226  240 TEKVSFLEKKVTELENDSLASGGLKSKLKLENVQLVHRVHELEEMVKDQETTAE-QALEEEARRHREVYCKLEREKST-- 316
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvASAEREIAELEAELERLDASSDDla 688

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226  317 ----ELELLNTRVQQLEEENTDLRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEM--DLYKR----MMDKLRQN-R 385
Cdd:COG4913   689 aleeQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELraLLEERfaaaLGDAVERElR 768

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564373226  386 LEFQKEREATQELIEDLRRELEHLQM-YKLD--CERPGRGRSSSGLGEFNARARE------VELEHEVKRLKQEN 451
Cdd:COG4913   769 ENLEERIDALRARLNRAEEELERAMRaFNREwpAETADLDADLESLPEYLALLDRleedglPEYEERFKELLNEN 843
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 268-410 1.14e-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: 48.53  E-value: 1.14e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   268 KLENVQLVHRVHELEEMVKDQETTAEQaLEEEARRHREVYCKLEREKSTELELLNTRVQQLEEENTDLRTTVTRLKSQTE 347
Cdd:TIGR02169  314 ERELEDAEERLAKLEAEIDKLLAEIEE-LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564373226   348 KLD------EERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRRELEHLQ 410
Cdd:TIGR02169  393 KLEklkreiNELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
286-410 2.28e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.22  E-value: 2.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226  286 KDQETTAEQALEEEARRHREVYCKLEREKSTELELLNTRVQQLEEENTDLRTTVTRLKSQTEKLDEERQRMSDRLEDTSL 365
Cdd:COG4913   308 EAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 564373226  366 RLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRRELEHLQ 410
Cdd:COG4913   388 EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 298-507 2.62e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.36  E-value: 2.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   298 EEARRHREVYCKLEREKSTELELLNTRVQQLEEENTDLRTT-------VTRLKSQTEKLDEERQR---MSDRLEDTSLRL 367
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKEleelsrqISALRKDLARLEAEVEQleeRIAQLSKELTEL 759

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   368 KDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRRELEhLQMYKLDCERPGRGRSSSGLGefNARAREVELEHEVKRL 447
Cdd:TIGR02168  760 EAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELK-ALREALDELRAELTLLNEEAA--NLRERLESLERRIAAT 836

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564373226   448 KQENHKLRDQNDDLNGQILSLslyeAKNLFATQTKAQSLAAEID--TASRDELMEALKEQEE 507
Cdd:TIGR02168  837 ERRLEDLEEQIEELSEDIESL----AAEIEELEELIEELESELEalLNERASLEEALALLRS 894
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 270-411 4.56e-05

HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found in several huntingtin-associated protein 1 (HAP1) homologs. HAP1 binds to huntingtin in a polyglutamine repeat-length-dependent manner. However, its possible role in the pathogenesis of Huntington's disease is unclear. This family also includes a similar N-terminal conserved region from hypothetical protein products of ALS2CR3 genes found in the human juvenile amyotrophic lateral sclerosis critical region 2q33-2q34.


Pssm-ID: 461455 [Multi-domain]  Cd Length: 309  Bit Score: 45.40  E-value: 4.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226  270 ENVQLVHRVHELEEMVK-----DQETTAEQALEEEARRHREvycKLEREKSTELELLNTRVQQLEEENTDLRTTVTRLKS 344
Cdd:pfam04849 116 EILQLRHELSKKDDLLQiysndAEESETESSCSTPLRRNES---FSSLHGCVQLDALQEKLRGLEEENLKLRSEASHLKT 192

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564373226  345 QTEKL-DEERQRMSD---RLEDTSLRLKDEMD-LYKRMMDKLRQnrlefqkereatQELIEDLRRELEHLQM 411
Cdd:pfam04849 193 ETDTYeEKEQQLMSDcveQLSEANQQMAELSEeLARKMEENLRQ------------QEEITSLLAQIVDLQH 252
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 237-514 4.72e-05

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: 46.25  E-value: 4.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226  237 NDITEKVSFLEKKVTELEN-------------DSLASGGLKSKLKLENV-QLVHRVHELEEMVKD------QETTAEQAL 296
Cdd:pfam05483 236 NDKEKQVSLLLIQITEKENkmkdltflleesrDKANQLEEKTKLQDENLkELIEKKDHLTKELEDikmslqRSMSTQKAL 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226  297 EEEARRHREVYCKLEREKSTELELLNtrvqqleEENTDLRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLK-DEMDLYK 375
Cdd:pfam05483 316 EEDLQIATKTICQLTEEKEAQMEELN-------KAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKiITMELQK 388

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226  376 RMMDKLRQNRLEFQKE---REATQELIEDLRRELEHLQMYKLDCERPGRGRSSSGLgeFNARAREV-ELEHEVKRLKQEN 451
Cdd:pfam05483 389 KSSELEEMTKFKNNKEvelEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFL--LQAREKEIhDLEIQLTAIKTSE 466

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564373226  452 HKLRDQNDDLNGQILSLSLYEAKnLFATQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQ 514
Cdd:pfam05483 467 EHYLKEVEDLKTELEKEKLKNIE-LTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQ 528
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
310-513 7.29e-05

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.80  E-value: 7.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 310 LEREKSTELELLNTRVQQLEEEN-----TDLRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRL------KDEMDLYKRMM 378
Cdd:PRK02224 181 VLSDQRGSLDQLKAQIEEKEEKDlherlNGLESELAELDEEIERYEEQREQARETRDEADEVLeeheerREELETLEAEI 260

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 379 DKLRQNRLEFQKEREATQELIEDLRRELEHLQmykldcERPGRGRSSSGLGEFNARA---REVELEHEVKRLKQENHKLR 455
Cdd:PRK02224 261 EDLRETIAETEREREELAEEVRDLRERLEELE------EERDDLLAEAGLDDADAEAveaRREELEDRDEELRDRLEECR 334

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564373226 456 DQNDDLNGQILSLsLYEAKNLFATQTKAQSLAAEIDT---ASRDELMEALKEQEEINFRLR 513
Cdd:PRK02224 335 VAAQAHNEEAESL-REDADDLEERAEELREEAAELESeleEAREAVEDRREEIEELEEEIE 394
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
280-472 1.42e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 280 ELEEMVKDQETTAEQALEEEARRHREVycKLEREKSTELELLNTRVQQLEEENTDLRTTVTRLKSQTEKLDEERQRMSDR 359
Cdd:COG4717   54 EADELFKPQGRKPELNLKELKELEEEL--KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 360 LEDTSLR--LKDEMDLYKRMMDKLRQnRLEFQKEREATQELIEDLRRELEHLQMYKLDCERPGRGRSSSGLGEfnARARE 437
Cdd:COG4717  132 QELEALEaeLAELPERLEELEERLEE-LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE--LQQRL 208

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 564373226 438 VELEHEVKRLKQENHKLRDQNDDLNGQILSLSLYE 472
Cdd:COG4717  209 AELEEELEEAQEELEELEEELEQLENELEAAALEE 243
PTZ00121 PTZ00121
MAEBL; Provisional
 268-532 1.62e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.75  E-value: 1.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226  268 KLENVQLVHRVHELEEMVKDQETTAEQALEEEARRHREVYCKLEREKSTELE-LLNTRVQQLEEENTDLRTTVTRLKSQT 346
Cdd:PTZ00121 1559 KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEeAKKAEEAKIKAEELKKAEEEKKKVEQL 1638

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226  347 EKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRRELEhlqmykldcERPGRGRSSS 426
Cdd:PTZ00121 1639 KKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAE---------EAKKAEELKK 1709

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226  427 GLGEFNARAREVELEHEVKRLKQENHKLRDQNDDLNGQILSLSLYEAKNLFATQTKAQSLAAEIDTASRDELMEALKEQE 506
Cdd:PTZ00121 1710 KEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEED 1789

                         250       260
                  ....*....|....*....|....*.
gi 564373226  507 EinfRLRQYMDKIILAILDHNPSILE 532
Cdd:PTZ00121 1790 E---KRRMEVDKKIKDIFDNFANIIE 1812
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 271-460 2.30e-04

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: 43.96  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226  271 NVQLVHRVHELEEmvkdQETTAEQALEEEARRHR------EVYCKLEREKSTELELLNTRVQQLEEENTDLRTTVTRLKS 344
Cdd:pfam05557  50 NQELQKRIRLLEK----REAEAEEALREQAELNRlkkkylEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAEL 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226  345 QTEKLDEERQRMSDRLEDTSLRLKDemdlykrmMDKLRQNRLEFQKEREATQELIEDLRRELehlQMYKLDcerpgrgrs 424
Cdd:pfam05557 126 ELQSTNSELEELQERLDLLKAKASE--------AEQLRQNLEKQQSSLAEAEQRIKELEFEI---QSQEQD--------- 185

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 564373226  425 SSGLGEFNAR-AREVELEHEVKRLKQENHKLRDQNDD 460
Cdd:pfam05557 186 SEIVKNSKSElARIPELEKELERLREHNKHLNENIEN 222
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 294-410 4.20e-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: 42.22  E-value: 4.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 294 QALEEEARRHREVYCKLERE---KSTELELLNTRVQQLEEENTDLRTTVTRLKSQTEKLDEERQRMSDRLED-TSLR--- 366
Cdd:COG1579   13 QELDSELDRLEHRLKELPAElaeLEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvRNNKeye 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 564373226 367 -LKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRRELEHLQ 410
Cdd:COG1579   93 aLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE 137
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 241-508 4.42e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 4.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   241 EKVSFLEKKVTELENDSLASGGLKSKLKLENVQLVHRVHELEEMVKDQETTAEQALEEEARrhrevycklEREKSTELEl 320
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEK---------LKERLEELE- 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   321 lnTRVQQLEEENTDLRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDE-MDLYKRMMDKLRQNRLEFQKE-REATQEL 398
Cdd:TIGR02169  744 --EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSrIPEIQAELSKLEEEVSRIEARlREIEQKL 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   399 ------IEDLRRELEHLQMYKLDCERPgrgRSSSGLGEFNARAREVELEHEVKRLKQENHKLRDQNDDLNGQILSLSlye 472
Cdd:TIGR02169  822 nrltleKEYLEKEIQELQEQRIDLKEQ---IKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE--- 895

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 564373226   473 aKNLFATQTKAQSLAAEIDTAsrDELMEALKEQEEI 508
Cdd:TIGR02169  896 -AQLRELERKIEELEAQIEKK--RKRLSELKAKLEA 928
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 253-510 7.69e-04

Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227569 [Multi-domain]  Cd Length: 669  Bit Score: 42.36  E-value: 7.69e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 253 LENDSLASGGLKSKLKL--ENVQLVHRVHELEEMVKDQETTAEQALEEEARRHREVYCKLEREK---------------- 314
Cdd:COG5244  393 LEDNKDVTLILKILHPIleTTVPKLLAFLRTNSNFNDNDTLCLIGSLYEIARIDKLIGKEEISKqdnrlflypscditls 472

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 315 -------STELELLNTRVQQLEEENTDLRTTVTRLKSQTEKLDEErQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRL- 386
Cdd:COG5244  473 siltilfSDKLEVFFQGIESLLENITIFPEQPSQQTSDSENIKEN-SLLSDRLNEENIRLKEVLVQKENMLTEETKIKIi 551

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 387 -EFQKEREATQELIEDLRRELEHLQMyKLDCERPgrgrsssglgefnararevELEHEVKRLKQENHKLRDQNdDLNGQI 465
Cdd:COG5244  552 iGRDLERKTLEENIKTLKVELNNKNN-KLKEENF-------------------NLVNRLKNMELKLYQIKDNN-TLNKIY 610

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 564373226 466 LSL--SLYEAKNLFATQTKAQsLAAEIDTASRDELMEALKE--QEEINF 510
Cdd:COG5244  611 LDLvsEIMELRETIRRQIKEQ-KRVSIDFSWLDELKQPFKEhiIEMFNF 658
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
269-450 1.02e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.82  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226  269 LENVQLVHRVHELEEMVKDQETTAEQaLEEEARRHREVYCKLER-----------EKSTELELLNTRVQQLEEENTDLRT 337
Cdd:COG4913   231 VEHFDDLERAHEALEDAREQIELLEP-IRELAERYAAARERLAEleylraalrlwFAQRRLELLEAELEELRAELARLEA 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226  338 TVTRLKSQTEKLDEERQRMSDRLEDTSL----RLKDEMDLYKRMMDKLRQNRLEFQK-------EREATQELIEDLRREL 406
Cdd:COG4913   310 ELERLEARLDALREELDELEAQIRGNGGdrleQLEREIERLERELEERERRRARLEAllaalglPLPASAEEFAALRAEA 389

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 564373226  407 EHLQmykldcERPGRGRSSSGLGEFNARAREVELEHEVKRLKQE 450
Cdd:COG4913   390 AALL------EALEEELEALEEALAEAEAALRDLRRELRELEAE 427
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 229-410 1.04e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 1.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 229 RDSIDSCDNDITEKVSFLEKKVTELENDSLAS----GGLKSKLKLENVQLVHRVHELEEMVKDQETTAEQALEE------ 298
Cdd:COG4942   50 EKALLKQLAALERRIAALARRIRALEQELAALeaelAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllspe 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 299 ---EARRHREVYCKLEREKSTELELLNTRVQQLEEENTDLRTTVTRLKSQTEKLDEERQrmsdrledtslRLKDEMDLYK 375
Cdd:COG4942  130 dflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA-----------ALEALKAERQ 198

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 564373226 376 RMMDKLRQNRLEFQKEREATQELIEDLRRELEHLQ 410
Cdd:COG4942  199 KLLARLEKELAELAAELAELQQEAEELEALIARLE 233
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 280-488 1.06e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 1.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 280 ELEEmVKDQETTAEQALEEEARRHREVYCKLErEKSTELELLNTRVQQLEEE----NTDLRTTVTRLKSQTEKLDEERQR 355
Cdd:COG4942   28 ELEQ-LQQEIAELEKELAALKKEEKALLKQLA-ALERRIAALARRIRALEQElaalEAELAELEKEIAELRAELEAQKEE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 356 MSDRL-----------------EDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRRELEHLQMYKLDCER 418
Cdd:COG4942  106 LAELLralyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEE 185

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564373226 419 pgrgRSSSGLGEFNARAREV-ELEHEVKRLKQENHKLRDQNDDLNGQILSLSLYEAKNlfATQTKAQSLAA 488
Cdd:COG4942  186 ----ERAALEALKAERQKLLaRLEKELAELAAELAELQQEAEELEALIARLEAEAAAA--AERTPAAGFAA 250
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
319-514 1.08e-03

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 41.93  E-value: 1.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 319 ELLNTRVQQLEEENTDLRTTVTRlkSQTEKLDEERQRMSDRLEDTSLRLKD------------EMDLYKRMMDKLRQNRL 386
Cdd:COG3206  152 AVANALAEAYLEQNLELRREEAR--KALEFLEEQLPELRKELEEAEAALEEfrqknglvdlseEAKLLLQQLSELESQLA 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 387 EFQKEREATQELIEDLRRELehlqmyKLDCERPGRGRSSSGLGEFNARAREVELEHEVKRLK-QENH----KLRDQNDDL 461
Cdd:COG3206  230 EARAELAEAEARLAALRAQL------GSGPDALPELLQSPVIQQLRAQLAELEAELAELSARyTPNHpdviALRAQIAAL 303

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564373226 462 NGQILSLSlyeAKNLFATQTKAQSLAAEIDT--ASRDELMEALKEQEEINFRLRQ 514
Cdd:COG3206  304 RAQLQQEA---QRILASLEAELEALQAREASlqAQLAQLEARLAELPELEAELRR 355
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 275-407 1.24e-03

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: 41.65  E-value: 1.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226  275 VHRVHELEEMVKDQETTAEQALEE-EARRHREVyckLEREKSTELELLNTRVQQLEEENTDLRttvtrlKSQTEKLDEER 353
Cdd:pfam17380 374 ISRMRELERLQMERQQKNERVRQElEAARKVKI---LEEERQRKIQQQKVEMEQIRAEQEEAR------QREVRRLEEER 444

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 564373226  354 QRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRRELE 407
Cdd:pfam17380 445 AREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE 498
ASY3-like pfam20435
Meiosis-specific protein ASY3-like; This entry represents a group of plant meiosis-specific ...
 244-367 1.40e-03

Meiosis-specific protein ASY3-like; This entry represents a group of plant meiosis-specific proteins, such as AtASY3 from Arabidopsis and PAIR3 from rice. They are coiled-coil domain proteins required for normal meiosis. PAIR3 is an axial element and part of the synaptonemal complex (SC) that forms between homologous chromosomes during meiosis. Members of this family are homologs of SCYP2 from vertebrates and fungal Red1/Rec10.


Pssm-ID: 466584 [Multi-domain]  Cd Length: 793  Bit Score: 41.41  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226  244 SFLEKKVTELendsLASGGLKSKLKLENVQ--LVHRVHELEEMVKDQETTAEQALEEEARRHREVYCKLEREKSTELELL 321
Cdd:pfam20435 646 SAAEKKSSEI----IASVSEEIHLELENIKshIITEAGKTSNLAKTKRKHAETRLQEQEEKMRMIHEKFKDDVSHHLEDF 721

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 564373226  322 NTRVQQLEEENTDLRTTVTRLKSQTEKLDEERQ-RMSDRLEDTSLRL 367
Cdd:pfam20435 722 KSTIEELEANQSELKGSIKKQRTSHQKLIAHFEgGIETKLDDATKRI 768
PRK12704 PRK12704
phosphodiesterase; Provisional
 279-408 1.61e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 279 HELEEMVKDQETTAEQALEEEARRHREVYCKLEREKSTELELLNTRVQQLEEEntdLRTTVTRLKSQTEKLDEERQRMSD 358
Cdd:PRK12704  38 EEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKR---LLQKEENLDRKLELLEKREEELEK 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564373226 359 RLEDTSlRLKDEMDLYKRMMDKLRQNRLE-------FQKErEATQELIEDLRRELEH 408
Cdd:PRK12704 115 KEKELE-QKQQELEKKEEELEELIEEQLQelerisgLTAE-EAKEILLEKVEEEARH 169
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 241-405 1.66e-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: 41.31  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   241 EKVSfLEKKVTELENDSLASGGLKSKLKLENVQLVHRVHELEEMVKDQETTAeQALEEEARRHREVYCKLE----REKST 316
Cdd:pfam01576  125 EKVT-TEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKA-KSLSKLKNKHEAMISDLEerlkKEEKG 202

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   317 ELELLNTRvQQLEEENTDLRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQnrLEFQkereaTQ 396
Cdd:pfam01576  203 RQELEKAK-RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRE--LEAQ-----IS 274


                   ....*....
gi 564373226   397 ELIEDLRRE 405
Cdd:pfam01576  275 ELQEDLESE 283
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 280-410 1.74e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 40.43  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 280 ELEEMVKDQETTAEQALEEEARRHREVYCKLEREKSTELEllnTRVQQLEeenTDLRTTVTRLKSQTEKLDEERQRMSDR 359
Cdd:cd22656   95 EILELIDDLADATDDEELEEAKKTIKALLDDLLKEAKKYQ---DKAAKVV---DKLTDFENQTEKDQTALETLEKALKDL 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564373226 360 LEDTSLRL-KDEMDLYKRMMDKLRQN-RLEFQKEREATQELIEDLRRELEHLQ 410
Cdd:cd22656  169 LTDEGGAIaRKEIKDLQKELEKLNEEyAAKLKAKIDELKALIADDEAKLAAAL 221
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 240-410 1.77e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 1.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 240 TEKVSFLEKKVTELENDSLASGGLKSKLKLENVQLVHRVHELEEMVKDQETTAEQALEEEARRHREvycklEREKSTELE 319
Cdd:COG1196  308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE-----LAEAEEELE 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 320 LLNTRVQQLEEENTDLRTTVTRLKSQTEKLDEERQRMSD---RLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQ 396
Cdd:COG1196  383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEeleELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462

                        170
                 ....*....|....
gi 564373226 397 ELIEDLRRELEHLQ 410
Cdd:COG1196  463 ELLAELLEEAALLE 476
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
280-462 2.55e-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: 2.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 280 ELEEmVKDQETTAEQALEEEARRHREVycKLEREKSTELELLNTRVQQLEEENTDLRTTVTRLKSQTEKLDEERQRMSDR 359
Cdd:COG3206  183 QLPE-LRKELEEAEAALEEFRQKNGLV--DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 360 LEDTSL-RLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRRELEhlqmykldcERPGRGRSSSGLGEFNARAREV 438
Cdd:COG3206  260 LQSPVIqQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQ---------QEAQRILASLEAELEALQAREA 330

                        170       180
                 ....*....|....*....|....
gi 564373226 439 ELEHEVKRLKQENHKLRDQNDDLN 462
Cdd:COG3206  331 SLQAQLAQLEARLAELPELEAELR 354
PRK10361 PRK10361
DNA recombination protein RmuC; Provisional
 291-522 2.64e-03

DNA recombination protein RmuC; Provisional


Pssm-ID: 182409 [Multi-domain]  Cd Length: 475  Bit Score: 40.35  E-value: 2.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 291 TAEQALEEEARRhREVYCKLEREKS---------TELELLNTRVQQLEEENT----DLRTTVTRLKS-QTEKLDEERQRM 356
Cdd:PRK10361  27 HAQQKAEQLAER-EEMVAELSAAKQqitqsehwrAECELLNNEVRSLQSINTsleaDLREVTTRMEAaQQHADDKIRQMI 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 357 SdrledTSLRLKDEMD-LYKRMMDKlrQNRLEFQKEREATQELIEDLRRELEHLQMYKLDcerpgrgrsssglgEFNARA 435
Cdd:PRK10361 106 N-----SEQRLSEQFEnLANRIFEH--SNRRVDEQNRQSLNSLLSPLREQLDGFRRQVQD--------------SFGKEA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 436 REVE-LEHEVKRLKQENHKLRDQNDDLN-------------GQILSLSLYEAKNLFATQTKAQSLAAEIDTASRdelmea 501
Cdd:PRK10361 165 QERHtLAHEIRNLQQLNAQMAQEAINLTralkgdnktqgnwGEVVLTRVLEASGLREGYEYETQVSIENDARSR------ 238

                        250       260
                 ....*....|....*....|.
gi 564373226 502 lkEQEEINFRLRQYMDKIILA 522
Cdd:PRK10361 239 --MQPDVIVRLPQGKDVVIDA 257
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 273-398 3.78e-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: 40.12  E-value: 3.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226  273 QLVHRVHELEEMVKDQETTAEQALEEEARRHREVYCKLerekSTELELLNTRVQQLEEENTDLRTTVTRLK-----SQTE 347
Cdd:pfam07111 506 QEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASV----GQQLEVARQGQQESTEEAASLRQELTQQQeiygqALQE 581

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 564373226  348 KLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQEL 398
Cdd:pfam07111 582 KVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQEL 632
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
277-410 4.64e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.02  E-value: 4.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 277 RVHELEEMVKDQETTAeQALEEEARRHREVYCKLEREKST---ELELLNtRVQQLEEENTDLRTTVTRL----KSQTEKL 349
Cdd:PRK02224 545 RAAELEAEAEEKREAA-AEAEEEAEEAREEVAELNSKLAElkeRIESLE-RIRTLLAAIADAEDEIERLrekrEALAELN 622

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564373226 350 DEERQRMSDRLEDTSlRLKDEMDlyKRMMDKLRQNRLEFQKEREATQELIEDLRRELEHLQ 410
Cdd:PRK02224 623 DERRERLAEKRERKR-ELEAEFD--EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQ 680
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 225-448 5.10e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.67  E-value: 5.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   225 EDLFRDSIDSCDNDITEKVSFLEKKVTELENDSLASGGLKSKLKLENVQLVHRVHELEEMVKDqettAEQALEEEARRHR 304
Cdd:TIGR02169  782 NDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID----LKEQIKSIEKEIE 857

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   305 EVYCKLErEKSTELELLNTRVQQLEEENTDLRTTVTRLKSQTEKLDEERQRMSDRLEDtslrlkdemdlyKRMMDKLRQN 384
Cdd:TIGR02169  858 NLNGKKE-ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEK------------KRKRLSELKA 924

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564373226   385 RLEFQKEREATqelIEDLRREL-----EHLQMYKLDCERPGRGRSSSGLGEFNARAREvELEHEVKRLK 448
Cdd:TIGR02169  925 KLEALEEELSE---IEDPKGEDeeipeEELSLEDVQAELQRVEEEIRALEPVNMLAIQ-EYEEVLKRLD 989
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 294-509 5.85e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.67  E-value: 5.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   294 QALEEEARRHREvycKLEREKSTELE--------------LLNTRVQQLEEENTDLRTTVTRLKSQTEKLDEERQRMSDR 359
Cdd:TIGR02169  190 DLIIDEKRQQLE---RLRREREKAERyqallkekreyegyELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226   360 LEDTSLRLKdemDLYKRMMDKLRQNRLEFQKEREATQELIEDLRRELEhlqmyklDCERPGRgrsssglgefNARAREVE 439
Cdd:TIGR02169  267 LEEIEQLLE---ELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIA-------EKERELE----------DAEERLAK 326

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564373226   440 LEHEVKRLKQENHKLRDQNDDLNGQILSLSlYEAKNLFATQTKAQSLAAEIDT---ASRDELMEALKEQEEIN 509
Cdd:TIGR02169  327 LEAEIDKLLAEIEELEREIEEERKRRDKLT-EEYAELKEELEDLRAELEEVDKefaETRDELKDYREKLEKLK 398
mukB PRK04863
chromosome partition protein MukB;
273-407 7.21e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.17  E-value: 7.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226  273 QLVHRVHELEEMVKdQETTAEQALEEEARRHR------EVYCKLEREKSTELELLNTRVQQLEEENTDLRTTVTRLKSQT 346
Cdd:PRK04863  517 QLRMRLSELEQRLR-QQQRAERLLAEFCKRLGknlddeDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARI 595

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564373226  347 EKLDEERQR---MSDRLEdtslRLKD---EMDLYKRMMDKLRQNRLEfqKEREATQE--LIEDLRRELE 407
Cdd:PRK04863  596 QRLAARAPAwlaAQDALA----RLREqsgEEFEDSQDVTEYMQQLLE--RERELTVErdELAARKQALD 658
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
239-455 7.25e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 7.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 239 ITEKVSFLEKKVTELENDSlasGGLKSKLK-LENV--QLVHRVHELEEMVKDQETTAEQALE-EEARRHREVYCKLEREK 314
Cdd:PRK03918 236 LKEEIEELEKELESLEGSK---RKLEEKIReLEERieELKKEIEELEEKVKELKELKEKAEEyIKLSEFYEEYLDELREI 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 315 STELELLNTRVQQLEEENTDLRTTVTRLKSQTEKLDEERQRMSD-----RLEDTSLRLKDEMDLYK------------RM 377
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEleerhELYEEAKAKKEELERLKkrltgltpekleKE 392

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 378 MDKLRQNRLEFQKE-REATQEL------IEDLRRELEHLQMYKLDCERPGRGRSSSGLGEFNARARE--VELEHEVKRLK 448
Cdd:PRK03918 393 LEELEKAKEEIEEEiSKITARIgelkkeIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAelKRIEKELKEIE 472


                 ....*..
gi 564373226 449 QENHKLR 455
Cdd:PRK03918 473 EKERKLR 479
PRK12705 PRK12705
hypothetical protein; Provisional
 276-418 7.39e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 38.92  E-value: 7.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 276 HRVHELEEMVKDQETTAEQALEEEARRHREvycklerEKSTELELLNTRVQQLEEENTDLRTTVTRLKSQTEKLDEERQR 355
Cdd:PRK12705  48 EKLEAALLEAKELLLRERNQQRQEARRERE-------ELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARELE 120

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564373226 356 MSDRLEDTSLRLKdemdlykrmmdklrqnRLEFQKEREATQELIEDLRRELEH--LQMYKLDCER 418
Cdd:PRK12705 121 LEELEKQLDNELY----------------RVAGLTPEQARKLLLKLLDAELEEekAQRVKKIEEE 169
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
293-519 9.09e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 9.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 293 EQALEEEARRHREVYCKLEREKSTELELLNTRVQQLEEENTDLRTTVTRLKSQTEKLDEERQRMSDrledtslrLKDEMD 372
Cdd:COG4717   48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEE--------LREELE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564373226 373 LYKRMmdklrQNRLEFQKEREATQELIEDLRRELEHLQmykldcerpgrgrsssglgefNARAREVELEHEVKRLKQENH 452
Cdd:COG4717  120 KLEKL-----LQLLPLYQELEALEAELAELPERLEELE---------------------ERLEELRELEEELEELEAELA 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564373226 453 KLRDQnddLNGQILSLSLYEAKNLFATQTKAQSLAAEIdtasrDELMEALKEQEEINFRLRQYMDKI 519
Cdd:COG4717  174 ELQEE---LEELLEQLSLATEEELQDLAEELEELQQRL-----AELEEELEEAQEELEELEEELEQL 232
 
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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