NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|568974136|ref|XP_006533467|]
View 

rab11 family-interacting protein 4 isoform X3 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 492-532 9.70e-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: 62.36  E-value: 9.70e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568974136  492 SRDELMEALKEQEEINFRLRQYMDKIILAILDHNPSILEIK 532
Cdd:pfam09457   1 SRDELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEVP 41
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 235-517 5.42e-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: 5.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   235 NDITEKVSFLEKKVTELENDSLTSGGLKSKLKQENMQLVHRVHELEEMVKDQETTAEQALEEEARRHREVYCKLEREKST 314
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   315 ELEL----------------LNTRVQQLEEENTDLRTTVARLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDK 378
Cdd:TIGR02168  767 EERLeeaeeelaeaeaeieeLEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   379 LRQNRLE---FQKEREATQELIEDLRRELEHLQMYKldcERPGRGRSSSGLGEFNARAREVELEHEVKRLKQENHKLRDQ 455
Cdd:TIGR02168  847 IEELSEDiesLAAEIEELEELIEELESELEALLNER---ASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568974136   456 NDDLNGQILSLSLyEAKNLFATQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQYMDKI 517
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 ...
 492-532 9.70e-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: 62.36  E-value: 9.70e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568974136  492 SRDELMEALKEQEEINFRLRQYMDKIILAILDHNPSILEIK 532
Cdd:pfam09457   1 SRDELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEVP 41
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 235-517 5.42e-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: 5.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   235 NDITEKVSFLEKKVTELENDSLTSGGLKSKLKQENMQLVHRVHELEEMVKDQETTAEQALEEEARRHREVYCKLEREKST 314
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   315 ELEL----------------LNTRVQQLEEENTDLRTTVARLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDK 378
Cdd:TIGR02168  767 EERLeeaeeelaeaeaeieeLEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   379 LRQNRLE---FQKEREATQELIEDLRRELEHLQMYKldcERPGRGRSSSGLGEFNARAREVELEHEVKRLKQENHKLRDQ 455
Cdd:TIGR02168  847 IEELSEDiesLAAEIEELEELIEELESELEALLNER---ASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568974136   456 NDDLNGQILSLSLyEAKNLFATQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQYMDKI 517
Cdd:TIGR02168  924 LAQLELRLEGLEV-RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 244-505 5.44e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 5.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 244 LEKKVTELENDSLTSGGLKSKLKQENMQLVHRVHELEEMVKDQETTAEQALEEEARrhrevyckLEREKSTELELLNTRV 323
Cdd:COG1196  265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE--------LEEELAELEEELEELE 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 324 QQLEEENTDLRTTVARLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQnRLEFQKEREATQELIEDLRRE 403
Cdd:COG1196  337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA-AAELAAQLEELEEAEEALLER 415

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 404 LEHLQMYKLDCERpgrgrsssglgefNARAREVELEHEVKRLKQENHKLRDQNDDLNGQILSLSLYEAKNLFATQTKAQS 483
Cdd:COG1196  416 LERLEEELEELEE-------------ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482

                        250       260
                 ....*....|....*....|..
gi 568974136 484 LAAEIDTASRDELMEALKEQEE 505
Cdd:COG1196  483 LEELAEAAARLLLLLEAEADYE 504
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
236-508 2.85e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 236 DITEKVSFLEKKVTELENDSLTSGGLKSKLKqenmQLVHRVHELEEMVKDQETTaeQALEEEARRHREVYCKLEREK-ST 314
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLK----ELEKRLEELEERHELYEEA--KAKKEELERLKKRLTGLTPEKlEK 391

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 315 ELELLNTRVQQLEEENTDLRTTVARLKSQTEKLDE--ERQRMSDRLEDTSLRLKDEMDlYKRMMDKLRQNRLEFQKEREA 392
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKaiEELKKAKGKCPVCGRELTEEH-RKELLEEYTAELKRIEKELKE 470

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 393 TQELIEDLRRELEHLQMYKLDCERPGRGRS-SSGLGEFNARAREVELEhEVKRLKQENHKLRDQNDDLNGQILSLsLYEA 471
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESELIKLKElAEQLKELEEKLKKYNLE-ELEKKAEEYEKLKEKLIKLKGEIKSL-KKEL 548

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 568974136 472 KNLFATQTKAQSLAAEIDTASRdELMEALKEQEEINF 508
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEE-ELAELLKELEELGF 584
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 235-512 3.41e-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: 46.64  E-value: 3.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136  235 NDITEKVSFLEKKVTELEN-------------DSLTSGGLKSKLKQENM-QLVHRVHELEEMVKD------QETTAEQAL 294
Cdd:pfam05483 236 NDKEKQVSLLLIQITEKENkmkdltflleesrDKANQLEEKTKLQDENLkELIEKKDHLTKELEDikmslqRSMSTQKAL 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136  295 EEEARRHREVYCKLEREKSTELELLNTRVQQLEEENTDLRTTVARLKsqtEKLDEERQRM---SDRLEDTSLRLKDEMDL 371
Cdd:pfam05483 316 EEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLE---ELLRTEQQRLeknEDQLKIITMELQKKSSE 392

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136  372 YKRMMdKLRQNRlEFQKErEATQELIEDLRRELEHLQMYKLDCERPGRGRSSSGLgeFNARAREV-ELEHEVKRLKQENH 450
Cdd:pfam05483 393 LEEMT-KFKNNK-EVELE-ELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFL--LQAREKEIhDLEIQLTAIKTSEE 467

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568974136  451 KLRDQNDDLNGQILSLSLYEAKnLFATQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQ 512
Cdd:pfam05483 468 HYLKEVEDLKTELEKEKLKNIE-LTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQ 528
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 278-408 2.92e-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: 40.05  E-value: 2.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 278 ELEEMVKDQETTAEQALEEEARRHREVYCKLEREKSTELEllnTRVQQLEeenTDLRTTVARLKSQTEKLDEERQRMSDR 357
Cdd:cd22656   95 EILELIDDLADATDDEELEEAKKTIKALLDDLLKEAKKYQ---DKAAKVV---DKLTDFENQTEKDQTALETLEKALKDL 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568974136 358 LEDTSLRL-KDEMDLYKRMMDKLRQN-RLEFQKEREATQELIEDLRRELEHLQ 408
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 ...
 492-532 9.70e-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: 62.36  E-value: 9.70e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 568974136  492 SRDELMEALKEQEEINFRLRQYMDKIILAILDHNPSILEIK 532
Cdd:pfam09457   1 SRDELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEVP 41
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 235-517 5.42e-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: 5.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   235 NDITEKVSFLEKKVTELENDSLTSGGLKSKLKQENMQLVHRVHELEEMVKDQETTAEQALEEEARRHREVYCKLEREKST 314
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   315 ELEL----------------LNTRVQQLEEENTDLRTTVARLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDK 378
Cdd:TIGR02168  767 EERLeeaeeelaeaeaeieeLEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   379 LRQNRLE---FQKEREATQELIEDLRRELEHLQMYKldcERPGRGRSSSGLGEFNARAREVELEHEVKRLKQENHKLRDQ 455
Cdd:TIGR02168  847 IEELSEDiesLAAEIEELEELIEELESELEALLNER---ASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568974136   456 NDDLNGQILSLSLyEAKNLFATQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQYMDKI 517
Cdd:TIGR02168  924 LAQLELRLEGLEV-RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 244-505 5.44e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.18  E-value: 5.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 244 LEKKVTELENDSLTSGGLKSKLKQENMQLVHRVHELEEMVKDQETTAEQALEEEARrhrevyckLEREKSTELELLNTRV 323
Cdd:COG1196  265 LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE--------LEEELAELEEELEELE 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 324 QQLEEENTDLRTTVARLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQnRLEFQKEREATQELIEDLRRE 403
Cdd:COG1196  337 EELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRA-AAELAAQLEELEEAEEALLER 415

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 404 LEHLQMYKLDCERpgrgrsssglgefNARAREVELEHEVKRLKQENHKLRDQNDDLNGQILSLSLYEAKNLFATQTKAQS 483
Cdd:COG1196  416 LERLEEELEELEE-------------ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAEL 482

                        250       260
                 ....*....|....*....|..
gi 568974136 484 LAAEIDTASRDELMEALKEQEE 505
Cdd:COG1196  483 LEELAEAAARLLLLLEAEADYE 504
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 261-512 9.57e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 9.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 261 LKSKLKQENMQLVHRVHELEEMVKDQETTAEQALEEEARRHREVYCKLERE---KSTELELLNTRVQQLEEENTDLRTTV 337
Cdd:COG1196  232 LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEleeAQAEEYELLAELARLEQDIARLEERR 311

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 338 ARLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRRELEHLQMYKLDCERP 417
Cdd:COG1196  312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 418 GRGRSSSGLGEFNARAREVELEHEVKRLKQENHKLRDQNDDLNGQILSLSLyEAKNLFATQTKAQSLAAEIDTASRDELM 497
Cdd:COG1196  392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEE-ALEEAAEEEAELEEEEEALLELLAELLE 470

                        250
                 ....*....|....*
gi 568974136 498 EALKEQEEINFRLRQ 512
Cdd:COG1196  471 EAALLEAALAELLEE 485
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
271-408 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 568974136 271 QLVHRVHELEEMVKD-----QETTAEQALEEEARRHREVYCKLEREKStELELLNTRVQQLEEENTDLRTTVARLKSQTE 345
Cdd:COG4717   92 ELQEELEELEEELEEleaelEELREELEKLEKLLQLLPLYQELEALEA-ELAELPERLEELEERLEELRELEEELEELEA 170

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568974136 346 KLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRRELEHLQ 408
Cdd:COG4717  171 ELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
279-413 4.01e-07

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 52.94  E-value: 4.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 279 LEEMVKDQETTAEQALEEEARRHREVYCKLEREKSTELELLNTRVQQLEEENTDLRTTVARLKSQTEKLDEERQRMSDRl 358
Cdd:COG2433  378 IEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSE- 456

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 568974136 359 EDTSLRLKDEMDLYKRMMDKLRqnrlefqKEREATQELIEDLRRELEHL-QMYKLD 413
Cdd:COG2433  457 ERREIRKDREISRLDREIERLE-------RELEEERERIEELKRKLERLkELWKLE 505
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
238-449 6.17e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 52.22  E-value: 6.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136  238 TEKVSFLEKKVTELENDSLTSGGLKSKLKQENMQLVHRVHELEEMVKDQETTAE-QALEEEARRHREVYCKLEREKST-- 314
Cdd:COG4913   609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvASAEREIAELEAELERLDASSDDla 688

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136  315 ----ELELLNTRVQQLEEENTDLRTTVARLKSQTEKLDEERQRMSDRLEDTSLRLKDEM--DLYKR----MMDKLRQN-R 383
Cdd:COG4913   689 aleeQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELraLLEERfaaaLGDAVERElR 768

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568974136  384 LEFQKEREATQELIEDLRRELEHLQM-YKLD--CERPGRGRSSSGLGEFNARARE------VELEHEVKRLKQEN 449
Cdd:COG4913   769 ENLEERIDALRARLNRAEEELERAMRaFNREwpAETADLDADLESLPEYLALLDRleedglPEYEERFKELLNEN 843
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 230-466 1.14e-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: 1.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   230 IDSCDNDITEKVSF---LEKKVTELENDSLTSGGLKSKLKQENMQLVHRVHELE---EMVKDQETTAEQALEEEARRHRE 303
Cdd:TIGR02168  262 LQELEEKLEELRLEvseLEEEIEELQKELYALANEISRLEQQKQILRERLANLErqlEELEAQLEELESKLDELAEELAE 341

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   304 VYCKLER-------------EKSTELELLNTRVQQLEEENTDLRTTVARLKSQTEKLDEERQRMSDRLEDTSLRLkdemd 370
Cdd:TIGR02168  342 LEEKLEElkeelesleaeleELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRR----- 416

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   371 lykrmmDKLRQNRLEFQK-----EREATQELIEDLRRELEHLQmykldcerpgrgrsssgLGEFNARAREVELEHEVKRL 445
Cdd:TIGR02168  417 ------ERLQQEIEELLKkleeaELKELQAELEELEEELEELQ-----------------EELERLEEALEELREELEEA 473

                          250       260
                   ....*....|....*....|.
gi 568974136   446 KQENHKLRDQNDDLNGQILSL 466
Cdd:TIGR02168  474 EQALDAAERELAQLQARLDSL 494
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 266-408 2.20e-06

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: 50.84  E-value: 2.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   266 KQENMQLVHRVHELEEMVKDQETTAEQaLEEEARRHREVYCKLEREKSTELELLNTRVQQLEEENTDLRTTVARLKSQTE 345
Cdd:TIGR02169  314 ERELEDAEERLAKLEAEIDKLLAEIEE-LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568974136   346 KLD------EERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRRELEHLQ 408
Cdd:TIGR02169  393 KLEklkreiNELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 272-512 2.76e-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: 2.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   272 LVHRVHELEEMVKDQETTAEQALEEEARRHREVyckleREKSTELELLNTRVQQLEEENTDLRTTVARLKSQTEKLDEER 351
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEELTAEL-----QELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   352 QRMSDR---LEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRRELEHLQMYKldcerpgrgrsssglge 428
Cdd:TIGR02168  305 QILRERlanLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL----------------- 367

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   429 FNARAREVELEHEVKRLKQENHKLRDQNDDLNGQILSL-SLYE--AKNLFATQTKAQSLAAEIDTASRDELMEALKEQEE 505
Cdd:TIGR02168  368 EELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLeARLErlEDRRERLQQEIEELLKKLEEAELKELQAELEELEE 447


                   ....*..
gi 568974136   506 INFRLRQ 512
Cdd:TIGR02168  448 ELEELQE 454
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 239-511 3.79e-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: 3.79e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   239 EKVSFLEKKVTELENDSLTSGGLKSKLKQENMQLVHRVHELEEMVKD-----QETTAEQA-LEEEARRHREvycKLEREK 312
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkelYALANEISrLEQQKQILRE---RLANLE 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   313 sTELELLNTRVQQLEEENTDLRTTVARLKSQTEKLDEERQRMSDRLEdtslRLKDEMDLYKRMMDKLRQNRLEFQKEREA 392
Cdd:TIGR02168  316 -RQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE----ELEAELEELESRLEELEEQLETLRSKVAQ 390

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   393 TQELIEDLRRELEhlqmykldcerpgrgrsssglgefNARAREVELEHEVKRLKQENHKLRDQNDDLNGQILSLSLYE-- 470
Cdd:TIGR02168  391 LELQIASLNNEIE------------------------RLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEle 446

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 568974136   471 ------AKNLFATQTKAQSLAAEIDTASRdELMEALKEQEEINFRLR 511
Cdd:TIGR02168  447 eeleelQEELERLEEALEELREELEEAEQ-ALDAAERELAQLQARLD 492
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 251-512 5.86e-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: 49.28  E-value: 5.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   251 LENDSLTSGGLKSK-LKQENMQLVHRVHELEEMVKDQETTAEQAleeearrhrevyckleREKSTELELLNTRVQQLEEE 329
Cdd:TIGR02168  650 LDGDLVRPGGVITGgSAKTNSSILERRREIEELEEKIEELEEKI----------------AELEKALAELRKELEELEEE 713

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   330 NTDLRTT-------VARLKSQTEKLDEERQR---MSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIED 399
Cdd:TIGR02168  714 LEQLRKEleelsrqISALRKDLARLEAEVEQleeRIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQ 793

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   400 LRRELEHLqmykldcerpgrgrsSSGLGEFNARAREV-----ELEHEVKRLKQENHKLRDQNDDLNGQILSLSLyEAKNL 474
Cdd:TIGR02168  794 LKEELKAL---------------REALDELRAELTLLneeaaNLRERLESLERRIAATERRLEDLEEQIEELSE-DIESL 857

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 568974136   475 FATQTKAQSLAAEIdtasRDELMEALKEQEEINFRLRQ 512
Cdd:TIGR02168  858 AAEIEELEELIEEL----ESELEALLNERASLEEALAL 891
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 267-506 6.63e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.16  E-value: 6.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 267 QENMQLVH-RVHELEEMVKDQETTAEQAL------EEEARRHREVYCKLEREKSTELELLNTRVQQLEEENTDLRTTVAR 339
Cdd:COG1196  185 EENLERLEdILGELERQLEPLERQAEKAEryrelkEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAE 264

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 340 LKSQTEKLDEERQRMSDRLEDTS----------LRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRRELEHLQ- 408
Cdd:COG1196  265 LEAELEELRLELEELELELEEAQaeeyellaelARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEe 344

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 409 ---MYKLDCERPGRGRSSSGLGEFNARAREVELEHEVKRLKQENHKLRDQNDDLNGQILSLSLyEAKNLFATQTKAQSLA 485
Cdd:COG1196  345 eleEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEE-AEEALLERLERLEEEL 423

                        250       260
                 ....*....|....*....|.
gi 568974136 486 AEIDTASRDELMEALKEQEEI 506
Cdd:COG1196  424 EELEEALAELEEEEEEEEEAL 444
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
278-523 1.03e-05

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 48.47  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 278 ELEEmVKDQETTAEQALEEEARRHREVycKLEREKSTELELLNTRVQQLEEENTDLRTTVARLKSQTEKLDEERQRMSDR 357
Cdd:COG3206  183 QLPE-LRKELEEAEAALEEFRQKNGLV--DLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 358 LEDTSL-RLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRRELEHlqmykldcerpgrgrsssglgefNARAREV 436
Cdd:COG3206  260 LQSPVIqQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQ-----------------------EAQRILA 316

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 437 ELEHEVKRLKQENHKLRDQNDDLNGQILSLSlyeaknlfATQTKAQSLAAEIDTAsRDELMEALKEQEEInfRLRQYMDK 516
Cdd:COG3206  317 SLEAELEALQAREASLQAQLAQLEARLAELP--------ELEAELRRLEREVEVA-RELYESLLQRLEEA--RLAEALTV 385


                 ....*..
gi 568974136 517 IILAILD 523
Cdd:COG3206  386 GNVRVID 392
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
284-408 1.29e-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: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136  284 KDQETTAEQALEEEARRHREVYCKLEREKSTELELLNTRVQQLEEENTDLRTTVARLKSQTEKLDEERQRMSDRLEDTSL 363
Cdd:COG4913   308 EAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 568974136  364 RLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRRELEHLQ 408
Cdd:COG4913   388 EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
236-508 2.85e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 2.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 236 DITEKVSFLEKKVTELENDSLTSGGLKSKLKqenmQLVHRVHELEEMVKDQETTaeQALEEEARRHREVYCKLEREK-ST 314
Cdd:PRK03918 318 RLEEEINGIEERIKELEEKEERLEELKKKLK----ELEKRLEELEERHELYEEA--KAKKEELERLKKRLTGLTPEKlEK 391

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 315 ELELLNTRVQQLEEENTDLRTTVARLKSQTEKLDE--ERQRMSDRLEDTSLRLKDEMDlYKRMMDKLRQNRLEFQKEREA 392
Cdd:PRK03918 392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKaiEELKKAKGKCPVCGRELTEEH-RKELLEEYTAELKRIEKELKE 470

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 393 TQELIEDLRRELEHLQMYKLDCERPGRGRS-SSGLGEFNARAREVELEhEVKRLKQENHKLRDQNDDLNGQILSLsLYEA 471
Cdd:PRK03918 471 IEEKERKLRKELRELEKVLKKESELIKLKElAEQLKELEEKLKKYNLE-ELEKKAEEYEKLKEKLIKLKGEIKSL-KKEL 548

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 568974136 472 KNLFATQTKAQSLAAEIDTASRdELMEALKEQEEINF 508
Cdd:PRK03918 549 EKLEELKKKLAELEKKLDELEE-ELAELLKELEELGF 584
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 235-512 3.41e-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: 46.64  E-value: 3.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136  235 NDITEKVSFLEKKVTELEN-------------DSLTSGGLKSKLKQENM-QLVHRVHELEEMVKD------QETTAEQAL 294
Cdd:pfam05483 236 NDKEKQVSLLLIQITEKENkmkdltflleesrDKANQLEEKTKLQDENLkELIEKKDHLTKELEDikmslqRSMSTQKAL 315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136  295 EEEARRHREVYCKLEREKSTELELLNTRVQQLEEENTDLRTTVARLKsqtEKLDEERQRM---SDRLEDTSLRLKDEMDL 371
Cdd:pfam05483 316 EEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLE---ELLRTEQQRLeknEDQLKIITMELQKKSSE 392

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136  372 YKRMMdKLRQNRlEFQKErEATQELIEDLRRELEHLQMYKLDCERPGRGRSSSGLgeFNARAREV-ELEHEVKRLKQENH 450
Cdd:pfam05483 393 LEEMT-KFKNNK-EVELE-ELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFL--LQAREKEIhDLEIQLTAIKTSEE 467

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568974136  451 KLRDQNDDLNGQILSLSLYEAKnLFATQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQ 512
Cdd:pfam05483 468 HYLKEVEDLKTELEKEKLKNIE-LTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQ 528
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 239-506 4.99e-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: 4.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   239 EKVSFLEKKVTELENDSLTSGGLKSKLKQENMQLVHRVHELEEMVKDQETTAEQALEEEARrhrevycklEREKSTELEl 318
Cdd:TIGR02169  674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEK---------LKERLEELE- 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   319 lnTRVQQLEEENTDLRTTVARLKSQTEKLDEERQRMSDRLEDTSLRLKDE-MDLYKRMMDKLRQNRLEFQKE-REATQEL 396
Cdd:TIGR02169  744 --EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSrIPEIQAELSKLEEEVSRIEARlREIEQKL 821

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   397 ------IEDLRRELEHLQMYKLDCERPgrgRSSSGLGEFNARAREVELEHEVKRLKQENHKLRDQNDDLNGQILSLSlye 470
Cdd:TIGR02169  822 nrltleKEYLEKEIQELQEQRIDLKEQ---IKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE--- 895

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 568974136   471 aKNLFATQTKAQSLAAEIDTAsrDELMEALKEQEEI 506
Cdd:TIGR02169  896 -AQLRELERKIEELEAQIEKK--RKRLSELKAKLEA 928
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 266-409 7.20e-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: 45.02  E-value: 7.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136  266 KQENMQLVHRVHELEEMVK-----DQETTAEQALEEEARRHREvycKLEREKSTELELLNTRVQQLEEENTDLRTTVARL 340
Cdd:pfam04849 114 REEILQLRHELSKKDDLLQiysndAEESETESSCSTPLRRNES---FSSLHGCVQLDALQEKLRGLEEENLKLRSEASHL 190

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568974136  341 KSQTEKL-DEERQRMSD---RLEDTSLRLKDEMD-LYKRMMDKLRQnrlefqkereatQELIEDLRRELEHLQM 409
Cdd:pfam04849 191 KTETDTYeEKEQQLMSDcveQLSEANQQMAELSEeLARKMEENLRQ------------QEEITSLLAQIVDLQH 252
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 250-458 9.44e-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: 45.12  E-value: 9.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136  250 ELENDSLTSGGLKSKLKQENMQLVHRVHELEEmvkdQETTAEQALEEEARRHR------EVYCKLEREKSTELELLNTRV 323
Cdd:pfam05557  31 ELEKKASALKRQLDRESDRNQELQKRIRLLEK----REAEAEEALREQAELNRlkkkylEALNKKLNEKESQLADAREVI 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136  324 QQLEEENTDLRTTVARLKSQTEKLDEERQRMSDRLEDTSLRLKDemdlykrmMDKLRQNRLEFQKEREATQELIEDLRRE 403
Cdd:pfam05557 107 SCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASE--------AEQLRQNLEKQQSSLAEAEQRIKELEFE 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 568974136  404 LehlQMYKLDcerpgrgrsSSGLGEFNAR-AREVELEHEVKRLKQENHKLRDQNDD 458
Cdd:pfam05557 179 I---QSQEQD---------SEIVKNSKSElARIPELEKELERLREHNKHLNENIEN 222
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
278-470 1.33e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.76  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 278 ELEEMVKDQETTAEQALEEEARRHREVycKLEREKSTELELLNTRVQQLEEENTDLRTTVARLKSQTEKLDEERQRMSDR 357
Cdd:COG4717   54 EADELFKPQGRKPELNLKELKELEEEL--KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 358 LEDTSLR--LKDEMDLYKRMMDKLRQnRLEFQKEREATQELIEDLRRELEHLQMYKLDCERPGRGRSSSGLGEfnARARE 435
Cdd:COG4717  132 QELEALEaeLAELPERLEELEERLEE-LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE--LQQRL 208

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568974136 436 VELEHEVKRLKQENHKLRDQNDDLNGQILSLSLYE 470
Cdd:COG4717  209 AELEEELEEAQEELEELEEELEQLENELEAAALEE 243
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
267-448 1.56e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136  267 QENMQLVHRVHELEEMVKDQETTAEQaLEEEARRHREVYCKLER-----------EKSTELELLNTRVQQLEEENTDLRT 335
Cdd:COG4913   231 VEHFDDLERAHEALEDAREQIELLEP-IRELAERYAAARERLAEleylraalrlwFAQRRLELLEAELEELRAELARLEA 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136  336 TVARLKSQTEKLDEERQRMSDRLEDTSL----RLKDEMDLYKRMMDKLRQNRLEFQK-------EREATQELIEDLRREL 404
Cdd:COG4913   310 ELERLEARLDALREELDELEAQIRGNGGdrleQLEREIERLERELEERERRRARLEAllaalglPLPASAEEFAALRAEA 389

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 568974136  405 EHLQmykldcERPGRGRSSSGLGEFNARAREVELEHEVKRLKQE 448
Cdd:COG4913   390 AALL------EALEEELEALEEALAEAEAALRDLRRELRELEAE 427
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 239-403 1.58e-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: 44.78  E-value: 1.58e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   239 EKVSfLEKKVTELENDSLTSGGLKSKLKQENMQLVHRVHELEEMVKDQETTAeQALEEEARRHREVYCKLE----REKST 314
Cdd:pfam01576  125 EKVT-TEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKA-KSLSKLKNKHEAMISDLEerlkKEEKG 202

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   315 ELELLNTRvQQLEEENTDLRTTVARLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQnrLEFQkereaTQ 394
Cdd:pfam01576  203 RQELEKAK-RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRE--LEAQ-----IS 274


                   ....*....
gi 568974136   395 ELIEDLRRE 403
Cdd:pfam01576  275 ELQEDLESE 283
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 227-408 2.06e-04

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: 43.60  E-value: 2.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 227 RDSIDSCDNDITEKVSFLEKKVTELENDSLTS----GGLKSKLKQENMQLVHRVHELEEMVKDQETTAEQALEE------ 296
Cdd:COG4942   50 EKALLKQLAALERRIAALARRIRALEQELAALeaelAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllspe 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 297 ---EARRHREVYCKLEREKSTELELLNTRVQQLEEENTDLRTTVARLKSQTEKLDEERQrmsdrledtslRLKDEMDLYK 373
Cdd:COG4942  130 dflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA-----------ALEALKAERQ 198

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 568974136 374 RMMDKLRQNRLEFQKEREATQELIEDLRRELEHLQ 408
Cdd:COG4942  199 KLLARLEKELAELAAELAELQQEAEELEALIARLE 233
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 292-408 3.68e-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: 3.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 292 QALEEEARRHREVYCKLERE---KSTELELLNTRVQQLEEENTDLRTTVARLKSQTEKLDEERQRMSDRLED-TSLR--- 364
Cdd:COG1579   13 QELDSELDRLEHRLKELPAElaeLEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvRNNKeye 92

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 568974136 365 -LKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRRELEHLQ 408
Cdd:COG1579   93 aLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELE 137
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
317-512 3.99e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.08  E-value: 3.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 317 ELLNTRVQQLEEENTDLRTtvARLKSQTEKLDEERQRMSDRLEDTSLRLKD------------EMDLYKRMMDKLRQNRL 384
Cdd:COG3206  152 AVANALAEAYLEQNLELRR--EEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvdlseEAKLLLQQLSELESQLA 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 385 EFQKEREATQELIEDLRRELehlqmyKLDCERPGRGRSSSGLGEFNARAREVELEHEVKRLK-QENH----KLRDQNDDL 459
Cdd:COG3206  230 EARAELAEAEARLAALRAQL------GSGPDALPELLQSPVIQQLRAQLAELEAELAELSARyTPNHpdviALRAQIAAL 303

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 568974136 460 NGQILSLSlyeAKNLFATQTKAQSLAAEIDT--ASRDELMEALKEQEEINFRLRQ 512
Cdd:COG3206  304 RAQLQQEA---QRILASLEAELEALQAREASlqAQLAQLEARLAELPELEAELRR 355
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 262-486 4.52e-04

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: 42.44  E-value: 4.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 262 KSKLKQENMQLVHRVHELEEMVKDQETTAEQALEEEArrhrevycKLEREKSTELELLNTRVQQLEEENTDLRTTVARLK 341
Cdd:COG4942   22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA--------ALERRIAALARRIRALEQELAALEAELAELEKEIA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 342 SQTEKLDEERQRMSDRL-----------------EDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRREL 404
Cdd:COG4942   94 ELRAELEAQKEELAELLralyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAER 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 405 EHLQMYKLDCERpgrgRSSSGLGEFNARAREV-ELEHEVKRLKQENHKLRDQNDDLNGQILSLSLYEAKNlfATQTKAQS 483
Cdd:COG4942  174 AELEALLAELEE----ERAALEALKAERQKLLaRLEKELAELAAELAELQQEAEELEALIARLEAEAAAA--AERTPAAG 247


                 ...
gi 568974136 484 LAA 486
Cdd:COG4942  248 FAA 250
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 264-405 6.62e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.42  E-value: 6.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136  264 KLKQENMQL-VHRVHELEEMVKDQETTAEQALEE-EARRHREVyckLEREKSTELELLNTRVQQLEEENTDLRttvarlK 341
Cdd:pfam17380 364 RIRQEEIAMeISRMRELERLQMERQQKNERVRQElEAARKVKI---LEEERQRKIQQQKVEMEQIRAEQEEAR------Q 434

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568974136  342 SQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRRELE 405
Cdd:pfam17380 435 REVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE 498
PTZ00121 PTZ00121
MAEBL; Provisional
 266-530 8.45e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 8.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136  266 KQENMQLVHRVHELEEMVKDQET-TAEQALEEEARRHREVYcKLEREKSTElELLNTRVQQLEEENTDLRTTVARlKSQT 344
Cdd:PTZ00121 1541 KAEEKKKADELKKAEELKKAEEKkKAEEAKKAEEDKNMALR-KAEEAKKAE-EARIEEVMKLYEEEKKMKAEEAK-KAEE 1617

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136  345 EKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLE--FQKEREATQE-----LIEDLRRELEHL-----QMYKL 412
Cdd:PTZ00121 1618 AKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEEnkIKAAEEAKKAeedkkKAEEAKKAEEDEkkaaeALKKE 1697

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136  413 DCERPGRGRSSSGLGEFNARAREVELEHEVKRLKQENHKLRDQNDDLNGQILSLSLYEAKNLFATQTKAQSLAAEIDTAS 492
Cdd:PTZ00121 1698 AEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEK 1777

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 568974136  493 RDELMEALKEQEEinfRLRQYMDKIILAILDHNPSILE 530
Cdd:PTZ00121 1778 EAVIEEELDEEDE---KRRMEVDKKIKDIFDNFANIIE 1812
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 238-408 8.59e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 8.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 238 TEKVSFLEKKVTELENDSLTSGGLKSKLKQENMQLVHRVHELEEMVKDQETTAEQALEEEARRHREvycklEREKSTELE 317
Cdd:COG1196  308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE-----LAEAEEELE 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 318 LLNTRVQQLEEENTDLRTTVARLKSQTEKLDEERQRMSD---RLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQ 394
Cdd:COG1196  383 ELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEeleELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALL 462

                        170
                 ....*....|....
gi 568974136 395 ELIEDLRRELEHLQ 408
Cdd:COG1196  463 ELLAELLEEAALLE 476
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 287-448 9.93e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 9.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 287 ETTAEQALEEEARRHREVYCKLEREKSTELELLNTRVQQLEEENTDLRTTVARLKSQTEKLDEERQRmsDRLEDTSLRLK 366
Cdd:COG1196  624 GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE--EELELEEALLA 701

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 367 DEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRRELEHLQMYKLDcerpgrgrSSSGLGEFNARAREVELEHEVKRLK 446
Cdd:COG1196  702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL--------EEEALEELPEPPDLEELERELERLE 773


                 ..
gi 568974136 447 QE 448
Cdd:COG1196  774 RE 775
PRK12704 PRK12704
phosphodiesterase; Provisional
 277-406 1.05e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 277 HELEEMVKDQETTAEQALEEEARRHREVYCKLEREKSTELELLNTRVQQLEEEntdLRTTVARLKSQTEKLDEERQRMSD 356
Cdd:PRK12704  38 EEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKR---LLQKEENLDRKLELLEKREEELEK 114

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 568974136 357 RLEDTSlRLKDEMDLYKRMMDKLRQNRLE-------FQKErEATQELIEDLRRELEH 406
Cdd:PRK12704 115 KEKELE-QKQQELEKKEEELEELIEEQLQelerisgLTAE-EAKEILLEKVEEEARH 169
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
237-453 1.12e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 237 ITEKVSFLEKKVTELENDSltsGGLKSKLKQENMQ---LVHRVHELEEMVKDQETTAEQALE-EEARRHREVYCKLEREK 312
Cdd:PRK03918 236 LKEEIEELEKELESLEGSK---RKLEEKIRELEERieeLKKEIEELEEKVKELKELKEKAEEyIKLSEFYEEYLDELREI 312

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 313 STELELLNTRVQQLEEENTDLRTTVARLKSQTEKLDEERQRMSD-----RLEDTSLRLKDEMDLYK------------RM 375
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEleerhELYEEAKAKKEELERLKkrltgltpekleKE 392

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 376 MDKLRQNRLEFQKE-REATQEL------IEDLRRELEHLQMYKLDCERPGRGRSSSGLGEFNARARE--VELEHEVKRLK 446
Cdd:PRK03918 393 LEELEKAKEEIEEEiSKITARIgelkkeIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAelKRIEKELKEIE 472


                 ....*..
gi 568974136 447 QENHKLR 453
Cdd:PRK03918 473 EKERKLR 479
PRK12705 PRK12705
hypothetical protein; Provisional
 255-416 1.14e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 41.62  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 255 SLTSGGLKSKLKQENMQLVHRVHELEEMVKDQETTAEQALEE------EARRHREVYCKLEREKS-TELELLNTRVQQLE 327
Cdd:PRK12705  15 GLLLGVLVVLLKKRQRLAKEAERILQEAQKEAEEKLEAALLEakelllRERNQQRQEARREREELqREEERLVQKEEQLD 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 328 EENTDLRTTVARLKSQTEKLDEERQRMSDRLEDTSLRLKdemdlykrmmdklrqnRLEFQKEREATQELIEDLRRELEH- 406
Cdd:PRK12705  95 ARAEKLDNLENQLEEREKALSARELELEELEKQLDNELY----------------RVAGLTPEQARKLLLKLLDAELEEe 158

                        170
                 ....*....|.
gi 568974136 407 -LQMYKLDCER 416
Cdd:PRK12705 159 kAQRVKKIEEE 169
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 251-508 1.43e-03

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: 41.21  E-value: 1.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 251 LENDSLTSGGLKSK--LKQENMQLVHRVHELEEMVKDQETTAEQALEEEARRHREVYCKLEREK---------------- 312
Cdd:COG5244  393 LEDNKDVTLILKILhpILETTVPKLLAFLRTNSNFNDNDTLCLIGSLYEIARIDKLIGKEEISKqdnrlflypscditls 472

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 313 -------STELELLNTRVQQLEEENTDLRTTVARLKSQTEKLDEErQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRL- 384
Cdd:COG5244  473 siltilfSDKLEVFFQGIESLLENITIFPEQPSQQTSDSENIKEN-SLLSDRLNEENIRLKEVLVQKENMLTEETKIKIi 551

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 385 -EFQKEREATQELIEDLRRELEHLQMyKLDCERPgrgrsssglgefnararevELEHEVKRLKQENHKLRDQNdDLNGQI 463
Cdd:COG5244  552 iGRDLERKTLEENIKTLKVELNNKNN-KLKEENF-------------------NLVNRLKNMELKLYQIKDNN-TLNKIY 610

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 568974136 464 LSL--SLYEAKNLFATQTKAQsLAAEIDTASRDELMEALKE--QEEINF 508
Cdd:COG5244  611 LDLvsEIMELRETIRRQIKEQ-KRVSIDFSWLDELKQPFKEhiIEMFNF 658
HOOK pfam05622
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ...
 223-455 1.85e-03

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


Pssm-ID: 461694 [Multi-domain]  Cd Length: 528  Bit Score: 40.83  E-value: 1.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136  223 EDLFRdsIDSCDNDITEKVSFLEKKVTELE--NDSLTSGGLKSK-LKQENMQLVH---RVHELEEMVkdqeTTAEQALEE 296
Cdd:pfam05622  73 EENFR--LETARDDYRIKCEELEKEVLELQhrNEELTSLAEEAQaLKDEMDILREssdKVKKLEATV----ETYKKKLED 146

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136  297 EARRHREVycKLEREKSTELeLLNTRvqQLEEEntdLRTTVArLKSQTEKLDEERQRMSDRLEDTSLR---LKDEMDLYK 373
Cdd:pfam05622 147 LGDLRRQV--KLLEERNAEY-MQRTL--QLEEE---LKKANA-LRGQLETYKRQVQELHGKLSEESKKadkLEFEYKKLE 217

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136  374 RMMDKLRQNRLEFQKEREATQELIEDLRreLEHLQMYKLDCERPGRGRSSSGLGEFNARAREVELEHEVKRLKQENHKLR 453
Cdd:pfam05622 218 EKLEALQKEKERLIIERDTLRETNEELR--CAQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLR 295


                  ..
gi 568974136  454 DQ 455
Cdd:pfam05622 296 LG 297
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 292-507 2.33e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   292 QALEEEARRHREvycKLEREKSTELE--------------LLNTRVQQLEEENTDLRTTVARLKSQTEKLDEERQRMSDR 357
Cdd:TIGR02169  190 DLIIDEKRQQLE---RLRREREKAERyqallkekreyegyELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKR 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   358 LEDTSLRLKdemDLYKRMMDKLRQNRLEFQKEREATQELIEDLRRELEhlqmyklDCERPGRgrsssglgefNARAREVE 437
Cdd:TIGR02169  267 LEEIEQLLE---ELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIA-------EKERELE----------DAEERLAK 326

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568974136   438 LEHEVKRLKQENHKLRDQNDDLNGQILSLSlYEAKNLFATQTKAQSLAAEIDT---ASRDELMEALKEQEEIN 507
Cdd:TIGR02169  327 LEAEIDKLLAEIEELEREIEEERKRRDKLT-EEYAELKEELEDLRAELEEVDKefaETRDELKDYREKLEKLK 398
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 278-408 2.92e-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: 40.05  E-value: 2.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 278 ELEEMVKDQETTAEQALEEEARRHREVYCKLEREKSTELEllnTRVQQLEeenTDLRTTVARLKSQTEKLDEERQRMSDR 357
Cdd:cd22656   95 EILELIDDLADATDDEELEEAKKTIKALLDDLLKEAKKYQ---DKAAKVV---DKLTDFENQTEKDQTALETLEKALKDL 168

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568974136 358 LEDTSLRL-KDEMDLYKRMMDKLRQN-RLEFQKEREATQELIEDLRRELEHLQ 408
Cdd:cd22656  169 LTDEGGAIaRKEIKDLQKELEKLNEEyAAKLKAKIDELKALIADDEAKLAAAL 221
PRK10929 PRK10929
putative mechanosensitive channel protein; Provisional
 253-396 3.46e-03

putative mechanosensitive channel protein; Provisional


Pssm-ID: 236798 [Multi-domain]  Cd Length: 1109  Bit Score: 40.42  E-value: 3.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136  253 NDSLTSGGLKSKLKQENMQLVHRVHELEEmvkDQETTAEQA--------LEEEARRhrevyckLEREKSTELELLNTRVQ 324
Cdd:PRK10929   99 PPNMSTDALEQEILQVSSQLLEKSRQAQQ---EQDRAREISdslsqlpqQQTEARR-------QLNEIERRLQTLGTPNT 168

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568974136  325 QLEE-ENTDLRTTVARLKSQTEKLDEERQRMSDRLEDTSLRLkdemDLYKRMMDKLR------QNRLEFQKEREATQEL 396
Cdd:PRK10929  169 PLAQaQLTALQAESAALKALVDELELAQLSANNRQELARLRS----ELAKKRSQQLDaylqalRNQLNSQRQREAERAL 243
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 236-446 5.62e-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: 5.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   236 DITEKVSFLEKKVTELENDSL-----TSGGLKSKLKQENMQLVHRVHELEemVKDQETTAEQALEEEARRHREV---YCK 307
Cdd:TIGR02169  769 ELEEDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRIEARLREIE--QKLNRLTLEKEYLEKEIQELQEqriDLK 846

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136   308 LER---------------EKSTELELLNTRVQQLEEENTDLRTTVARLKSQTEKLDEERQRMSDRLEDtslrlkdemdly 372
Cdd:TIGR02169  847 EQIksiekeienlngkkeELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEK------------ 914

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568974136   373 KRMMDKLRQNRLEFQKEREATqelIEDLRREL-----EHLQMYKLDCERPGRGRSSSGLGEFNARAREvELEHEVKRLK 446
Cdd:TIGR02169  915 KRKRLSELKAKLEALEEELSE---IEDPKGEDeeipeEELSLEDVQAELQRVEEEIRALEPVNMLAIQ-EYEEVLKRLD 989
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
291-517 6.58e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 6.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 291 EQALEEEARrhrevycKLEREKSTELELLNTRVQQLEEENTDLRTTVARLKSQTEKLDEERQRMsDRLEDTSLRLKDEMD 370
Cdd:COG4717   48 LERLEKEAD-------ELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEEL-EELEAELEELREELE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136 371 LYKRMmdklrQNRLEFQKEREATQELIEDLRRELEHLQmykldcerpgrgrsssglgefNARAREVELEHEVKRLKQENH 450
Cdd:COG4717  120 KLEKL-----LQLLPLYQELEALEAELAELPERLEELE---------------------ERLEELRELEEELEELEAELA 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568974136 451 KLRDQnddLNGQILSLSLYEAKNLFATQTKAQSLAAEIdtasrDELMEALKEQEEINFRLRQYMDKI 517
Cdd:COG4717  174 ELQEE---LEELLEQLSLATEEELQDLAEELEELQQRL-----AELEEELEEAQEELEELEEELEQL 232
mukB PRK04863
chromosome partition protein MukB;
271-405 7.36e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 39.17  E-value: 7.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136  271 QLVHRVHELEEMVKdQETTAEQALEEEARRHR------EVYCKLEREKSTELELLNTRVQQLEEENTDLRTTVARLKSQT 344
Cdd:PRK04863  517 QLRMRLSELEQRLR-QQQRAERLLAEFCKRLGknlddeDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARI 595

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568974136  345 EKLDEERQR---MSDRLEdtslRLKD---EMDLYKRMMDKLRQNRLEfqKEREATQE--LIEDLRRELE 405
Cdd:PRK04863  596 QRLAARAPAwlaAQDALA----RLREqsgEEFEDSQDVTEYMQQLLE--RERELTVErdELAARKQALD 658
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 310-512 9.61e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 39.01  E-value: 9.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136  310 REKSTELELLNTRVQQLEEENTDLRTTVARLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYkrmmdklrqNRLEFQKE 389
Cdd:PRK10246  415 LAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQL---------ADVKTICE 485

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568974136  390 REATQELIEDLRRELEHLQMYKL--DCERPGRgRSSSGLGEFNARAREVELEHEVKRLKQENHKLRDQNDDLNGQIL--- 464
Cdd:PRK10246  486 QEARIKDLEAQRAQLQAGQPCPLcgSTSHPAV-EAYQALEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQrde 564

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 568974136  465 --SLSLYEAKNLFATQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQ 512
Cdd:PRK10246  565 seAQSLRQEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLRL 614
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH