NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1092878841|ref|NP_001333678|]
View 

rab11 family-interacting protein 4 isoform 5 [Homo sapiens]

Protein Classification

ClyA-like and RBD-FIP domain-containing protein( domain architecture ID 10559615)

ClyA-like and RBD-FIP domain-containing protein

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 ...
 336-376 3.48e-11

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: 57.73  E-value: 3.48e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1092878841 336 SRDELMEALKEQEEINFRLRQYMDKIILAILDHNPSILEIK 376
Cdd:pfam09457   1 SRDELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEVP 41
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 78-361 4.90e-08

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.06  E-value: 4.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841   78 NDITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKAT 157
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  158 ----------------EVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDK 221
Cdd:TIGR02168  767 eerleeaeeelaeaeaEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  222 LRQNRLE---FQKEREATQELIEDLRKELEHLQMYKLDCERpgRGRSASSGLGEFNARARevELEHEVKRLKQENYKLRD 298
Cdd:TIGR02168  847 IEELSEDiesLAAEIEELEELIEELESELEALLNERASLEE--ALALLRSELEELSEELR--ELESKRSELRRELEELRE 922

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092878841  299 QNDDLNGQILSLSLyEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQYMDKI 361
Cdd:TIGR02168  923 KLAQLELRLEGLEV-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 ...
 336-376 3.48e-11

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: 57.73  E-value: 3.48e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1092878841 336 SRDELMEALKEQEEINFRLRQYMDKIILAILDHNPSILEIK 376
Cdd:pfam09457   1 SRDELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEVP 41
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 78-361 4.90e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.06  E-value: 4.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841   78 NDITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKAT 157
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  158 ----------------EVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDK 221
Cdd:TIGR02168  767 eerleeaeeelaeaeaEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  222 LRQNRLE---FQKEREATQELIEDLRKELEHLQMYKLDCERpgRGRSASSGLGEFNARARevELEHEVKRLKQENYKLRD 298
Cdd:TIGR02168  847 IEELSEDiesLAAEIEELEELIEELESELEALLNERASLEE--ALALLRSELEELSEELR--ELESKRSELRRELEELRE 922

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092878841  299 QNDDLNGQILSLSLyEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQYMDKI 361
Cdd:TIGR02168  923 KLAQLELRLEGLEV-RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 79-364 2.47e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 2.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  79 DITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMvKDQETTAEQALEEEARRHREAYGKLEREKAtE 158
Cdd:COG1196   226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL-RLELEELELELEEAQAEEYELLAELARLEQ-D 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841 159 VELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDtslrLKDEMDLYKRMMDKLRQNRLEFQKEREATQE 238
Cdd:COG1196   304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE----AEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841 239 LIEDLRKELEHLQMYKLDCERpgrgRSASSGLGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKNL 318
Cdd:COG1196   380 ELEELAEELLEALRAAAELAA----QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1092878841 319 FAAQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQYMDKIILA 364
Cdd:COG1196   456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 90-252 3.56e-04

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: 41.93  E-value: 3.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  90 KVTELENDSLtNGDLKSkLKQENTQLVHRVHELEEMVK-----DQETTAEQALEEEARRHREaygKLEREKATEVELLNA 164
Cdd:pfam04849  97 SVLTERNEAL-EEQLGS-AREEILQLRHELSKKDDLLQiysndAEESETESSCSTPLRRNES---FSSLHGCVQLDALQE 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841 165 RVQQLEEENTELRTTVTRLKSQTEKL-DEERQRMSD---RLEDTSLRLKDEMD-LYKRMMDKLRQnrlefqkereatQEL 239
Cdd:pfam04849 172 KLRGLEEENLKLRSEASHLKTETDTYeEKEQQLMSDcveQLSEANQQMAELSEeLARKMEENLRQ------------QEE 239

                         170
                  ....*....|...
gi 1092878841 240 IEDLRKELEHLQM 252
Cdd:pfam04849 240 ITSLLAQIVDLQH 252
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
79-352 6.19e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 6.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  79 DITEKVSFLEKKVTELENDSLTNGDLKSKLKqentQLVHRVHELEEMVKDQETTaeQALEEEARRHREAYGKLEREKAT- 157
Cdd:PRK03918  318 RLEEEINGIEERIKELEEKEERLEELKKKLK----ELEKRLEELEERHELYEEA--KAKKEELERLKKRLTGLTPEKLEk 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841 158 EVELLNARVQQLEEENTELRTTVTRLKSQTEKLDE--ERQRMSDRLEDTSLRLKDEMDlYKRMMDKLRQNRLEFQKEREA 235
Cdd:PRK03918  392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKaiEELKKAKGKCPVCGRELTEEH-RKELLEEYTAELKRIEKELKE 470

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841 236 TQELIEDLRKELEHLQMYKLDCERPGRGRSASSGLGEFNARAREVELEhEVKRLKQENYKLRDQNDDLNGQILSLsLYEA 315
Cdd:PRK03918  471 IEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE-ELEKKAEEYEKLKEKLIKLKGEIKSL-KKEL 548

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1092878841 316 KNLFAAQTKAQSLAAEIDTASRdELMEALKEQEEINF 352
Cdd:PRK03918  549 EKLEELKKKLAELEKKLDELEE-ELAELLKELEELGF 584
 
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 ...
 336-376 3.48e-11

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: 57.73  E-value: 3.48e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1092878841 336 SRDELMEALKEQEEINFRLRQYMDKIILAILDHNPSILEIK 376
Cdd:pfam09457   1 SRDELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEVP 41
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 78-361 4.90e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 55.06  E-value: 4.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841   78 NDITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKAT 157
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  158 ----------------EVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDK 221
Cdd:TIGR02168  767 eerleeaeeelaeaeaEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  222 LRQNRLE---FQKEREATQELIEDLRKELEHLQMYKLDCERpgRGRSASSGLGEFNARARevELEHEVKRLKQENYKLRD 298
Cdd:TIGR02168  847 IEELSEDiesLAAEIEELEELIEELESELEALLNERASLEE--ALALLRSELEELSEELR--ELESKRSELRRELEELRE 922

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092878841  299 QNDDLNGQILSLSLyEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQYMDKI 361
Cdd:TIGR02168  923 KLAQLELRLEGLEV-RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 78-251 2.03e-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: 2.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841   78 NDITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQET--TAEQALEEEARRHREAYGKLEREK 155
Cdd:TIGR02168  298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEelESLEAELEELEAELEELESRLEEL 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  156 ATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKD-EMDLYKRMMDKLRQNRLEFQKERE 234
Cdd:TIGR02168  378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELE 457

                          170
                   ....*....|....*..
gi 1092878841  235 ATQELIEDLRKELEHLQ 251
Cdd:TIGR02168  458 RLEEALEELREELEEAE 474
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 79-364 2.47e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 2.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  79 DITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMvKDQETTAEQALEEEARRHREAYGKLEREKAtE 158
Cdd:COG1196   226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL-RLELEELELELEEAQAEEYELLAELARLEQ-D 303

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841 159 VELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDtslrLKDEMDLYKRMMDKLRQNRLEFQKEREATQE 238
Cdd:COG1196   304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE----AEEELEEAEAELAEAEEALLEAEAELAEAEE 379

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841 239 LIEDLRKELEHLQMYKLDCERpgrgRSASSGLGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKNL 318
Cdd:COG1196   380 ELEELAEELLEALRAAAELAA----QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE 455

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1092878841 319 FAAQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQYMDKIILA 364
Cdd:COG1196   456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA 501
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
122-256 2.76e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 49.09  E-value: 2.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841 122 LEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRl 201
Cdd:COG2433   378 IEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSE- 456

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1092878841 202 EDTSLRLKDEMDLYKRMMDKLRqnrlefqKEREATQELIEDLRKELEHL-QMYKLD 256
Cdd:COG2433   457 ERREIRKDREISRLDREIERLE-------RELEEERERIEELKRKLERLkELWKLE 505
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
127-251 1.03e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  127 KDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSL 206
Cdd:COG4913    308 EAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1092878841  207 RLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQ 251
Cdd:COG4913    388 EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
109-251 1.51e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 47.07  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841 109 KQENTQLVHRVHELEEMVKD-----QETTAEQALEEEARRHREAYGKLEREKAtEVELLNARVQQLEEENTELRTTVTRL 183
Cdd:COG4717    87 EEEYAELQEELEELEEELEEleaelEELREELEKLEKLLQLLPLYQELEALEA-ELAELPERLEELEERLEELRELEEEL 165

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092878841 184 KSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQ 251
Cdd:COG4717   166 EELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
81-248 1.56e-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: 1.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841   81 TEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAE-QALEEEARRHREAYGKLEREKAT-- 157
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvASAEREIAELEAELERLDASSDDla 688

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  158 ----EVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLY------KRMMDKLRQN-R 226
Cdd:COG4913    689 aleeQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALleerfaAALGDAVERElR 768

                          170       180
                   ....*....|....*....|..
gi 1092878841  227 LEFQKEREATQELIEDLRKELE 248
Cdd:COG4913    769 ENLEERIDALRARLNRAEEELE 790
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 71-246 3.63e-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: 45.83  E-value: 3.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841   71 DSIDSCDNDITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQ------ALEEEARRH 144
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDlesrlgDLKKERDEL 894

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  145 REAYGKLER----------EKATEVELLNARVQQLEEENTELRTTVTRLKSQT------EKLDEERQRMSDR---LEDTS 205
Cdd:TIGR02169  895 EAQLRELERkieeleaqieKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPeeelslEDVQAELQRVEEEiraLEPVN 974

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1092878841  206 LRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKE 246
Cdd:TIGR02169  975 MLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 109-251 5.09e-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: 45.44  E-value: 5.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  109 KQENTQLVHRVHELEEMVKDQETTAEQaLEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTE 188
Cdd:TIGR02169  314 ERELEDAEERLAKLEAEIDKLLAEIEE-LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092878841  189 KLD------EERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQ 251
Cdd:TIGR02169  393 KLEklkreiNELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 103-350 5.60e-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: 45.44  E-value: 5.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  103 DLKSKLKQENTQLVHRVHELEEMVKDqettAEQALEEEARRHREAYGKLEREKAtEVELLNARVQQLEEENTELRTTVTR 182
Cdd:TIGR02169  688 RELSSLQSELRRIENRLDELSQELSD----ASRKIGEIEKEIEQLEQEEEKLKE-RLEELEEDLSSLEQEIENVKSELKE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  183 LKSQTEKLDEERQRMSDRLEDTSLRLKDE-MDLYKRMMDKLRQNR-------LEFQKEREATQELIEDLRKELEHLQMYK 254
Cdd:TIGR02169  763 LEARIEELEEDLHKLEEALNDLEARLSHSrIPEIQAELSKLEEEVsriearlREIEQKLNRLTLEKEYLEKEIQELQEQR 842

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  255 LDCERpgrgRSASSGLGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSlyeaKNLFAAQTKAQSLAAEIDT 334
Cdd:TIGR02169  843 IDLKE----QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE----AQLRELERKIEELEAQIEK 914

                          250
                   ....*....|....*.
gi 1092878841  335 AsrDELMEALKEQEEI 350
Cdd:TIGR02169  915 K--RKRLSELKAKLEA 928
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 121-361 6.55e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.05  E-value: 6.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  121 ELEEMVKDQETTAEQalEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDR 200
Cdd:TIGR02168  233 RLEELREELEELQEE--LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  201 ---LEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQMYKLDCER----------PGRGRSAS 267
Cdd:TIGR02168  311 lanLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESrleeleeqleTLRSKVAQ 390

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  268 SGLGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQ 347
Cdd:TIGR02168  391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470

                          250
                   ....*....|....
gi 1092878841  348 EEINFRLRQYMDKI 361
Cdd:TIGR02168  471 EEAEQALDAAEREL 484
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 82-355 1.08e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.28  E-value: 1.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841   82 EKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKD-----QETTAEQA-LEEEARRHREAYGKLEREK 155
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkelYALANEISrLEQQKQILRERLANLERQL 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  156 atevELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEdtslRLKDEMDLYKRMMDKLRQNRLEFQKEREA 235
Cdd:TIGR02168  319 ----EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE----ELEAELEELESRLEELEEQLETLRSKVAQ 390

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  236 TQELIEDLRKELEhlqmykldcerpgrgrsassglgefNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYE- 314
Cdd:TIGR02168  391 LELQIASLNNEIE-------------------------RLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEl 445

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1092878841  315 -------AKNLFAAQTKAQSLAAEIDTASRdELMEALKEQEEINFRLR 355
Cdd:TIGR02168  446 eeeleelQEELERLEEALEELREELEEAEQ-ALDAAERELAQLQARLD 492
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 70-251 1.81e-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: 43.21  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  70 RDSIDSCDNDITEKVSFLEKKVTELENDSLTN----GDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEE------ 139
Cdd:COG4942    50 EKALLKQLAALERRIAALARRIRALEQELAALeaelAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllspe 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841 140 ---EARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQrmsdrledtslRLKDEMDLYK 216
Cdd:COG4942   130 dflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA-----------ALEALKAERQ 198

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1092878841 217 RMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQ 251
Cdd:COG4942   199 KLLARLEKELAELAAELAELQQEAEELEALIARLE 233
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 107-356 2.99e-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: 2.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  107 KLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKAT---EVELLNARVQQLEEENTELRTTVTRL 183
Cdd:TIGR02169  255 KLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASlerSIAEKERELEDAEERLAKLEAEIDKL 334

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  184 KSQTEKLDEERQRMSDRLEdtslRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQmykldcERPGRG 263
Cdd:TIGR02169  335 LAEIEELEREIEEERKRRD----KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK------REINEL 404

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  264 RSASSGLGEFNARARE--VELEHEVKRLKQENYKLRDQNDDLngqilslslyeAKNLFAAQTKAQSLAAEIDTAsRDELM 341
Cdd:TIGR02169  405 KRELDRLQEELQRLSEelADLNAAIAGIEAKINELEEEKEDK-----------ALEIKKQEWKLEQLAADLSKY-EQELY 472

                          250
                   ....*....|....*
gi 1092878841  342 EALKEQEEINFRLRQ 356
Cdd:TIGR02169  473 DLKEEYDRVEKELSK 487
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 133-349 3.21e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 3.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841 133 AEQAL------EEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTS- 205
Cdd:COG1196   209 AEKAEryrelkEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQa 288

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841 206 ---------LRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQmykldcerpgrgrsASSGLGEFNAR 276
Cdd:COG1196   289 eeyellaelARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE--------------EELEEAEEELE 354

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092878841 277 AREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQEE 349
Cdd:COG1196   355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
 90-252 3.56e-04

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: 41.93  E-value: 3.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  90 KVTELENDSLtNGDLKSkLKQENTQLVHRVHELEEMVK-----DQETTAEQALEEEARRHREaygKLEREKATEVELLNA 164
Cdd:pfam04849  97 SVLTERNEAL-EEQLGS-AREEILQLRHELSKKDDLLQiysndAEESETESSCSTPLRRNES---FSSLHGCVQLDALQE 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841 165 RVQQLEEENTELRTTVTRLKSQTEKL-DEERQRMSD---RLEDTSLRLKDEMD-LYKRMMDKLRQnrlefqkereatQEL 239
Cdd:pfam04849 172 KLRGLEEENLKLRSEASHLKTETDTYeEKEQQLMSDcveQLSEANQQMAELSEeLARKMEENLRQ------------QEE 239

                         170
                  ....*....|...
gi 1092878841 240 IEDLRKELEHLQM 252
Cdd:pfam04849 240 ITSLLAQIVDLQH 252
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
79-352 6.19e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 6.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  79 DITEKVSFLEKKVTELENDSLTNGDLKSKLKqentQLVHRVHELEEMVKDQETTaeQALEEEARRHREAYGKLEREKAT- 157
Cdd:PRK03918  318 RLEEEINGIEERIKELEEKEERLEELKKKLK----ELEKRLEELEERHELYEEA--KAKKEELERLKKRLTGLTPEKLEk 391

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841 158 EVELLNARVQQLEEENTELRTTVTRLKSQTEKLDE--ERQRMSDRLEDTSLRLKDEMDlYKRMMDKLRQNRLEFQKEREA 235
Cdd:PRK03918  392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKaiEELKKAKGKCPVCGRELTEEH-RKELLEEYTAELKRIEKELKE 470

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841 236 TQELIEDLRKELEHLQMYKLDCERPGRGRSASSGLGEFNARAREVELEhEVKRLKQENYKLRDQNDDLNGQILSLsLYEA 315
Cdd:PRK03918  471 IEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE-ELEKKAEEYEKLKEKLIKLKGEIKSL-KKEL 548

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1092878841 316 KNLFAAQTKAQSLAAEIDTASRdELMEALKEQEEINF 352
Cdd:PRK03918  549 EKLEELKKKLAELEKKLDELEE-ELAELLKELEELGF 584
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 105-299 6.38e-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: 41.65  E-value: 6.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841 105 KSKLKQENTQ--LVHRVHELEEMVKDQETTAE---QALEEEARRHREAYGKLEREKATEVEllnaRVQQLEEENTELRTT 179
Cdd:pfam17380 403 KVKILEEERQrkIQQQKVEMEQIRAEQEEARQrevRRLEEERAREMERVRLEEQERQQQVE----RLRQQEEERKRKKLE 478

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841 180 VTRLKSQTEKLDEERQRMsdrledtslrLKDEMDLYKRMMDKLRQNRLEFQKEREATQELI--EDLRKELEHLQMYKLDC 257
Cdd:pfam17380 479 LEKEKRDRKRAEEQRRKI----------LEKELEERKQAMIEEERKRKLLEKEMEERQKAIyeEERRREAEEERRKQQEM 548

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1092878841 258 ERPGRGRSASSGLGEFNARAREVELEHEVKRLKQENYKLRDQ 299
Cdd:pfam17380 549 EERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
PTZ00121 PTZ00121
MAEBL; Provisional
 105-374 9.49e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 9.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  105 KSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLK 184
Cdd:PTZ00121  1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  185 SQTEKLDEERQRMSDRLEDTSLRLKDEMDLyKRMMDKLRQNRLEFQKEREATQELIEDLRKELEH----LQMYKLDCERP 260
Cdd:PTZ00121  1623 EELKKAEEEKKKVEQLKKKEAEEKKKAEEL-KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDekkaAEALKKEAEEA 1701

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  261 GRGRSASSGLGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKNLFAAQTKAQSLAAEIDTASRDEL 340
Cdd:PTZ00121  1702 KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1092878841  341 MEALKEQEEinfRLRQYMDKIILAILDHNPSILE 374
Cdd:PTZ00121  1782 EEELDEEDE---KRRMEVDKKIKDIFDNFANIIE 1812
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 109-248 1.22e-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: 40.88  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841 109 KQENTQLVHRVHELEEMVKDQETTAEQALEE-EARRHreaYGKLEREKATEVELLNARVQQLEEENTELRttvtrlKSQT 187
Cdd:pfam17380 367 QEEIAMEISRMRELERLQMERQQKNERVRQElEAARK---VKILEEERQRKIQQQKVEMEQIRAEQEEAR------QREV 437

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092878841 188 EKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELE 248
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE 498
PRK12705 PRK12705
hypothetical protein; Provisional
 108-249 1.84e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 40.08  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841 108 LKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQT 187
Cdd:PRK12705   39 LQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARE 118

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092878841 188 EKLDEERQRMSDRLEdtslrlkdemdlykrmmdklrqnRLEFQKEREATQELIEDLRKELEH 249
Cdd:PRK12705  119 LELEELEKQLDNELY-----------------------RVAGLTPEQARKLLLKLLDAELEE 157
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
135-351 1.85e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 1.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  135 QALEEEARRHREAYGKLEREKATEVELLNA--RVQQLEEENTELRTTVTRLksqtEKLDEERQRM---SDRLEdtslRLK 209
Cdd:COG4913    620 AELEEELAEAEERLEALEAELDALQERREAlqRLAEYSWDEIDVASAEREI----AELEAELERLdasSDDLA----ALE 691

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  210 DEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQMYKLDCERPGRGRSASsglgEFNARAREVELEHEVKRL 289
Cdd:COG4913    692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA----LLEERFAAALGDAVEREL 767

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092878841  290 KQEnykLRDQNDDLNGQILSLS--LYEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQEEIN 351
Cdd:COG4913    768 REN---LEERIDALRARLNRAEeeLERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDG 828
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
118-292 2.33e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 2.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  118 RVHELEEMVKDQETTAEQALEEEARRHREAYGKLEReKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRM 197
Cdd:COG4913    250 QIELLEPIRELAERYAAARERLAELEYLRAALRLWF-AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL 328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  198 SDRLEDTSLRLKDEMdlyKRMMDKLRQNRLEFQKEREATQELIEDL-------RKELEHLQmyKLDCERPGRGRSASSGL 270
Cdd:COG4913    329 EAQIRGNGGDRLEQL---EREIERLERELEERERRRARLEALLAALglplpasAEEFAALR--AEAAALLEALEEELEAL 403

                          170       180
                   ....*....|....*....|....
gi 1092878841  271 GE--FNARAREVELEHEVKRLKQE 292
Cdd:COG4913    404 EEalAEAEAALRDLRRELRELEAE 427
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
139-355 2.80e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.64  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841 139 EEARRHREAYGKLEREKATEVELLNARVQQLEEEN-----TELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRL----- 208
Cdd:PRK02224  169 ERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDlherlNGLESELAELDEEIERYEEQREQARETRDEADEVLeehee 248

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841 209 -KDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLqmykldcERPGRGRSASSGLGEFNARA---REVELEH 284
Cdd:PRK02224  249 rREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEEL-------EEERDDLLAEAGLDDADAEAveaRREELED 321

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092878841 285 EVKRLKQENYKLRDQNDDLNGQILSLsLYEAKNLFAAQTKAQSLAAEIDT---ASRDELMEALKEQEEINFRLR 355
Cdd:PRK02224  322 RDEELRDRLEECRVAAQAHNEEAESL-REDADDLEERAEELREEAAELESeleEAREAVEDRREEIEELEEEIE 394
PRK12704 PRK12704
phosphodiesterase; Provisional
 85-249 3.55e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.38  E-value: 3.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841  85 SFLEKKVTELENDSltngdlKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNA 164
Cdd:PRK12704   27 KIAEAKIKEAEEEA------KRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDR 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841 165 RVQQLEEENTELRTTVTRLKSQTEKLDEERQRmsdrledtslrlkdemdlYKRMMDKLRQnRLE----FQKErEATQELI 240
Cdd:PRK12704  101 KLELLEKREEELEKKEKELEQKQQELEKKEEE------------------LEELIEEQLQ-ELErisgLTAE-EAKEILL 160


                  ....*....
gi 1092878841 241 EDLRKELEH 249
Cdd:PRK12704  161 EKVEEEARH 169
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 103-330 5.29e-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: 38.59  E-value: 5.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841 103 DLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEArrhreaygKLEREKATEVELLNARVQQLEEENTELRTTVTR 182
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA--------ALERRIAALARRIRALEQELAALEAELAELEKE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841 183 LKSQTEKLDEERQRMSDRL-----------------EDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRK 245
Cdd:COG4942    92 IAELRAELEAQKEELAELLralyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841 246 ELEHLQMYKLDCERpgRGRSASSGLGEfnARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKNlfAAQTKA 325
Cdd:COG4942   172 ERAELEALLAELEE--ERAALEALKAE--RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA--AERTPA 245


                  ....*
gi 1092878841 326 QSLAA 330
Cdd:COG4942   246 AGFAA 250
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
87-200 8.19e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.36  E-value: 8.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841   87 LEKKVTELENDSLTN-GDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQaLEEEARRHREAYGKLEREKATEVELLNAR 165
Cdd:COG4913    321 LREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAA-LGLPLPASAEEFAALRAEAAALLEALEEE 399

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1092878841  166 VQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDR 200
Cdd:COG4913    400 LEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 82-224 9.49e-03

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 38.23  E-value: 9.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841   82 EKVSfLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQ-----------ALEEEARRHREAYGK 150
Cdd:pfam01576  125 EKVT-TEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSlsklknkheamISDLEERLKKEEKGR 203

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092878841  151 LEREKATevellnarvQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQ 224
Cdd:pfam01576  204 QELEKAK---------RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRE 268
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 119-292 9.51e-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: 38.18  E-value: 9.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841 119 VHELEEMVKDQETTAEQALEEEARRHREAYGKLERE-KATEVEllnaRVQQLEEENTELRTTVTR---LKSQTEKLDEER 194
Cdd:pfam17380 271 LNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEeKAREVE----RRRKLEEAEKARQAEMDRqaaIYAEQERMAMER 346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878841 195 QRMSDRLedtslRLKDEmdlyKRMMDKLRQNRL--EFQKERE------ATQELIEDLRKELEHLQMYKLDCERPGRGRSA 266
Cdd:pfam17380 347 ERELERI-----RQEER----KRELERIRQEEIamEISRMRElerlqmERQQKNERVRQELEAARKVKILEEERQRKIQQ 417

                         170       180
                  ....*....|....*....|....*.
gi 1092878841 267 SSGLGEFNARAREVELEHEVKRLKQE 292
Cdd:pfam17380 418 QKVEMEQIRAEQEEARQREVRRLEEE 443
 
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