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Conserved domains on  [gi|1092878822|ref|NP_001333676|]
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rab11 family-interacting protein 4 isoform 3 [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

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List of domain hits

Name Accession Description Interval E-value
RBD-FIP pfam09457
FIP domain; The FIP domain is the Rab11-binding domain (RBD) at the C-terminus of a family of ...
429-469 1.98e-12

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: 61.20  E-value: 1.98e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1092878822 429 SRDELMEALKEQEEINFRLRQYMDKIILAILDHNPSILEIK 469
Cdd:pfam09457   1 SRDELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEVP 41
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
171-454 1.74e-09

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.46  E-value: 1.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  171 NDITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHRE----------- 239
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKElteleaeieel 766
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  240 --AYGKLEREKA---TEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDK 314
Cdd:TIGR02168  767 eeRLEEAEEELAeaeAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  315 LRQNRLE---FQKEREATQELIEDLRKELEHLQMYKLDCERpgRGRSASSGLGEFNARARevELEHEVKRLKQENYKLRD 391
Cdd:TIGR02168  847 IEELSEDiesLAAEIEELEELIEELESELEALLNERASLEE--ALALLRSELEELSEELR--ELESKRSELRRELEELRE 922
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092878822  392 QNDDLNGQILSLSLyEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQYMDKI 454
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 ...
429-469 1.98e-12

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: 61.20  E-value: 1.98e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1092878822 429 SRDELMEALKEQEEINFRLRQYMDKIILAILDHNPSILEIK 469
Cdd:pfam09457   1 SRDELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEVP 41
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
171-454 1.74e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.46  E-value: 1.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  171 NDITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHRE----------- 239
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKElteleaeieel 766
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  240 --AYGKLEREKA---TEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDK 314
Cdd:TIGR02168  767 eeRLEEAEEELAeaeAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  315 LRQNRLE---FQKEREATQELIEDLRKELEHLQMYKLDCERpgRGRSASSGLGEFNARARevELEHEVKRLKQENYKLRD 391
Cdd:TIGR02168  847 IEELSEDiesLAAEIEELEELIEELESELEALLNERASLEE--ALALLRSELEELSEELR--ELESKRSELRRELEELRE 922
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092878822  392 QNDDLNGQILSLSLyEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQYMDKI 454
Cdd:TIGR02168  923 KLAQLELRLEGLEV-RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
172-449 2.09e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 2.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 172 DITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMvKDQETTAEQALEEEARRHREAYGKLEREKAtE 251
Cdd:COG1196   226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL-RLELEELELELEEAQAEEYELLAELARLEQ-D 303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 252 VELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDtslrLKDEMDLYKRMMDKLRQNRLEFQKEREATQE 331
Cdd:COG1196   304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE----AEEELEEAEAELAEAEEALLEAEAELAEAEE 379
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 332 LIEDLRKELEHLQMykldcerpgrgrsassglGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLyEAKNL 411
Cdd:COG1196   380 ELEELAEELLEALR------------------AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE-EEEEE 440
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1092878822 412 FAAQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQ 449
Cdd:COG1196   441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
172-445 8.30e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.52  E-value: 8.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 172 DITEKVSFLEKKVTELENDSLTNGDLKSKLKqentQLVHRVHELEEMVKDQETTaeQALEEEARRHREAYGKLEREKAT- 250
Cdd:PRK03918  318 RLEEEINGIEERIKELEEKEERLEELKKKLK----ELEKRLEELEERHELYEEA--KAKKEELERLKKRLTGLTPEKLEk 391
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 251 EVELLNARVQQLEEENTELRTTVTRLKSQTEKLDE--ERQRMSDRLEDTSLRLKDEMDlYKRMMDKLRQNRLEFQKEREA 328
Cdd:PRK03918  392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKaiEELKKAKGKCPVCGRELTEEH-RKELLEEYTAELKRIEKELKE 470
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 329 TQELIEDLRKELEHLQMYKLDCERPGRGRSASSGLGEFNARAREVELEhEVKRLKQENYKLRDQNDDLNGQILSLsLYEA 408
Cdd:PRK03918  471 IEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE-ELEKKAEEYEKLKEKLIKLKGEIKSL-KKEL 548
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1092878822 409 KNLFAAQTKAQSLAAEIDTASRdELMEALKEQEEINF 445
Cdd:PRK03918  549 EKLEELKKKLAELEKKLDELEE-ELAELLKELEELGF 584
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
183-345 2.58e-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: 46.17  E-value: 2.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 183 KVTELENDSLtNGDLKSkLKQENTQLVHRVHELEEMVK-----DQETTAEQALEEEARRHREaygKLEREKATEVELLNA 257
Cdd:pfam04849  97 SVLTERNEAL-EEQLGS-AREEILQLRHELSKKDDLLQiysndAEESETESSCSTPLRRNES---FSSLHGCVQLDALQE 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 258 RVQQLEEENTELRTTVTRLKSQTEKL-DEERQRMSD---RLEDTSLRLKDEMD-LYKRMMDKLRQnrlefqkereatQEL 332
Cdd:pfam04849 172 KLRGLEEENLKLRSEASHLKTETDTYeEKEQQLMSDcveQLSEANQQMAELSEeLARKMEENLRQ------------QEE 239
                         170
                  ....*....|...
gi 1092878822 333 IEDLRKELEHLQM 345
Cdd:pfam04849 240 ITSLLAQIVDLQH 252
alph_xenorhab_A NF033928
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ...
245-445 3.35e-03

alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding member of a family of alpha-helical pore-forming binary toxins. YaxAB from Yersinia enterocolitica has been studied structurally. This HMM represents subunit A proteins such as XaxA and YaxA, capable of binding to the membrane even in the absence of the B subunit. This family is related to the Bacillus haemolytic enterotoxin family (see PF05791.9), although thresholds for this HMM are set to exclude that family.


Pssm-ID: 468250 [Multi-domain]  Cd Length: 340  Bit Score: 39.59  E-value: 3.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 245 EREKATEVELLNARVQQLEEENTElrtTVTRLKSQTEKLDEERQRMSDRLE-----------DTSLRLKDEMDLYKRMMD 313
Cdd:NF033928  100 KRGDLTEEELSELPPIPLSSDDKE---IVKELKEILEDLKNDIKDYQQKADdvkkelddfenDLREELLPQLKLKKKLYD 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 314 KLRQNrlefqKEREATQELIEDLRKELEHLQMYKLDCERPGRGRSASSGLGEF-----------NARAREVELEHEVKRL 382
Cdd:NF033928  177 DNLGS-----DSIEELREKIDQLEKEIEQLNKEYDDYVKLSFTGLAGGPIGLAitggifgskaeKIRKEKNALIQEIDEL 251
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092878822 383 KQenyKLRDQN------DDLNGQILSLSLYEAKNLFAAQTKA---QSLAAEIDtASRDELMEALKEQEEINF 445
Cdd:NF033928  252 QE---QLKKKNallgslERLQTSLDDILTRMEDALPALKKLKgvwQSLLTDID-SSINALKEIDDADSLRLF 319
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
228-344 4.65e-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: 38.89  E-value: 4.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 228 QALEEEARRHREAYGKLEREKATE-----VELLNARVQQLEEENTELRTTVTRLKSQTEK----LDEERQRMSDRLEDTS 298
Cdd:cd22656    94 AEILELIDDLADATDDEELEEAKKtikalLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKdqtaLETLEKALKDLLTDEG 173
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1092878822 299 LRL-KDEMDLYKRMMDKLRQN-RLEFQKEREATQELIEDLRKELEHLQ 344
Cdd:cd22656   174 GAIaRKEIKDLQKELEKLNEEyAAKLKAKIDELKALIADDEAKLAAAL 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 ...
429-469 1.98e-12

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: 61.20  E-value: 1.98e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1092878822 429 SRDELMEALKEQEEINFRLRQYMDKIILAILDHNPSILEIK 469
Cdd:pfam09457   1 SRDELQDALQKQEEENRRLEDYIDNILLRIMEHNPSILEVP 41
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
171-454 1.74e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.46  E-value: 1.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  171 NDITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHRE----------- 239
Cdd:TIGR02168  687 EELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKElteleaeieel 766
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  240 --AYGKLEREKA---TEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDK 314
Cdd:TIGR02168  767 eeRLEEAEEELAeaeAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  315 LRQNRLE---FQKEREATQELIEDLRKELEHLQMYKLDCERpgRGRSASSGLGEFNARARevELEHEVKRLKQENYKLRD 391
Cdd:TIGR02168  847 IEELSEDiesLAAEIEELEELIEELESELEALLNERASLEE--ALALLRSELEELSEELR--ELESKRSELRRELEELRE 922
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092878822  392 QNDDLNGQILSLSLyEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQYMDKI 454
Cdd:TIGR02168  923 KLAQLELRLEGLEV-RIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
172-449 2.09e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 53.40  E-value: 2.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 172 DITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMvKDQETTAEQALEEEARRHREAYGKLEREKAtE 251
Cdd:COG1196   226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEEL-RLELEELELELEEAQAEEYELLAELARLEQ-D 303
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 252 VELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDtslrLKDEMDLYKRMMDKLRQNRLEFQKEREATQE 331
Cdd:COG1196   304 IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEE----AEEELEEAEAELAEAEEALLEAEAELAEAEE 379
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 332 LIEDLRKELEHLQMykldcerpgrgrsassglGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLyEAKNL 411
Cdd:COG1196   380 ELEELAEELLEALR------------------AAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE-EEEEE 440
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1092878822 412 FAAQTKAQSLAAEIDTASRDELMEALKEQEEINFRLRQ 449
Cdd:COG1196   441 EEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAA 478
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
171-344 2.68e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.14  E-value: 2.68e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  171 NDITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQET--TAEQALEEEARRHREAYGKLEREK 248
Cdd:TIGR02168  298 SRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEelESLEAELEELEAELEELESRLEEL 377
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  249 ATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKD-EMDLYKRMMDKLRQNRLEFQKERE 327
Cdd:TIGR02168  378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELE 457
                          170
                   ....*....|....*..
gi 1092878822  328 ATQELIEDLRKELEHLQ 344
Cdd:TIGR02168  458 RLEEALEELREELEEAE 474
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
202-344 5.14e-07

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.08  E-value: 5.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 202 KQENTQLVHRVHELEEMVKD-----QETTAEQALEEEARRHREAYGKLEREKAtEVELLNARVQQLEEENTELRTTVTRL 276
Cdd:COG4717    87 EEEYAELQEELEELEEELEEleaelEELREELEKLEKLLQLLPLYQELEALEA-ELAELPERLEELEERLEELRELEEEL 165
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1092878822 277 KSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQ 344
Cdd:COG4717   166 EELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLE 233
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
215-349 1.03e-06

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 51.01  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 215 LEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRl 294
Cdd:COG2433   378 IEEALEELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSE- 456
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1092878822 295 EDTSLRLKDEMDLYKRMMDKLRqnrlefqKEREATQELIEDLRKELEHL-QMYKLD 349
Cdd:COG2433   457 ERREIRKDREISRLDREIERLE-------RELEEERERIEELKRKLERLkELWKLE 505
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
174-341 2.19e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.30  E-value: 2.19e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  174 TEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAE-QALEEEARRHREAYGKLEREKAT-- 250
Cdd:COG4913    609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvASAEREIAELEAELERLDASSDDla 688
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  251 ----EVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEM--DLYKR----MMDKLRQN-R 319
Cdd:COG4913    689 aleeQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELraLLEERfaaaLGDAVERElR 768
                          170       180
                   ....*....|....*....|..
gi 1092878822  320 LEFQKEREATQELIEDLRKELE 341
Cdd:COG4913    769 ENLEERIDALRARLNRAEEELE 790
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
196-443 2.59e-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: 50.07  E-value: 2.59e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  196 DLKSKLKQENTQLVHRVHELEEMVKDqettAEQALEEEARRHREAYGKLEREKAtEVELLNARVQQLEEENTELRTTVTR 275
Cdd:TIGR02169  688 RELSSLQSELRRIENRLDELSQELSD----ASRKIGEIEKEIEQLEQEEEKLKE-RLEELEEDLSSLEQEIENVKSELKE 762
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  276 LKSQTEKLDEERQRMSDRLEDTSLRLKDE-MDLYKRMMDKLRQNR-------LEFQKEREATQELIEDLRKELEHLQMYK 347
Cdd:TIGR02169  763 LEARIEELEEDLHKLEEALNDLEARLSHSrIPEIQAELSKLEEEVsriearlREIEQKLNRLTLEKEYLEKEIQELQEQR 842
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  348 LDCERpgrgRSASSGLGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSlyeaKNLFAAQTKAQSLAAEIDT 427
Cdd:TIGR02169  843 IDLKE----QIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELE----AQLRELERKIEELEAQIEK 914
                          250
                   ....*....|....*.
gi 1092878822  428 AsrDELMEALKEQEEI 443
Cdd:TIGR02169  915 K--RKRLSELKAKLEA 928
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
164-339 2.94e-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: 50.07  E-value: 2.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  164 DSIDSCDNDITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQ------ALEEEARRH 237
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDlesrlgDLKKERDEL 894
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  238 REAYGKLER----------EKATEVELLNARVQQLEEENTELRTTVTRLKSQT------EKLDEERQRMSDR---LEDTS 298
Cdd:TIGR02169  895 EAQLRELERkieeleaqieKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPeeelslEDVQAELQRVEEEiraLEPVN 974
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1092878822  299 LRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKE 339
Cdd:TIGR02169  975 MLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKK 1015
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
220-344 3.26e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 49.91  E-value: 3.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  220 KDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSL 299
Cdd:COG4913    308 EAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRA 387
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1092878822  300 RLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQ 344
Cdd:COG4913    388 EAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
175-448 3.27e-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: 49.67  E-value: 3.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  175 EKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKD-----QETTAEQA-LEEEARRHREAYGKLEREK 248
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEElqkelYALANEISrLEQQKQILRERLANLERQL 318
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  249 atevELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEdtslRLKDEMDLYKRMMDKLRQNRLEFQKEREA 328
Cdd:TIGR02168  319 ----EELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELE----ELEAELEELESRLEELEEQLETLRSKVAQ 390
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  329 TQELIEDLRKELEhlqmykldcerpgrgrsassglgefNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYE- 407
Cdd:TIGR02168  391 LELQIASLNNEIE-------------------------RLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEEl 445
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1092878822  408 -------AKNLFAAQTKAQSLAAEIDTASRdELMEALKEQEEINFRLR 448
Cdd:TIGR02168  446 eeeleelQEELERLEEALEELREELEEAEQ-ALDAAERELAQLQARLD 492
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
214-454 6.63e-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: 48.90  E-value: 6.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  214 ELEEMVKDQETTAEQalEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDR 293
Cdd:TIGR02168  233 RLEELREELEELQEE--LKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  294 ---LEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQMYKLDCER----------PGRGRSAS 360
Cdd:TIGR02168  311 lanLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESrleeleeqleTLRSKVAQ 390
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  361 SGLGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQ 440
Cdd:TIGR02168  391 LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
                          250
                   ....*....|....
gi 1092878822  441 EEINFRLRQYMDKI 454
Cdd:TIGR02168  471 EEAEQALDAAEREL 484
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
202-344 8.14e-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: 48.53  E-value: 8.14e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  202 KQENTQLVHRVHELEEMVKDQETTAEQaLEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTE 281
Cdd:TIGR02169  314 ERELEDAEERLAKLEAEIDKLLAEIEE-LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE 392
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1092878822  282 KLD------EERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQ 344
Cdd:TIGR02169  393 KLEklkreiNELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
172-445 8.30e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.52  E-value: 8.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 172 DITEKVSFLEKKVTELENDSLTNGDLKSKLKqentQLVHRVHELEEMVKDQETTaeQALEEEARRHREAYGKLEREKAT- 250
Cdd:PRK03918  318 RLEEEINGIEERIKELEEKEERLEELKKKLK----ELEKRLEELEERHELYEEA--KAKKEELERLKKRLTGLTPEKLEk 391
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 251 EVELLNARVQQLEEENTELRTTVTRLKSQTEKLDE--ERQRMSDRLEDTSLRLKDEMDlYKRMMDKLRQNRLEFQKEREA 328
Cdd:PRK03918  392 ELEELEKAKEEIEEEISKITARIGELKKEIKELKKaiEELKKAKGKCPVCGRELTEEH-RKELLEEYTAELKRIEKELKE 470
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 329 TQELIEDLRKELEHLQMYKLDCERPGRGRSASSGLGEFNARAREVELEhEVKRLKQENYKLRDQNDDLNGQILSLsLYEA 408
Cdd:PRK03918  471 IEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLE-ELEKKAEEYEKLKEKLIKLKGEIKSL-KKEL 548
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1092878822 409 KNLFAAQTKAQSLAAEIDTASRdELMEALKEQEEINF 445
Cdd:PRK03918  549 EKLEELKKKLAELEKKLDELEE-ELAELLKELEELGF 584
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
200-449 1.92e-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: 47.37  E-value: 1.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  200 KLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKAT---EVELLNARVQQLEEENTELRTTVTRL 276
Cdd:TIGR02169  255 KLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASlerSIAEKERELEDAEERLAKLEAEIDKL 334
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  277 KSQTEKLDEERQRMSDRLEdtslRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQmykldcERPGRG 356
Cdd:TIGR02169  335 LAEIEELEREIEEERKRRD----KLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLK------REINEL 404
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  357 RSASSGLGEFNARARE--VELEHEVKRLKQENYKLRDQNDDLngqilslslyeAKNLFAAQTKAQSLAAEIDTAsRDELM 434
Cdd:TIGR02169  405 KRELDRLQEELQRLSEelADLNAAIAGIEAKINELEEEKEDK-----------ALEIKKQEWKLEQLAADLSKY-EQELY 472
                          250
                   ....*....|....*
gi 1092878822  435 EALKEQEEINFRLRQ 449
Cdd:TIGR02169  473 DLKEEYDRVEKELSK 487
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
163-344 2.48e-05

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: 46.30  E-value: 2.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 163 RDSIDSCDNDITEKVSFLEKKVTELENDSLTN----GDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEE------ 232
Cdd:COG4942    50 EKALLKQLAALERRIAALARRIRALEQELAALeaelAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllspe 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 233 ---EARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQrmsdrledtslRLKDEMDLYK 309
Cdd:COG4942   130 dflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA-----------ALEALKAERQ 198
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1092878822 310 RMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQ 344
Cdd:COG4942   199 KLLARLEKELAELAAELAELQQEAEELEALIARLE 233
HAP1_N pfam04849
HAP1 N-terminal conserved region; This family represents an N-terminal conserved region found ...
183-345 2.58e-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: 46.17  E-value: 2.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 183 KVTELENDSLtNGDLKSkLKQENTQLVHRVHELEEMVK-----DQETTAEQALEEEARRHREaygKLEREKATEVELLNA 257
Cdd:pfam04849  97 SVLTERNEAL-EEQLGS-AREEILQLRHELSKKDDLLQiysndAEESETESSCSTPLRRNES---FSSLHGCVQLDALQE 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 258 RVQQLEEENTELRTTVTRLKSQTEKL-DEERQRMSD---RLEDTSLRLKDEMD-LYKRMMDKLRQnrlefqkereatQEL 332
Cdd:pfam04849 172 KLRGLEEENLKLRSEASHLKTETDTYeEKEQQLMSDcveQLSEANQQMAELSEeLARKMEENLRQ------------QEE 239
                         170
                  ....*....|...
gi 1092878822 333 IEDLRKELEHLQM 345
Cdd:pfam04849 240 ITSLLAQIVDLQH 252
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
226-442 3.54e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 3.54e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 226 AEQAL------EEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTS- 298
Cdd:COG1196   209 AEKAEryrelkEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQa 288
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 299 ---------LRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQmykldcerpgrgrsASSGLGEFNAR 369
Cdd:COG1196   289 eeyellaelARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELE--------------EELEEAEEELE 354
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1092878822 370 AREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQEE 442
Cdd:COG1196   355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELE 427
PTZ00121 PTZ00121
MAEBL; Provisional
198-467 1.65e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  198 KSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLK 277
Cdd:PTZ00121  1543 EEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKA 1622
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  278 SQTEKLDEERQRMSDRLEDTSLRLKDEMDLyKRMMDKLRQNRLEFQKEREATQELIEDLRKELEH----LQMYKLDCERP 353
Cdd:PTZ00121  1623 EELKKAEEEKKKVEQLKKKEAEEKKKAEEL-KKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDekkaAEALKKEAEEA 1701
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  354 GRGRSASSGLGEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKNLFAAQTKAQSLAAEIDTASRDEL 433
Cdd:PTZ00121  1702 KKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVI 1781
                          250       260       270
                   ....*....|....*....|....*....|....
gi 1092878822  434 MEALKEQEEinfRLRQYMDKIILAILDHNPSILE 467
Cdd:PTZ00121  1782 EEELDEEDE---KRRMEVDKKIKDIFDNFANIIE 1812
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
228-444 1.83e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.14  E-value: 1.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  228 QALEEEARRHREAYGKLEREKATEVELLNA--RVQQLEEENTELRTTVTRLksqtEKLDEERQRM---SDRLEdtslRLK 302
Cdd:COG4913    620 AELEEELAEAEERLEALEAELDALQERREAlqRLAEYSWDEIDVASAEREI----AELEAELERLdasSDDLA----ALE 691
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  303 DEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLQMYKLDCERPGRGRSASsglgEFNARAREVELEHEVKRL 382
Cdd:COG4913    692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRA----LLEERFAAALGDAVEREL 767
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092878822  383 KQEnykLRDQNDDLNGQILSLS--LYEAKNLFAAQTKAQSLAAEIDTASRDELMEALKEQEEIN 444
Cdd:COG4913    768 REN---LEERIDALRARLNRAEeeLERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDG 828
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
198-392 2.47e-04

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.57  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 198 KSKLKQENTQ--LVHRVHELEEMVKDQETTAE---QALEEEARRHREAYGKLEREKATEVEllnaRVQQLEEENTELRTT 272
Cdd:pfam17380 403 KVKILEEERQrkIQQQKVEMEQIRAEQEEARQrevRRLEEERAREMERVRLEEQERQQQVE----RLRQQEEERKRKKLE 478
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 273 VTRLKSQTEKLDEERQRMsdrledtslrLKDEMDLYKRMMDKLRQNRLEFQKEREATQELI--EDLRKELEHLQMYKLDC 350
Cdd:pfam17380 479 LEKEKRDRKRAEEQRRKI----------LEKELEERKQAMIEEERKRKLLEKEMEERQKAIyeEERRREAEEERRKQQEM 548
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1092878822 351 ERPGRGRSASSGLGEFNARAREVELEHEVKRLKQENYKLRDQ 392
Cdd:pfam17380 549 EERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAE 590
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
211-385 3.40e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 3.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  211 RVHELEEMVKDQETTAEQALEEEARRHREAYGKLEReKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRM 290
Cdd:COG4913    250 QIELLEPIRELAERYAAARERLAELEYLRAALRLWF-AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDEL 328
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  291 SDRLEDTSLRLKDEMdlyKRMMDKLRQNRLEFQKEREATQELIEDL-------RKELEHLQmyKLDCERPGRGRSASSGL 363
Cdd:COG4913    329 EAQIRGNGGDRLEQL---EREIERLERELEERERRRARLEALLAALglplpasAEEFAALR--AEAAALLEALEEELEAL 403
                          170       180
                   ....*....|....*....|....
gi 1092878822  364 GE--FNARAREVELEHEVKRLKQE 385
Cdd:COG4913    404 EEalAEAEAALRDLRRELRELEAE 427
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
232-448 3.44e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 3.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 232 EEARRHREAYGKLEREKATEVELLNARVQQLEEEN-----TELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRL----- 301
Cdd:PRK02224  169 ERASDARLGVERVLSDQRGSLDQLKAQIEEKEEKDlherlNGLESELAELDEEIERYEEQREQARETRDEADEVLeehee 248
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 302 -KDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHLqmykldcERPGRGRSASSGLGEFNARA---REVELEH 377
Cdd:PRK02224  249 rREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEEL-------EEERDDLLAEAGLDDADAEAveaRREELED 321
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092878822 378 EVKRLKQENYKLRDQNDDLNGQILSLsLYEAKNLFAAQTKAQSLAAEIDT---ASRDELMEALKEQEEINFRLR 448
Cdd:PRK02224  322 RDEELRDRLEECRVAAQAHNEEAESL-REDADDLEERAEELREEAAELESeleEAREAVEDRREEIEELEEEIE 394
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
175-344 3.93e-04

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


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 43.24  E-value: 3.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  175 EKVSfLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQ-----------ALEEEARRHREAYGK 243
Cdd:pfam01576  125 EKVT-TEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSlsklknkheamISDLEERLKKEEKGR 203
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  244 LEREKATevellnarvQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLR------- 316
Cdd:pfam01576  204 QELEKAK---------RKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIReleaqis 274
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1092878822  317 --QNRLEFQK-EREATQELIEDLRKELEHLQ 344
Cdd:pfam01576  275 elQEDLESERaARNKAEKQRRDLGEELEALK 305
PRK12705 PRK12705
hypothetical protein; Provisional
201-352 4.78e-04

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 42.39  E-value: 4.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 201 LKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQT 280
Cdd:PRK12705   39 LQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQLEEREKALSARE 118
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1092878822 281 EKLDEERQRMSDRLEdtslrlkdemdlykrmmdklrqnRLEFQKEREATQELIEDLRKELEH--LQMYKLDCER 352
Cdd:PRK12705  119 LELEELEKQLDNELY-----------------------RVAGLTPEQARKLLLKLLDAELEEekAQRVKKIEEE 169
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
227-407 5.31e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 5.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 227 EQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSD-------------- 292
Cdd:COG4717    48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEElreeleklekllql 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 293 -----RLEDTSLRLKDEMDLYKRMMDKLRQnRLEFQKEREATQELIEDLRKELEHLQMyKLDCERPGRGRSASSGLGEfn 367
Cdd:COG4717   128 lplyqELEALEAELAELPERLEELEERLEE-LRELEEELEELEAELAELQEELEELLE-QLSLATEEELQDLAEELEE-- 203
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1092878822 368 ARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYE 407
Cdd:COG4717   204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEE 243
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
196-423 5.41e-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: 42.06  E-value: 5.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 196 DLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEArrhreaygKLEREKATEVELLNARVQQLEEENTELRTTVTR 275
Cdd:COG4942    20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA--------ALERRIAALARRIRALEQELAALEAELAELEKE 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 276 LKSQTEKLDEERQRMSDRL-----------------EDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRK 338
Cdd:COG4942    92 IAELRAELEAQKEELAELLralyrlgrqpplalllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 339 ELEHLQMYKLDCERpgRGRSASSGLGEfnARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKNlfAAQTKA 418
Cdd:COG4942   172 ERAELEALLAELEE--ERAALEALKAE--RQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA--AERTPA 245

                  ....*
gi 1092878822 419 QSLAA 423
Cdd:COG4942   246 AGFAA 250
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
202-341 5.42e-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: 5.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 202 KQENTQLVHRVHELEEMVKDQETTAEQALEE-EARRHreaYGKLEREKATEVELLNARVQQLEEENTELRttvtrlKSQT 280
Cdd:pfam17380 367 QEEIAMEISRMRELERLQMERQQKNERVRQElEAARK---VKILEEERQRKIQQQKVEMEQIRAEQEEAR------QREV 437
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092878822 281 EKLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELE 341
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE 498
PRK12704 PRK12704
phosphodiesterase; Provisional
178-342 8.96e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.69  E-value: 8.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 178 SFLEKKVTELENDSltngdlKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNA 257
Cdd:PRK12704   27 KIAEAKIKEAEEEA------KRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDR 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 258 RVQQLEEENTELRTTVTRLKSQTEKLDEERQRmsdrledtslrlkdemdlYKRMMDKLRQnRLE----FQKErEATQELI 333
Cdd:PRK12704  101 KLELLEKREEELEKKEKELEQKQQELEKKEEE------------------LEELIEEQLQ-ELErisgLTAE-EAKEILL 160

                  ....*....
gi 1092878822 334 EDLRKELEH 342
Cdd:PRK12704  161 EKVEEEARH 169
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
186-345 1.32e-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: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 186 ELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKA------------TEVE 253
Cdd:COG5244   394 EDNKDVTLILKILHPILETTVPKLLAFLRTNSNFNDNDTLCLIGSLYEIARIDKLIGKEEISKQdnrlflypscdiTLSS 473
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 254 LLNARVQ-------QLEEENTELRTTVTRLKSQTEKLDE---ERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRL--E 321
Cdd:COG5244   474 ILTILFSdklevffQGIESLLENITIFPEQPSQQTSDSEnikENSLLSDRLNEENIRLKEVLVQKENMLTEETKIKIiiG 553
                         170       180
                  ....*....|....*....|....
gi 1092878822 322 FQKEREATQELIEDLRKELEHLQM 345
Cdd:COG5244   554 RDLERKTLEENIKTLKVELNNKNN 577
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
172-301 1.75e-03

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: 39.91  E-value: 1.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 172 DITEKVSFLEKKVTELENDSltnGDLKSKLKQENTQL--VHRVHELEEMVKDQETTAE--QALEEEARRHREAYGKLERE 247
Cdd:COG1579    49 AAKTELEDLEKEIKRLELEI---EEVEARIKKYEEQLgnVRNNKEYEALQKEIESLKRriSDLEDEILELMERIEELEEE 125
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1092878822 248 KATEVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLEDTSLRL 301
Cdd:COG1579   126 LAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPELLAL 179
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
180-293 2.61e-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: 2.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  180 LEKKVTELENDSLTN-GDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQaLEEEARRHREAYGKLEREKATEVELLNAR 258
Cdd:COG4913    321 LREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRARLEALLAA-LGLPLPASAEEFAALRAEAAALLEALEEE 399
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1092878822  259 VQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDR 293
Cdd:COG4913    400 LEALEEALAEAEAALRDLRRELRELEAEIASLERR 434
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
212-385 2.91e-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: 40.11  E-value: 2.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 212 VHELEEMVKDQETTAEQALEEEARRHREAYGKLERE-KATEVEllnaRVQQLEEENTELRTTVTR---LKSQTEKLDEER 287
Cdd:pfam17380 271 LNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEeKAREVE----RRRKLEEAEKARQAEMDRqaaIYAEQERMAMER 346
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 288 QRMSDRLedtslRLKDEmdlyKRMMDKLRQNRL--EFQKERE------ATQELIEDLRKELEHLQMYKLDCERPGRGRSA 359
Cdd:pfam17380 347 ERELERI-----RQEER----KRELERIRQEEIamEISRMRElerlqmERQQKNERVRQELEAARKVKILEEERQRKIQQ 417
                         170       180
                  ....*....|....*....|....*.
gi 1092878822 360 SSGLGEFNARAREVELEHEVKRLKQE 385
Cdd:pfam17380 418 QKVEMEQIRAEQEEARQREVRRLEEE 443
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
180-339 2.99e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.00  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 180 LEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEqALEEEARRHREAYGKLERE---KATEVELLN 256
Cdd:TIGR04523 424 LEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLK-VLSRSINKIKQNLEQKQKElksKEKELKKLN 502
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 257 ARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMSDRLED------------TSLRLKDEMDLYKRMMDKLRQNRLEFQK 324
Cdd:TIGR04523 503 EEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDledelnkddfelKKENLEKEIDEKNKEIEELKQTQKSLKK 582
                         170
                  ....*....|....*
gi 1092878822 325 EREATQELIEDLRKE 339
Cdd:TIGR04523 583 KQEEKQELIDQKEKE 597
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
120-456 3.11e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 40.34  E-value: 3.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  120 LEARLKNLKANSPNRKISSTAFGRQLMHSSNFSSSNGSTEDLFRDSIDSCDNDITEKVSFLEKKVTELENDSLTNGDLKS 199
Cdd:pfam02463  688 ELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKS 767
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  200 KLKQENTQL-VHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLEREKATEVELLNARVQQLEEENTELRTTVTRLKS 278
Cdd:pfam02463  768 ELSLKEKELaEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQK 847
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  279 QTEKLDEERQRmsDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQELIEDLRKELEhlqmykldcerpgrgrs 358
Cdd:pfam02463  848 LEKLAEEELER--LEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQK----------------- 908
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822  359 assglgEFNARAREVELEHEVKRLKQENYKLRDQNDDLNGQILSLSLYEAKNLFAAQTKAQSLAAEIDTASRDELMEALK 438
Cdd:pfam02463  909 ------LNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEE 982
                          330
                   ....*....|....*...
gi 1092878822  439 EQEEINFRLRQYMDKIIL 456
Cdd:pfam02463  983 FEEKEERYNKDELEKERL 1000
alph_xenorhab_A NF033928
alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding ...
245-445 3.35e-03

alpha-xenorhabdolysin family binary toxin subunit A; Alpha-xenorhabdolysin was the founding member of a family of alpha-helical pore-forming binary toxins. YaxAB from Yersinia enterocolitica has been studied structurally. This HMM represents subunit A proteins such as XaxA and YaxA, capable of binding to the membrane even in the absence of the B subunit. This family is related to the Bacillus haemolytic enterotoxin family (see PF05791.9), although thresholds for this HMM are set to exclude that family.


Pssm-ID: 468250 [Multi-domain]  Cd Length: 340  Bit Score: 39.59  E-value: 3.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 245 EREKATEVELLNARVQQLEEENTElrtTVTRLKSQTEKLDEERQRMSDRLE-----------DTSLRLKDEMDLYKRMMD 313
Cdd:NF033928  100 KRGDLTEEELSELPPIPLSSDDKE---IVKELKEILEDLKNDIKDYQQKADdvkkelddfenDLREELLPQLKLKKKLYD 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 314 KLRQNrlefqKEREATQELIEDLRKELEHLQMYKLDCERPGRGRSASSGLGEF-----------NARAREVELEHEVKRL 382
Cdd:NF033928  177 DNLGS-----DSIEELREKIDQLEKEIEQLNKEYDDYVKLSFTGLAGGPIGLAitggifgskaeKIRKEKNALIQEIDEL 251
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1092878822 383 KQenyKLRDQN------DDLNGQILSLSLYEAKNLFAAQTKA---QSLAAEIDtASRDELMEALKEQEEINF 445
Cdd:NF033928  252 QE---QLKKKNallgslERLQTSLDDILTRMEDALPALKKLKgvwQSLLTDID-SSINALKEIDDADSLRLF 319
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
173-343 3.97e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 3.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 173 ITEKVSFLEKKVTELENDSLTNGDLKSKLKQENTQLVHRVHELEEMVKDQETTAEQA-----LEEEARRHREAYGKLERE 247
Cdd:PRK03918  236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAeeyikLSEFYEEYLDELREIEKR 315
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 248 KAT-------------EVELLNARVQQLEEENTELRTTVTRLKSQTEKLDEERQRMsDRLEDTSLRLKD-EMDLYKRMMD 313
Cdd:PRK03918  316 LSRleeeingieerikELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKK-EELERLKKRLTGlTPEKLEKELE 394
                         170       180       190
                  ....*....|....*....|....*....|
gi 1092878822 314 KLRQNRLEFQKEREATQELIEDLRKELEHL 343
Cdd:PRK03918  395 ELEKAKEEIEEEISKITARIGELKKEIKEL 424
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
228-344 4.65e-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: 38.89  E-value: 4.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 228 QALEEEARRHREAYGKLEREKATE-----VELLNARVQQLEEENTELRTTVTRLKSQTEK----LDEERQRMSDRLEDTS 298
Cdd:cd22656    94 AEILELIDDLADATDDEELEEAKKtikalLDDLLKEAKKYQDKAAKVVDKLTDFENQTEKdqtaLETLEKALKDLLTDEG 173
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1092878822 299 LRL-KDEMDLYKRMMDKLRQN-RLEFQKEREATQELIEDLRKELEHLQ 344
Cdd:cd22656   174 GAIaRKEIKDLQKELEKLNEEyAAKLKAKIDELKALIADDEAKLAAAL 221
PRK10361 PRK10361
DNA recombination protein RmuC; Provisional
203-457 5.34e-03

DNA recombination protein RmuC; Provisional


Pssm-ID: 182409 [Multi-domain]  Cd Length: 475  Bit Score: 39.20  E-value: 5.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 203 QENTQLVHRVHELEEMVKDQETTAEQALEEEARRhreaygklerekaTEVELLNARVQQLEEENT----ELRTTVTRLKS 278
Cdd:PRK10361   26 QHAQQKAEQLAEREEMVAELSAAKQQITQSEHWR-------------AECELLNNEVRSLQSINTsleaDLREVTTRMEA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 279 -QTEKLDEERQRMSdrledTSLRLKDEMD-LYKRMMDKlrQNRLEFQKEREATQELIEDLRKELEhlqmykldcerpGRG 356
Cdd:PRK10361   93 aQQHADDKIRQMIN-----SEQRLSEQFEnLANRIFEH--SNRRVDEQNRQSLNSLLSPLREQLD------------GFR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 357 RSASSGLGEfNARAREVeLEHEVKRLKQENYKLRDQNDDLN-------------GQILSLSLYEAKNLFAAQTKAQSLAA 423
Cdd:PRK10361  154 RQVQDSFGK-EAQERHT-LAHEIRNLQQLNAQMAQEAINLTralkgdnktqgnwGEVVLTRVLEASGLREGYEYETQVSI 231
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1092878822 424 EIDTASRdelmealkEQEEINFRLRQYMDKIILA 457
Cdd:PRK10361  232 ENDARSR--------MQPDVIVRLPQGKDVVIDA 257
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
170-343 6.31e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 6.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 170 DNDITEKVSFLEKKVTELENDSltngdlkSKLKQENTQLVHRVHELEEMVKDQETTAE--QALEEEARRHREAYGKLERE 247
Cdd:PRK02224  201 EKDLHERLNGLESELAELDEEI-------ERYEEQREQARETRDEADEVLEEHEERREelETLEAEIEDLRETIAETERE 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 248 KAT---EVELLNARVQQLEEENTELRTTV-------TRLKSQTEKLDEERQRMSDRLEDTSL----------RLKDEMDL 307
Cdd:PRK02224  274 REElaeEVRDLRERLEELEEERDDLLAEAglddadaEAVEARREELEDRDEELRDRLEECRVaaqahneeaeSLREDADD 353
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1092878822 308 YKRMMDKLRQNRLEFQKEREATQELIEDLRKELEHL 343
Cdd:PRK02224  354 LEERAEELREEAAELESELEEAREAVEDRREEIEEL 389
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
207-339 7.08e-03

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


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 38.96  E-value: 7.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1092878822 207 QLVHRVHELEEMVKDQETTAEQALEEEARRHREAYGKLerekATEVELLNARVQQLEEENTELRTTVTRLK-----SQTE 281
Cdd:pfam07111 506 QEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASV----GQQLEVARQGQQESTEEAASLRQELTQQQeiygqALQE 581
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1092878822 282 KLDEERQRMSDRLEDTSLRLKDEMDLYKRMMDKLRQNRLEFQKEREATQE---LIEDLRKE 339
Cdd:pfam07111 582 KVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQElrrLQDEARKE 642
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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