NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|25151737|ref|NP_498828|]
View 

Spindle assembly abnormal protein 4 [Caenorhabditis elegans]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Mplasa_alph_rch super family cl37461
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 315-505 8.31e-07

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


The actual alignment was detected with superfamily member TIGR04523:

Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 52.72  E-value: 8.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737   315 DRQKLEIEIRRHRNLNIQLRDTIAHLDyaeesvhTTKRQLEEKISEVNNFKKEL---IEEFKKCKKGVEEEFEKKFEKIK 391
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLT-------NQDSVKELIIKNLDNTRESLetqLKVLSRSINKIKQNLEQKQKELK 492

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737   392 EDYDELyEKLKRDQRDLERDQKILKKgtgeRNKEFTETIATLRDKLRASETKNAQYRQDIRVRDEKLKK---------KD 462
Cdd:TIGR04523 493 SKEKEL-KKLNEEKKELEEKVKDLTK----KISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKenlekeideKN 567

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 25151737   463 EEIEKLQKDGNRLKSTLQTLEKRVKQLrtEKERDDKEKEMFAK 505
Cdd:TIGR04523 568 KEIEELKQTQKSLKKKQEEKQELIDQK--EKEKKDLIKEIEEK 608
HSD3 super family cl21103
Spermatogenesis-associated protein 7, or HSD3; Spermatogenesis-associated protein HSD3 also ...
 454-558 9.80e-03

Spermatogenesis-associated protein 7, or HSD3; Spermatogenesis-associated protein HSD3 also goes by the name of spermatogenesis-associated protein 7 or SPAT7. The family carries a single transmembrane domain. It functions in several tissues, and is expressed in the developing and mature mouse retina; it is expressed in multiple retinal layers in the adult mouse retina. Mutations lead to LCA disease, or Leber congenital amaurosis, which results in a number of retinal dystrophies. The disease- phenotype is characterized by severe visual loss at birth, nystagmus, a variety of fundus changes, and minimal or absent recordable responses on the electroretinogram (ERG).


The actual alignment was detected with superfamily member pfam15244:

Pssm-ID: 464584  Cd Length: 414  Bit Score: 39.01  E-value: 9.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737   454 RDEKLKKKDEEIEK---LQKDG------NRLKSTLQTLEKRVKQLRTEKERDDKEKEMFAKVAmnrKTSNPVPPVLNQSV 524
Cdd:pfam15244  77 RREKLKKELARCEKelkSAKTAsqanskNNSKSLSNTLQKPSGEPQDEDDVLIEEMNEFPSFS---KSRVPSSERLHLSL 153

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 25151737   525 PIS--ITSNGPSRHpSSSSLTTFRKPSTSNRERGVS 558
Cdd:pfam15244 154 PKSsrSLTNGTEKN-SSSSLSSMDSTSSRRRKSGSS 188
 
Name Accession Description Interval E-value
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 315-505 8.31e-07

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 52.72  E-value: 8.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737   315 DRQKLEIEIRRHRNLNIQLRDTIAHLDyaeesvhTTKRQLEEKISEVNNFKKEL---IEEFKKCKKGVEEEFEKKFEKIK 391
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLT-------NQDSVKELIIKNLDNTRESLetqLKVLSRSINKIKQNLEQKQKELK 492

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737   392 EDYDELyEKLKRDQRDLERDQKILKKgtgeRNKEFTETIATLRDKLRASETKNAQYRQDIRVRDEKLKK---------KD 462
Cdd:TIGR04523 493 SKEKEL-KKLNEEKKELEEKVKDLTK----KISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKenlekeideKN 567

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 25151737   463 EEIEKLQKDGNRLKSTLQTLEKRVKQLrtEKERDDKEKEMFAK 505
Cdd:TIGR04523 568 KEIEELKQTQKSLKKKQEEKQELIDQK--EKEKKDLIKEIEEK 608
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
322-511 2.97e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.83  E-value: 2.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737  322 EIRRHRNLNIQ-LRDTIAHLDYAEESVHTTKRQLEEKISEVNNFKKELI---EEFKKCKKGVEeefekkfekikeDYDEL 397
Cdd:PRK03918 169 EVIKEIKRRIErLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPelrEELEKLEKEVK------------ELEEL 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737  398 YEK---LKRDQRDLERDQKILK---KGTGERNKEFTETIATLRDKLRASET---KNAQYR-------------QDIRVRD 455
Cdd:PRK03918 237 KEEieeLEKELESLEGSKRKLEekiRELEERIEELKKEIEELEEKVKELKElkeKAEEYIklsefyeeyldelREIEKRL 316

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 25151737  456 EKLKKKDEEIEKLQKDGNRLKSTLQTLEKRVKQLRTEKERDDKEKEMF--AKVAMNRK 511
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYeeAKAKKEEL 374
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
317-501 4.53e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 4.53e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 317 QKLEIEIRRHRNLNIQLRDTIAHLDYAEESVHTTKRQLEEKISEVNNFKK-----ELIEEFKKCKKgveeefekkfekIK 391
Cdd:COG4717  74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllqllPLYQELEALEA------------EL 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 392 EDYDELYEKLKRDQRDLERDQkilkkgtgERNKEFTETIATLRDKL-RASETKNAQYRQDIRVRDEKLKKKDEEIEKLQK 470
Cdd:COG4717 142 AELPERLEELEERLEELRELE--------EELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEELQQRLAELEE 213

                       170       180       190
                ....*....|....*....|....*....|.
gi 25151737 471 DGNRLKSTLQTLEKRVKQLRTEKERDDKEKE 501
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAALEER 244
BBP1_C pfam15272
Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole ...
 393-499 9.63e-04

Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole body component, carries coiled-coils that are necessary for the localization of BBP1 to the spindle pole body (SPB). Although not a membrane protein itself, BBP1 binds to Mps2 as well as to Spc29 and the half-bridge protein Kar1, thus providing a model for how the SPB core is tethered within the nuclear envelope and to the half-bridge


Pssm-ID: 405864 [Multi-domain]  Cd Length: 183  Bit Score: 40.84  E-value: 9.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737   393 DYDELYEKLKRDQRDLErdqkILKKGTGERNKEFTETIATLRDKLRasETKN---AQYRQDIRVRDE--KLKKKDEEIEK 467
Cdd:pfam15272   5 EYLELLDKLDKNNRALH----LLNKDVRERDEHYQLQETSYKKKYL--QTRNeliNELKQSKKLYDNyyKLYSKYQQLKK 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 25151737   468 LQKDGNRLKSTLQTLEKRVKQLRTEKERDDKE 499
Cdd:pfam15272  79 ISNESLDLQSTITNLESQLVDQAIDKDREIHN 110
TOPEUc smart00435
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ...
 423-508 5.43e-03

DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras


Pssm-ID: 214661 [Multi-domain]  Cd Length: 391  Bit Score: 40.03  E-value: 5.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737    423 NKEFTETIATLRDKLRASETKNAQYRQDI----RVRDEK--LKKKDE-EIEKLQKDGNRLKSTLQTLEKRVKQL-----R 490
Cdd:smart00435 272 SKTHEKSMEKLQEKIKALKYQLKRLKKMIllfeMISDLKrkLKSKFErDNEKLDAEVKEKKKEKKKEEKKKKQIerleeR 351

                           90
                   ....*....|....*....
gi 25151737    491 TEK-ERDDKEKEMFAKVAM 508
Cdd:smart00435 352 IEKlEVQATDKEENKTVAL 370
HSD3 pfam15244
Spermatogenesis-associated protein 7, or HSD3; Spermatogenesis-associated protein HSD3 also ...
 454-558 9.80e-03

Spermatogenesis-associated protein 7, or HSD3; Spermatogenesis-associated protein HSD3 also goes by the name of spermatogenesis-associated protein 7 or SPAT7. The family carries a single transmembrane domain. It functions in several tissues, and is expressed in the developing and mature mouse retina; it is expressed in multiple retinal layers in the adult mouse retina. Mutations lead to LCA disease, or Leber congenital amaurosis, which results in a number of retinal dystrophies. The disease- phenotype is characterized by severe visual loss at birth, nystagmus, a variety of fundus changes, and minimal or absent recordable responses on the electroretinogram (ERG).


Pssm-ID: 464584  Cd Length: 414  Bit Score: 39.01  E-value: 9.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737   454 RDEKLKKKDEEIEK---LQKDG------NRLKSTLQTLEKRVKQLRTEKERDDKEKEMFAKVAmnrKTSNPVPPVLNQSV 524
Cdd:pfam15244  77 RREKLKKELARCEKelkSAKTAsqanskNNSKSLSNTLQKPSGEPQDEDDVLIEEMNEFPSFS---KSRVPSSERLHLSL 153

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 25151737   525 PIS--ITSNGPSRHpSSSSLTTFRKPSTSNRERGVS 558
Cdd:pfam15244 154 PKSsrSLTNGTEKN-SSSSLSSMDSTSSRRRKSGSS 188
 
Name Accession Description Interval E-value
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 315-505 8.31e-07

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 52.72  E-value: 8.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737   315 DRQKLEIEIRRHRNLNIQLRDTIAHLDyaeesvhTTKRQLEEKISEVNNFKKEL---IEEFKKCKKGVEEEFEKKFEKIK 391
Cdd:TIGR04523 420 EKELLEKEIERLKETIIKNNSEIKDLT-------NQDSVKELIIKNLDNTRESLetqLKVLSRSINKIKQNLEQKQKELK 492

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737   392 EDYDELyEKLKRDQRDLERDQKILKKgtgeRNKEFTETIATLRDKLRASETKNAQYRQDIRVRDEKLKK---------KD 462
Cdd:TIGR04523 493 SKEKEL-KKLNEEKKELEEKVKDLTK----KISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKenlekeideKN 567

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 25151737   463 EEIEKLQKDGNRLKSTLQTLEKRVKQLrtEKERDDKEKEMFAK 505
Cdd:TIGR04523 568 KEIEELKQTQKSLKKKQEEKQELIDQK--EKEKKDLIKEIEEK 608
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 318-500 9.47e-07

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: 52.76  E-value: 9.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737    318 KLEIEIRRHRN----LNIQLRDTIAHLDYAEESVHTTKRQ---LEEKISEVNNFKKELIEEFKKCKK---------GVEE 381
Cdd:TIGR02169  298 ELEAEIASLERsiaeKERELEDAEERLAKLEAEIDKLLAEieeLEREIEEERKRRDKLTEEYAELKEeledlraelEEVD 377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737    382 EFEKKFEKIKEDYDELYEKLKRDQRDLERDQKILkkgtGERNKEFTETIATLRDKLRASETKNAQYRQDIRVRDEKLKKK 461
Cdd:TIGR02169  378 KEFAETRDELKDYREKLEKLKREINELKRELDRL----QEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ 453

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 25151737    462 DEEIEKLQKDGN-------RLKSTLQTLEKRVKQLRTEKERDDKEK 500
Cdd:TIGR02169  454 EWKLEQLAADLSkyeqelyDLKEEYDRVEKELSKLQRELAEAEAQA 499
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 345-495 1.01e-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: 52.76  E-value: 1.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737    345 ESVHTTKRQLEEKISEVNNFKKELIEEFKKckkgveeefekkfekikedYDELYEKLKRDQRDLERD---QKILKKGTGE 421
Cdd:TIGR02169  297 GELEAEIASLERSIAEKERELEDAEERLAK-------------------LEAEIDKLLAEIEELEREieeERKRRDKLTE 357

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25151737    422 RNKEFTETIATLRDKLRASETKNAQYRQDIRVRDEKLKKKDEEIEKLQKDGNRLKSTLQTLEKRVKQLRTEKER 495
Cdd:TIGR02169  358 EYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAG 431
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
322-511 2.97e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 50.83  E-value: 2.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737  322 EIRRHRNLNIQ-LRDTIAHLDYAEESVHTTKRQLEEKISEVNNFKKELI---EEFKKCKKGVEeefekkfekikeDYDEL 397
Cdd:PRK03918 169 EVIKEIKRRIErLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPelrEELEKLEKEVK------------ELEEL 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737  398 YEK---LKRDQRDLERDQKILK---KGTGERNKEFTETIATLRDKLRASET---KNAQYR-------------QDIRVRD 455
Cdd:PRK03918 237 KEEieeLEKELESLEGSKRKLEekiRELEERIEELKKEIEELEEKVKELKElkeKAEEYIklsefyeeyldelREIEKRL 316

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 25151737  456 EKLKKKDEEIEKLQKDGNRLKSTLQTLEKRVKQLRTEKERDDKEKEMF--AKVAMNRK 511
Cdd:PRK03918 317 SRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYeeAKAKKEEL 374
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
317-501 4.53e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 50.15  E-value: 4.53e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 317 QKLEIEIRRHRNLNIQLRDTIAHLDYAEESVHTTKRQLEEKISEVNNFKK-----ELIEEFKKCKKgveeefekkfekIK 391
Cdd:COG4717  74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllqllPLYQELEALEA------------EL 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 392 EDYDELYEKLKRDQRDLERDQkilkkgtgERNKEFTETIATLRDKL-RASETKNAQYRQDIRVRDEKLKKKDEEIEKLQK 470
Cdd:COG4717 142 AELPERLEELEERLEELRELE--------EELEELEAELAELQEELeELLEQLSLATEEELQDLAEELEELQQRLAELEE 213

                       170       180       190
                ....*....|....*....|....*....|.
gi 25151737 471 DGNRLKSTLQTLEKRVKQLRTEKERDDKEKE 501
Cdd:COG4717 214 ELEEAQEELEELEEELEQLENELEAAALEER 244
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
408-502 7.01e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.77  E-value: 7.01e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 408 LERDQKILKKGTGERNKEFTETIATLRDKLRASETKNAQYRQDIrvrdEKLKKKDEEIEKLQKDGNRLKSTLQTLEKRVK 487
Cdd:COG4717  51 LEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQ----EELEELEEELEELEAELEELREELEKLEKLLQ 126

                        90
                ....*....|....*
gi 25151737 488 QLRTEKERDDKEKEM 502
Cdd:COG4717 127 LLPLYQELEALEAEL 141
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
318-506 7.97e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.68  E-value: 7.97e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737  318 KLEIEIRRHRNLnIQLRDTIAHLdyaeesvhttkRQLEEKISEVNnfkkelIEEFKKCKkgveeefekkfekikedydEL 397
Cdd:PRK03918 484 ELEKVLKKESEL-IKLKELAEQL-----------KELEEKLKKYN------LEELEKKA-------------------EE 526

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737  398 YEKLKRDQRDLERDQKILKKGTgERNKEFTETIATLRDKLRASETKNAQYRQDIRVRD----EKLKKKDEEIEKLQKDGN 473
Cdd:PRK03918 527 YEKLKEKLIKLKGEIKSLKKEL-EKLEELKKKLAELEKKLDELEEELAELLKELEELGfesvEELEERLKELEPFYNEYL 605

                        170       180       190
                 ....*....|....*....|....*....|...
gi 25151737  474 RLKSTLQTLEKRVKQLRTEKERDDKEKEMFAKV 506
Cdd:PRK03918 606 ELKDAEKELEREEKELKKLEEELDKAFEELAET 638
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
317-512 1.08e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 49.29  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737  317 QKLEIEIRRHRNLNIQLRDTIAHLDYAEESVHTTKRQLEEKISEVNNfKKELIEEFKKCKKGVEEEFEKKFEkikedYDE 396
Cdd:PRK03918 289 KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE-KEERLEELKKKLKELEKRLEELEE-----RHE 362

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737  397 LYEKLKRDQRDLERDQKILKKGTGE-----------RNKEFTETIATLRDKLRASETKNAQYRQDIrvrdEKLKK----- 460
Cdd:PRK03918 363 LYEEAKAKKEELERLKKRLTGLTPEklekeleelekAKEEIEEEISKITARIGELKKEIKELKKAI----EELKKakgkc 438

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25151737  461 -----------KDEEIEKLQKDGNRLKSTLQTLEKRVKQLRTEKERDDKEKEMFAKVAMNRKT 512
Cdd:PRK03918 439 pvcgrelteehRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKEL 501
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
393-506 1.16e-05

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: 1.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 393 DYDELYEKLKRDQRDLERdqkiLKkgtgERNKEFTETIATLRDKLRASETK----NAQYRQDIRvRDEKLKKKDEEIEKL 468
Cdd:COG2433 407 ELTEEEEEIRRLEEQVER----LE----AEVEELEAELEEKDERIERLERElseaRSEERREIR-KDREISRLDREIERL 477

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 25151737 469 QKDGNRLKSTLQTLEKRVKQLRTEKERDDKEKEMFAKV 506
Cdd:COG2433 478 ERELEEERERIEELKRKLERLKELWKLEHSGELVPVKV 515
PRK12704 PRK12704
phosphodiesterase; Provisional
 351-494 1.26e-05

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 48.62  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737  351 KRQLEEKISEVNNFKKELIEEFKkckkgveeefekkfekikedydelyEKLKRDQRDLERDQKilkkgtgERNKEFTETi 430
Cdd:PRK12704  41 KRILEEAKKEAEAIKKEALLEAK-------------------------EEIHKLRNEFEKELR-------ERRNELQKL- 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 25151737  431 atlrdklrasETKNAQYRQDIRVRDEKLKKKDEEIEKLQKDGNRLKSTLQTLEKRVKQLRTEKE 494
Cdd:PRK12704  88 ----------EKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQL 141
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
317-501 1.33e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.91  E-value: 1.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737  317 QKLEIEIRRHRNLNIQLRDTIAHLDYAEESVhttkRQLEEKISEVNNFKKELiEEFKKCKKGVEEEFEKKfekikedyDE 396
Cdd:PRK03918 200 KELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKEL-ESLEGSKRKLEEKIREL--------EE 266

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737  397 LYEKLKRDQRDLERDQKILK--KGTGERNKEFTETIATLRDKLRASETKNAQYRQDIRV----------RDEKLKKKDEE 464
Cdd:PRK03918 267 RIEELKKEIEELEEKVKELKelKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGieerikeleeKEERLEELKKK 346

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 25151737  465 IEKLQKDGNRLKSTLQTLEkRVKQLRTEKERDDKEKE 501
Cdd:PRK03918 347 LKELEKRLEELEERHELYE-EAKAKKEELERLKKRLT 382
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
311-495 1.57e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.97  E-value: 1.57e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 311 GSSLDRQKLEIEIRRHRN------LNIQLRDTIAHLDYAEESVHTTKRQLEEKISEVNNFKKELIEEfkkckkgveeefe 384
Cdd:COG4372   5 GEKVGKARLSLFGLRPKTgiliaaLSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQA------------- 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 385 kkfekiKEDYDELYEKLKRDQRDLERDQKILK------KGTGERNKEFTETIATLRDKLRASETKNAQYRQDIRVRDEKL 458
Cdd:COG4372  72 ------RSELEQLEEELEELNEQLQAAQAELAqaqeelESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI 145

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 25151737 459 KKKDEEIEKLQKDGNRLKSTLQTLEKRVKQLRTEKER 495
Cdd:COG4372 146 AEREEELKELEEQLESLQEELAALEQELQALSEAEAE 182
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
395-501 2.22e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 47.59  E-value: 2.22e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 395 DELYEKLKRDQRDLERDQKILKKGTGERnKEFTETIATLRDKLRASETKNAQYRQDIRVRDEKLKKKDEEIEKLQKDGNR 474
Cdd:COG4372  48 EQLREELEQAREELEQLEEELEQARSEL-EQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQD 126

                        90       100
                ....*....|....*....|....*..
gi 25151737 475 LKSTLQTLEKRVKQLRTEKERDDKEKE 501
Cdd:COG4372 127 LEQQRKQLEAQIAELQSEIAEREEELK 153
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
316-519 4.69e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 46.98  E-value: 4.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737  316 RQKLEIEIRRHRNLNiQLRDTIAHLDYAEESVHTTKRQLEEKISEVNNFKKELIEEFKKCKKGVEEEFEKKFEKIK-EDY 394
Cdd:PRK03918 220 REELEKLEKEVKELE-ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEyIKL 298

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737  395 DELYEKLKRDQRDLERD-----------QKILKKGTG--ERNKEFTETIATLRDKLRASETKNAQYrQDIRV---RDEKL 458
Cdd:PRK03918 299 SEFYEEYLDELREIEKRlsrleeeingiEERIKELEEkeERLEELKKKLKELEKRLEELEERHELY-EEAKAkkeELERL 377

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 25151737  459 KKK--DEEIEKLQKDGNRLKSTLQTLEKRVKQLRTEKERDDKEKEMFAKVAMNRKTSNPVPPV 519
Cdd:PRK03918 378 KKRltGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPV 440
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
327-512 2.45e-04

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 43.75  E-value: 2.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 327 RNLNIQLRDTIAHLDYAEESvhttKRQLEEKISEVNNFKKELIEEFKKCKKGVEEEFEKKFEKIKEDYD----------- 395
Cdd:COG1340  46 DELNAQVKELREEAQELREK----RDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGGSidklrkeierl 121

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 396 ---------------ELYEKLKRDQRDLERDQKILKKGtgERNKEFTETIATLRDKLRASETKNAQYRQDIRVRDEKLKK 460
Cdd:COG1340 122 ewrqqtevlspeeekELVEKIKELEKELEKAKKALEKN--EKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIE 199

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 461 KDEEIEKLQKDGNRLKSTLQTLEKRVKQLRTE--------KERDDKEKEMFAKVAMNRKT 512
Cdd:COG1340 200 LYKEADELRKEADELHKEIVEAQEKADELHEEiielqkelRELRKELKKLRKKQRALKRE 259
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 350-501 2.61e-04

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: 44.63  E-value: 2.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737   350 TKRQLEEKISEVNNFKKELIEEfkkcKKGVEEEFEKKFEKIKEDYDELYEKLKRDQRDLERDQKILKKGTGERNK---EF 426
Cdd:TIGR04523 265 IKKQLSEKQKELEQNNKKIKEL----EKQLNQLKSEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKiisQL 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737   427 TETIATLRDKLRASETKNAQYRQDIRVRDEKLKK-------KDEEIEKLQKDGNRLKSTLQTLEKRVKQLRT-----EKE 494
Cdd:TIGR04523 341 NEQISQLKKELTNSESENSEKQRELEEKQNEIEKlkkenqsYKQEIKNLESQINDLESKIQNQEKLNQQKDEqikklQQE 420


                  ....*..
gi 25151737   495 RDDKEKE 501
Cdd:TIGR04523 421 KELLEKE 427
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 314-505 3.17e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 42.99  E-value: 3.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 314 LDRQKLEIEIRRHRNLNIQLRDTIAHLdyaEESVHTTKRQLEEKISEVNNFKKELieefKKCKKgveeefekkfekikeD 393
Cdd:COG1579  10 LDLQELDSELDRLEHRLKELPAELAEL---EDELAALEARLEAAKTELEDLEKEI----KRLEL---------------E 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 394 YDELYEKLKRDQRDLerdqkilkkGTGERNKEF---TETIATLRDKLRASETKnaqyrqdIRVRDEKLKKKDEEIEKLQK 470
Cdd:COG1579  68 IEEVEARIKKYEEQL---------GNVRNNKEYealQKEIESLKRRISDLEDE-------ILELMERIEELEEELAELEA 131

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 25151737 471 DGNRLKSTL----QTLEKRVKQLRTEKERDDKEKEMFAK 505
Cdd:COG1579 132 ELAELEAELeekkAELDEELAELEAELEELEAEREELAA 170
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 314-501 7.23e-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: 43.12  E-value: 7.23e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737    314 LDRQKLEIE--IRRHRNLNIQLRDTIAHLDYAEESVHTTKRQLEEKISEVNNFKKElIEEFKKCKKgveeEFEKKFEKIK 391
Cdd:TIGR02168  241 LEELQEELKeaEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANE-ISRLEQQKQ----ILRERLANLE 315

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737    392 EDYDELYEKLKRDQRDLERDQKILKkgtgeRNKEFTETIATLRDKLRASETKNAQYRQDIRvrdEKLKKKDEEIEKLQKD 471
Cdd:TIGR02168  316 RQLEELEAQLEELESKLDELAEELA-----ELEEKLEELKEELESLEAELEELEAELEELE---SRLEELEEQLETLRSK 387

                          170       180       190
                   ....*....|....*....|....*....|
gi 25151737    472 GNRLKSTLQTLEKRVKQLRTEKERDDKEKE 501
Cdd:TIGR02168  388 VAQLELQIASLNNEIERLEARLERLEDRRE 417
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
312-501 7.87e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 7.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737  312 SSLDRQKLEIEIRRHRNLN---IQLRDTIAHLD---YAEESVHTTKRQLEEKISEVNNFKKELIEEFKKCKKGVEEEFEK 385
Cdd:PRK03918 513 KKYNLEELEKKAEEYEKLKeklIKLKGEIKSLKkelEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEE 592

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737  386 KFEKIKEDYDElYEKLKRDQRDLERDQKILKKgtgERNkEFTETIATLRDKLRASETKNAQYRQ-DIRVRDEKLKKKDEE 464
Cdd:PRK03918 593 RLKELEPFYNE-YLELKDAEKELEREEKELKK---LEE-ELDKAFEELAETEKRLEELRKELEElEKKYSEEEYEELREE 667

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 25151737  465 IEKLQKDGNRLKSTLQTLEKRVKQL--------RTEKERDDKEKE 501
Cdd:PRK03918 668 YLELSRELAGLRAELEELEKRREEIkktleklkEELEEREKAKKE 712
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 435-507 9.25e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.51  E-value: 9.25e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 25151737 435 DKLRASETKNAQYRQDIRVRDEKLKKKDEEIEKLQKDGNRLKSTLQTLEKRVKQLRTE----KERDDKEKEMFAKVA 507
Cdd:COG3883  16 PQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeaEAEIEERREELGERA 92
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 395-489 9.30e-04

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.44  E-value: 9.30e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 395 DELYEKLKRDQRDLERDQKILKKGTGERNKeftetiatLRDKLRASETKNAQYRQDIRVRDEKLKKKDEEIEKLQKDGNR 474
Cdd:COG4942  23 AEAEAELEQLQQEIAELEKELAALKKEEKA--------LLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94

                        90
                ....*....|....*
gi 25151737 475 LKSTLQTLEKRVKQL 489
Cdd:COG4942  95 LRAELEAQKEELAEL 109
BBP1_C pfam15272
Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole ...
 393-499 9.63e-04

Spindle pole body component BBP1, C-terminal; This C-terminal domain of BBP1, a spindle pole body component, carries coiled-coils that are necessary for the localization of BBP1 to the spindle pole body (SPB). Although not a membrane protein itself, BBP1 binds to Mps2 as well as to Spc29 and the half-bridge protein Kar1, thus providing a model for how the SPB core is tethered within the nuclear envelope and to the half-bridge


Pssm-ID: 405864 [Multi-domain]  Cd Length: 183  Bit Score: 40.84  E-value: 9.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737   393 DYDELYEKLKRDQRDLErdqkILKKGTGERNKEFTETIATLRDKLRasETKN---AQYRQDIRVRDE--KLKKKDEEIEK 467
Cdd:pfam15272   5 EYLELLDKLDKNNRALH----LLNKDVRERDEHYQLQETSYKKKYL--QTRNeliNELKQSKKLYDNyyKLYSKYQQLKK 78

                          90       100       110
                  ....*....|....*....|....*....|..
gi 25151737   468 LQKDGNRLKSTLQTLEKRVKQLRTEKERDDKE 499
Cdd:pfam15272  79 ISNESLDLQSTITNLESQLVDQAIDKDREIHN 110
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 317-499 1.23e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 1.23e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 317 QKLEIEIRRHRNLNIQLRDTIAHLDYAEESVHTTKRQLEEKISEVNNFKKELIEEFKKCKKGVEEEFE--KKFEKIKEDY 394
Cdd:COG1196 298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEalLEAEAELAEA 377

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 395 DELYEKLKRDQRDLERDQKILKKgtgeRNKEFTETIATLRDKLRASETKNAQYRQDIRVRDEKLKKKDEEIEKLQKDGNR 474
Cdd:COG1196 378 EEELEELAEELLEALRAAAELAA----QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453

                       170       180
                ....*....|....*....|....*
gi 25151737 475 LKSTLQTLEKRVKQLRTEKERDDKE 499
Cdd:COG1196 454 LEEEEEALLELLAELLEEAALLEAA 478
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 398-502 1.27e-03

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: 42.35  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737    398 YEKLKRDQRDLERDQKILKKgtgernKEFTETIATLRDKLRASETKNAQYRQDIRVRDEKLK-------KKDEEIEKLQK 470
Cdd:TIGR02168  215 YKELKAELRELELALLVLRL------EELREELEELQEELKEAEEELEELTAELQELEEKLEelrlevsELEEEIEELQK 288

                           90       100       110
                   ....*....|....*....|....*....|..
gi 25151737    471 DGNRLKSTLQTLEKRVKQLRTEKERDDKEKEM 502
Cdd:TIGR02168  289 ELYALANEISRLEQQKQILRERLANLERQLEE 320
PRK11281 PRK11281
mechanosensitive channel MscK;
399-492 1.34e-03

mechanosensitive channel MscK;


Pssm-ID: 236892 [Multi-domain]  Cd Length: 1113  Bit Score: 42.59  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737   399 EKLKrDQRDLERDQKILKKgtgernkEFTETIATLrDKLRASETKNAQYRQDIRVRDEKLKKKDEEIEKLQKDGN----- 473
Cdd:PRK11281   46 DALN-KQKLLEAEDKLVQQ-------DLEQTLALL-DKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDeetre 116

                          90       100
                  ....*....|....*....|
gi 25151737   474 RLKS-TLQTLEKRVKQLRTE 492
Cdd:PRK11281  117 TLSTlSLRQLESRLAQTLDQ 136
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 396-501 1.47e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 1.47e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 396 ELYEKLKRDQRDLERDQKILK-KGTGERNKEFTETIATLRDKLRASETKNAQYRQDIRVRDEKLKKKDEEIEKLQKDGNR 474
Cdd:COG1196 213 ERYRELKEELKELEAELLLLKlRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292

                        90       100
                ....*....|....*....|....*..
gi 25151737 475 LKSTLQTLEKRVKQLRTEKERDDKEKE 501
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLE 319
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 313-502 1.54e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.36  E-value: 1.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737    313 SLDRQKLEIEIRRHRNLNIQLRDTIAHLDYAEESVHTTKRQLEEKISEvnnfkkeLIEEFKKCKKGVEEEFEKKFEKIKE 392
Cdd:TIGR02169  722 EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE-------LEEDLHKLEEALNDLEARLSHSRIP 794

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737    393 DYDELYEKLKRDQRDLERDQKILKKGTGER--NKEFTET-IATLRDKLRASETKNAQYRQDIRVRDEKLKKKDEEIEKLQ 469
Cdd:TIGR02169  795 EIQAELSKLEEEVSRIEARLREIEQKLNRLtlEKEYLEKeIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELE 874

                          170       180       190
                   ....*....|....*....|....*....|...
gi 25151737    470 KDgnrlkstLQTLEKRVKQLrtEKERDDKEKEM 502
Cdd:TIGR02169  875 AA-------LRDLESRLGDL--KKERDELEAQL 898
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 316-501 1.77e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.67  E-value: 1.77e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 316 RQKLEIEIRRHRNLNIQLRDTIAHLDYAEESVHTTKRQL---EEKISEVNNFKKELIEEFKKCKKGVEEEFEKKFEKIKE 392
Cdd:COG4942  40 EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELaalEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQ 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 393 DYDELYEKlKRDQRDLERDQKILKKGTGERNKEftetIATLRDKLRASETKNAQYRQDIRVRDEKLKKKDEEIEKLQKDG 472
Cdd:COG4942 120 PPLALLLS-PEDFLDAVRRLQYLKYLAPARREQ----AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALK 194

                       170       180
                ....*....|....*....|....*....
gi 25151737 473 NRLKSTLQTLEKRVKQLRTEKERDDKEKE 501
Cdd:COG4942 195 AERQKLLARLEKELAELAAELAELQQEAE 223
PTZ00121 PTZ00121
MAEBL; Provisional
 344-514 2.01e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.05  E-value: 2.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737   344 EESVHTTKRQLEEKISEVNNFKKEliEEFKKCKKGVEEEFEKKFEKIKEDYDELYEKLKRDQRDLERDQKILKKGTGERN 423
Cdd:PTZ00121 1632 KKKVEQLKKKEAEEKKKAEELKKA--EEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737   424 KEFTETIATlrDKLRASETKNAQYRQDIRVRDEKLKKKDEEIEKLQKDGNRLKSTLQTLEKRVKQLRTEK----ERDDKE 499
Cdd:PTZ00121 1710 KEAEEKKKA--EELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKeaviEEELDE 1787

                         170
                  ....*....|....*
gi 25151737   500 KEMFAKVAMNRKTSN 514
Cdd:PTZ00121 1788 EDEKRRMEVDKKIKD 1802
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 312-505 2.18e-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: 41.54  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737   312 SSLDRQKLEI-----EIRRHRNLNIQLRDTIAHLDYAEESVHTTKRQLEEKISEVNNFKKELIEEFKKCKKGVEEEFEKK 386
Cdd:TIGR04523 482 QNLEQKQKELkskekELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEK 561

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737   387 FEKIkedYDELYEKLKRDQRDLERDQKILKkgtgERNKEFTETIATLRDKLRASETKNAQYRQDIrvrdEKLKKKDEEIE 466
Cdd:TIGR04523 562 EIDE---KNKEIEELKQTQKSLKKKQEEKQ----ELIDQKEKEKKDLIKEIEEKEKKISSLEKEL----EKAKKENEKLS 630

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 25151737   467 KLQKDgnrLKSTLQTLEKRVKQLRTE-KERDDKEKEMFAK 505
Cdd:TIGR04523 631 SIIKN---IKSKKNKLKQEVKQIKETiKEIRNKWPEIIKK 667
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 315-501 3.15e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 3.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 315 DRQKLEIEIRRHRNLNIQLRDTIAHLD----YAEESVHTTKRQLEEKISEVNNFKKELIEEfkkckKGVEEEFEKKFEKI 390
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEaeleELRLELEELELELEEAQAEEYELLAELARL-----EQDIARLEERRREL 314

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 391 KEDYDELYEKLKRDQRDLERDQKILKKGTGERnKEFTETIATLRDKLRASETKNAQYRQDIRVRDEKLKKKDEEIEKLQK 470
Cdd:COG1196 315 EERLEELEEELAELEEELEELEEELEELEEEL-EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393

                       170       180       190
                ....*....|....*....|....*....|.
gi 25151737 471 DGNRLKSTLQTLEKRVKQLRTEKERDDKEKE 501
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERLEEELE 424
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 428-520 4.11e-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: 40.13  E-value: 4.11e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 428 ETIATLRDKLRASETKNAQYRQDIRVRDEKLKKKDEEIEKLQKDGNRLKSTLQTLEKRVKQLRTEKERddkEKEMFAKV- 506
Cdd:COG4942  34 QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA---QKEELAELl 110

                        90
                ....*....|....*
gi 25151737 507 -AMNRKTSNPVPPVL 520
Cdd:COG4942 111 rALYRLGRQPPLALL 125
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
312-495 4.32e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 4.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737  312 SSLDRQKLEI-EIRRHRNLNIQLRDTIAHLDYAEESVHTTKRQLEEKISEVNNFKKElIEEFKKckkgveeefekKFEKI 390
Cdd:PRK03918 585 ESVEELEERLkELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKR-LEELRK-----------ELEEL 652

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737  391 KEDYD-ELYEKLKRDQRDLERDQKILKKGTgERNKEFTETIATLRDKLRAsetknaqyrqdirvRDEKLKKKDEEIEKLQ 469
Cdd:PRK03918 653 EKKYSeEEYEELREEYLELSRELAGLRAEL-EELEKRREEIKKTLEKLKE--------------ELEEREKAKKELEKLE 717

                        170       180
                 ....*....|....*....|....*.
gi 25151737  470 KdgnrLKSTLQTLEKRVKQLRTEKER 495
Cdd:PRK03918 718 K----ALERVEELREKVKKYKALLKE 739
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
316-501 4.61e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 4.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737  316 RQKLEI--EIRRHRNLNIQLRDTIAHLDYAEESVHTTKRQ-----LEEKISEVNNFKKELIEEFKKCKkgveeefekkfe 388
Cdd:COG4913  248 REQIELlePIRELAERYAAARERLAELEYLRAALRLWFAQrrlelLEAELEELRAELARLEAELERLE------------ 315

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737  389 kikedydELYEKLKRDQRDLERDqkILKKGtGERNKEFTETIATLRDKLRASETKNAQYRQDIRVRDEKLKKKDEEIEKL 468
Cdd:COG4913  316 -------ARLDALREELDELEAQ--IRGNG-GDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAAL 385

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 25151737  469 QKDGNRLKSTLQTLEKRVKQLRTE---------KERDDKEKE 501
Cdd:COG4913  386 RAEAAALLEALEEELEALEEALAEaeaalrdlrRELRELEAE 427
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 393-495 4.97e-03

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: 40.43  E-value: 4.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737    393 DYDELYEKLKRDQRDLERDQKILKKGTGERNKE---FTETIATLRDKLRASETKNAQYRQDIRVRDEKLKKKDEEIEKLQ 469
Cdd:TIGR02168  709 ELEEELEQLRKELEELSRQISALRKDLARLEAEveqLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE 788

                           90       100
                   ....*....|....*....|....*.
gi 25151737    470 KDGNRLKSTLQTLEKRVKQLRTEKER 495
Cdd:TIGR02168  789 AQIEQLKEELKALREALDELRAELTL 814
TOPEUc smart00435
DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina ...
 423-508 5.43e-03

DNA Topoisomerase I (eukaryota); DNA Topoisomerase I (eukaryota), DNA topoisomerase V, Vaccina virus topoisomerase, Variola virus topoisomerase, Shope fibroma virus topoisomeras


Pssm-ID: 214661 [Multi-domain]  Cd Length: 391  Bit Score: 40.03  E-value: 5.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737    423 NKEFTETIATLRDKLRASETKNAQYRQDI----RVRDEK--LKKKDE-EIEKLQKDGNRLKSTLQTLEKRVKQL-----R 490
Cdd:smart00435 272 SKTHEKSMEKLQEKIKALKYQLKRLKKMIllfeMISDLKrkLKSKFErDNEKLDAEVKEKKKEKKKEEKKKKQIerleeR 351

                           90
                   ....*....|....*....
gi 25151737    491 TEK-ERDDKEKEMFAKVAM 508
Cdd:smart00435 352 IEKlEVQATDKEENKTVAL 370
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 399-505 5.97e-03

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 38.73  E-value: 5.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737   399 EKLKRDQRDLERDQ----KILKKGTGERNK------EFTETIATLRDKLRASETKNaqyrqdiRVRDEKLKKKDEEIEKL 468
Cdd:pfam15619  28 EELRKENRLLKRLQkrqeKALGKYEGTESElpqliaRHNEEVRVLRERLRRLQEKE-------RDLERKLKEKEAELLRL 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 25151737   469 QKDGNRLKSTLQ--------TLEKRVKQLRTEKERDDKEKEMFAK 505
Cdd:pfam15619 101 RDQLKRLEKLSEdknlaereELQKKLEQLEAKLEDKDEKIQDLER 145
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
349-507 6.06e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.51  E-value: 6.06e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 349 TTKRQLEEKISEVNNFKKELIEEFKKCKKgveeefekkfekikeDYDELYEKLK--RDQRDLERDQKilkkgtgernKEF 426
Cdd:COG1340   1 SKTDELSSSLEELEEKIEELREEIEELKE---------------KRDELNEELKelAEKRDELNAQV----------KEL 55

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 427 TETIATLRDKLRAsetKNAQYRQDIRVRDEKLKKKDE------EIEKLQKDGNRLKSTLQTLEKRVKQLR----TEKERD 496
Cdd:COG1340  56 REEAQELREKRDE---LNEKVKELKEERDELNEKLNElreeldELRKELAELNKAGGSIDKLRKEIERLEwrqqTEVLSP 132

                       170
                ....*....|.
gi 25151737 497 DKEKEMFAKVA 507
Cdd:COG1340 133 EEEKELVEKIK 143
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
314-510 6.39e-03

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


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 39.51  E-value: 6.39e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 314 LDRQKLEIEIRRHRNLNI-QLRDTIAHLDYAEE-SVHTTK--RQLEEKISEvnnfKKELIEEFKKCKKGveeefekkfek 389
Cdd:COG1340  94 LDELRKELAELNKAGGSIdKLRKEIERLEWRQQtEVLSPEeeKELVEKIKE----LEKELEKAKKALEK----------- 158

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 390 iKEDYDELYEKLkRDQRDLERDQKILKKGTGERNKEFTETIATL---RDKLRAsetKNAQYRQDIRVRDEKLKKKDEEIE 466
Cdd:COG1340 159 -NEKLKELRAEL-KELRKEAEEIHKKIKELAEEAQELHEEMIELykeADELRK---EADELHKEIVEAQEKADELHEEII 233

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 25151737 467 KLQKDGNRLKSTLQTLEKRVKQLRTEKERDDKEKEmfAKVAMNR 510
Cdd:COG1340 234 ELQKELRELRKELKKLRKKQRALKREKEKEELEEK--AEEIFEK 275
PTZ00121 PTZ00121
MAEBL; Provisional
 315-511 6.45e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.12  E-value: 6.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737   315 DRQKLEIEIRRHRNLNIQLRDtiahldyAEESVHTTKRQLEEKISEVNNFKKELIEEFKKCKKG------VEEEFEKKFE 388
Cdd:PTZ00121 1562 EKKKAEEAKKAEEDKNMALRK-------AEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkikaeeLKKAEEEKKK 1634

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737   389 KIKEDYDELYEKLKRDQRDLERDQKILKKGTGERNKEftetiatlRDKLRASETKNAQyrQDIRVRDEKLKKKDEEIEKL 468
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAE--------EDKKKAEEAKKAE--EDEKKAAEALKKEAEEAKKA 1704

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 25151737   469 QKdgnrLKSTLQTLEKRVKQLRTEKERDDKEKEMFAKVAMNRK 511
Cdd:PTZ00121 1705 EE----LKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDK 1743
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 404-502 6.91e-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: 39.14  E-value: 6.91e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737 404 DQRDLERDQKILKkgtgeRNKEFTETIATLRDKLRASETKNAQYRQDIRVRDEKLKKKDEEIEKLQKDGNRLKSTLQTLE 483
Cdd:COG1579   5 DLRALLDLQELDS-----ELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYE 79

                        90
                ....*....|....*....
gi 25151737 484 KRVKQLRTEKERDDKEKEM 502
Cdd:COG1579  80 EQLGNVRNNKEYEALQKEI 98
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 314-511 7.92e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.05  E-value: 7.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737    314 LDRQKLEIE----IRRHRNLNIQLRDTIAHLDYAEESVHTTKRQLEEKISEVNNFKKELIEEFKKCKKgveeefekkfek 389
Cdd:TIGR02169  216 LLKEKREYEgyelLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD------------ 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737    390 ikeDYDELYEKLKRDQRDLERDQKILKKgtgernkefteTIATLRDKLRASETKNAQYRQDIRVRDEKLKKKDEEIEKLQ 469
Cdd:TIGR02169  284 ---LGEEEQLRVKEKIGELEAEIASLER-----------SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEER 349

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 25151737    470 KDGNRLKSTLQTLEKRVKQLRTEKERDDKE-KEMFAKVAMNRK 511
Cdd:TIGR02169  350 KRRDKLTEEYAELKEELEDLRAELEEVDKEfAETRDELKDYRE 392
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 312-501 8.06e-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: 39.62  E-value: 8.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737   312 SSLDRQKLEIEiRRHRNLNIQLRDTIAHLDYAEESVHTTKRQLEEKISEVNNFKKELIEEFKKCKKGVEEEFEKKFEKIK 391
Cdd:TIGR04523 127 NKLEKQKKENK-KNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSN 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737   392 ED-YDELYEKLKRDQRDLERDQKILKKGTGERNKEFTETIATLrdklraSETKNaqyrQDIRVRDEKLKKKDEEIEKlQK 470
Cdd:TIGR04523 206 LKkKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEI------SNTQT----QLNQLKDEQNKIKKQLSEK-QK 274

                         170       180       190
                  ....*....|....*....|....*....|.
gi 25151737   471 DGNRLKSTLQTLEKRVKQLRTEKERDDKEKE 501
Cdd:TIGR04523 275 ELEQNNKKIKELEKQLNQLKSEISDLNNQKE 305
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 315-507 9.06e-03

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


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 39.72  E-value: 9.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737   315 DRQKLEIEIRRHRNLnIQLRDTIAHLDYAEES-----VHTTKRQLEEKISEVNNFKKELIEEFKKCKKgveeefekkfek 389
Cdd:pfam05557  17 EKKQMELEHKRARIE-LEKKASALKRQLDRESdrnqeLQKRIRLLEKREAEAEEALREQAELNRLKKK------------ 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737   390 ikedYDELYEKLKRDQRDLERDQKILKKGTGERNKEFTETIATLRDKLRASETKNaqyrQDIRVRDEKLKKKDEEIEKLQ 469
Cdd:pfam05557  84 ----YLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSEL----EELQERLDLLKAKASEAEQLR 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 25151737   470 KDGNRLKSTLQTLEKRVKQL--RTEKERDDKE--KEMFAKVA 507
Cdd:pfam05557 156 QNLEKQQSSLAEAEQRIKELefEIQSQEQDSEivKNSKSELA 197
HSD3 pfam15244
Spermatogenesis-associated protein 7, or HSD3; Spermatogenesis-associated protein HSD3 also ...
 454-558 9.80e-03

Spermatogenesis-associated protein 7, or HSD3; Spermatogenesis-associated protein HSD3 also goes by the name of spermatogenesis-associated protein 7 or SPAT7. The family carries a single transmembrane domain. It functions in several tissues, and is expressed in the developing and mature mouse retina; it is expressed in multiple retinal layers in the adult mouse retina. Mutations lead to LCA disease, or Leber congenital amaurosis, which results in a number of retinal dystrophies. The disease- phenotype is characterized by severe visual loss at birth, nystagmus, a variety of fundus changes, and minimal or absent recordable responses on the electroretinogram (ERG).


Pssm-ID: 464584  Cd Length: 414  Bit Score: 39.01  E-value: 9.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 25151737   454 RDEKLKKKDEEIEK---LQKDG------NRLKSTLQTLEKRVKQLRTEKERDDKEKEMFAKVAmnrKTSNPVPPVLNQSV 524
Cdd:pfam15244  77 RREKLKKELARCEKelkSAKTAsqanskNNSKSLSNTLQKPSGEPQDEDDVLIEEMNEFPSFS---KSRVPSSERLHLSL 153

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 25151737   525 PIS--ITSNGPSRHpSSSSLTTFRKPSTSNRERGVS 558
Cdd:pfam15244 154 PKSsrSLTNGTEKN-SSSSLSSMDSTSSRRRKSGSS 188
 
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